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Conserved domains on  [gi|2462495797|ref|XP_054187456|]
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retinol dehydrogenase 13 isoform X1 [Homo sapiens]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 38-254 1.53e-140

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd09807:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 274  Bit Score: 395.68  E-value: 1.53e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTK 197
Cdd:cd09807    81 LDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLNSE-KSYNTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGsTFSSTTLA 254
Cdd:cd09807   160 FAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHH-LFLSTLLN 215
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 38-254 1.53e-140

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 395.68  E-value: 1.53e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTK 197
Cdd:cd09807    81 LDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLNSE-KSYNTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGsTFSSTTLA 254
Cdd:cd09807   160 FAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHH-LFLSTLLN 215
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 32-242 2.72e-78

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 238.77  E-value: 2.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  32 SKATIP---GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFA 108
Cdd:PRK06197    7 TAADIPdqsGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 109 AKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAH-VAGHIDFDDL 187
Cdd:PRK06197   87 DALRAAYPRIDLLINNAGVMYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHrIRAAIHFDDL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 188 NWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL--HPGVARTELGRHTG 242
Cdd:PRK06197  167 QWE-RRYNRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVaaHPGVSNTELARNLP 222
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 38-240 7.69e-52

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 169.20  E-value: 7.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:COG1028     6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA--GGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyn 195
Cdd:COG1028    84 LDILVNNAGITPPGplEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQ----------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 196 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:COG1028   153 --AAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRA 195
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 39-239 1.23e-33

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 120.80  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL--GGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVMR-CP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqtrKYNT 196
Cdd:pfam00106  79 DILVNNAGITGlGPfSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISS---VAGLV----------PYPG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 197 KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:pfam00106 146 GSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 39-237 3.47e-20

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 86.74  E-value: 3.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEI--NQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVmrCP----HWTTEDGFEMQFGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrk 193
Cdd:TIGR02415  79 DVMVNNAGV--APitpiLEITEEELKKVYNVNVKGvLFGIQAAARQFKKQGHGGKIINAASIAGHEG------------- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 194 YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:TIGR02415 144 NPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPM 187
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 39-129 1.24e-03

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.62  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797   39 KTVIVTGANTGIGKQTALELARRGG-NIILACRDMEKCEAAAKDIRG-ETLNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAElEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80

                           90
                   ....*....|...
gi 2462495797  117 RVDILINNAGVMR 129
Cdd:smart00822  81 PLTGVIHAAGVLD 93
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 38-254 1.53e-140

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 395.68  E-value: 1.53e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTK 197
Cdd:cd09807    81 LDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLNSE-KSYNTG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGsTFSSTTLA 254
Cdd:cd09807   160 FAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHH-LFLSTLLN 215
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 38-248 4.30e-107

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 310.70  E-value: 4.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRK-YNT 196
Cdd:cd05327    81 LDILINNAGIMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDFNDLDLENNKeYSP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 197 KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTF 248
Cdd:cd05327   161 YKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLY 212
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 32-242 2.72e-78

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 238.77  E-value: 2.72e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  32 SKATIP---GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFA 108
Cdd:PRK06197    7 TAADIPdqsGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 109 AKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAH-VAGHIDFDDL 187
Cdd:PRK06197   87 DALRAAYPRIDLLINNAGVMYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHrIRAAIHFDDL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 188 NWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL--HPGVARTELGRHTG 242
Cdd:PRK06197  167 QWE-RRYNRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVaaHPGVSNTELARNLP 222
PRK06196 PRK06196
oxidoreductase; Provisional
 38-240 1.11e-59

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 191.43  E-value: 1.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06196   26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDG------VEVVMLDLADLESVRAFAERFLDSGRR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWqTRKYNTK 197
Cdd:PRK06196  100 IDILINNAGVMACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSPIRWDDPHF-TRGYDKW 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK06196  179 LAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQRH 221
PRK05854 PRK05854
SDR family oxidoreductase;
31-260 3.51e-58

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 187.58  E-value: 3.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIP---GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREF 107
Cdd:PRK05854    4 PLDITVPdlsGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLRALDLSSLASVAAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAGVMRCP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKAsAPSRIINLSSLAHVAGHIDFDD 186
Cdd:PRK05854   84 GEQLRAEGRPIHLLINNAGVMTPPeRQTTADGFELQFGTNHLGHFALTAHLLPLLRA-GRARVTSQSSIAARRGAINWDD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 187 LNWQtRKYNTKAAYCQSKLAIVLFTKELSRR--LQGSGVTVNALHPGVARTELgrhtgihgstfssttLASKPQTG 260
Cdd:PRK05854  163 LNWE-RSYAGMRAYSQSKIAVGLFALELDRRsrAAGWGITSNLAHPGVAPTNL---------------LAARPEVG 222
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 38-240 7.69e-52

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 169.20  E-value: 7.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:COG1028     6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA--GGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyn 195
Cdd:COG1028    84 LDILVNNAGITPPGplEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQ----------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 196 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:COG1028   153 --AAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRA 195
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 38-231 5.22e-51

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 168.54  E-value: 5.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAH-------VAGHIDFDDLNWQ 190
Cdd:cd09809    81 LHVLVCNAAVFALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSESHrftdlpdSCGNLDFSLLSPP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 191 TRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd09809   161 KKKYWSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 41-244 3.22e-47

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 157.06  E-value: 3.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKdirGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA---IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHidfddlnwqtRKYNTKA 198
Cdd:cd05233    78 LVNNAGIARPgpLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISS---VAGL----------RPLPGQA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 199 AYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIH 244
Cdd:cd05233   145 AYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPE 190
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
35-251 9.13e-46

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 153.87  E-value: 9.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEE 114
Cdd:COG0300     2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEV--VALDVTDPDAVAALAEAVLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtr 192
Cdd:COG0300    80 FGPIDVLVNNAGVGGGgpFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGM-------- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFSST 251
Cdd:COG0300   152 -----AAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLS 205
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 39-240 9.70e-44

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 150.36  E-value: 9.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGG-NIILACRDMEKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09810     2 GTVVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSV--LHCDLASLDSVRQFVDNFRRTGRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM----RCPHWTtEDGFEMQFGVNHLGHFLLTNLLLDKLKAS--APSRIINLSSLAH----VAGHID---- 183
Cdd:cd09810    80 LDALVCNAAVYlptaKEPRFT-ADGFELTVGVNHLGHFLLTNLLLEDLQRSenASPRIVIVGSITHnpntLAGNVPprat 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 184 ----------FDDLNWQT--RKYNTKAAYCQSKLAIVLFTKELSRRL-QGSGVTVNALHPG-VARTELGRH 240
Cdd:cd09810   159 lgdleglaggLKGFNSMIdgGEFEGAKAYKDSKVCNMLTTYELHRRLhEETGITFNSLYPGcIAETGLFRE 229
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 35-240 4.01e-42

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 144.17  E-value: 4.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLnhhvnARHLDLASLKSIREFAAKIIEE 114
Cdd:COG4221     2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRAL-----AVPLDVTDEAAVEAAVAAAVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtr 192
Cdd:COG4221    77 FGRLDVLVNNAGVALLGPLeeLDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISS---IAGLRPYPGG----- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:COG4221   149 -----AVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDS 191
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
39-241 2.34e-39

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 139.36  E-value: 2.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKD--IRGETLNHhvnaRHLDLASLKSIREFAAKIIEEEE 116
Cdd:COG5748     7 STVIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQElgIPPDSYTI----IHIDLASLESVRRFVADFRALGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGV----MRCPHWtTEDGFEMQFGVNHLGHFLLTNLLLDKLKAS--APSRIINLSSLAH----VAGHI---- 182
Cdd:COG5748    83 PLDALVCNAAVyyplLKEPLR-SPDGYELSVATNHLGHFLLCNLLLEDLKKSpaSDPRLVILGTVTAnpkeLGGKIpipa 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462495797 183 --DFDDLNW------------QTRKYNTKAAYCQSKLAIVLFTKELSRRL-QGSGVTVNALHPG-VARTELGRHT 241
Cdd:COG5748   162 ppDLGDLEGfeagfkapismiDGKKFKPGKAYKDSKLCNVLTMRELHRRYhESTGIVFSSLYPGcVADTPLFRNH 236
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 39-242 3.96e-37

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 130.82  E-value: 3.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGN-IILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKLRAEGLS--VRFHQLDVTDDASIEAAADFVEEKYGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMR---CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLahvAGHIdfddlnwqtrky 194
Cdd:cd05324    79 LDILVNNAGIAFkgfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSG---LGSL------------ 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462495797 195 ntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTG 242
Cdd:cd05324   144 --TSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKA 189
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 38-235 3.21e-34

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 123.86  E-value: 3.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09808     1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRKYNTK 197
Cdd:cd09808    81 LHVLINNAGCMVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVQKLNTNNLQSERTAFDGT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRlqGSGVTVNALHPGVART 235
Cdd:cd09808   161 MVYAQNKRQQVIMTEQWAKK--HPEIHFSVMHPGWADT 196
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 39-239 1.23e-33

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 120.80  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL--GGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVMR-CP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqtrKYNT 196
Cdd:pfam00106  79 DILVNNAGITGlGPfSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISS---VAGLV----------PYPG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 197 KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:pfam00106 146 GSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
PLN00015 PLN00015
protochlorophyllide reductase
 42-243 1.93e-30

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 115.19  E-value: 1.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  42 IVTGANTGIGKQTALELARRGG-NIILACRDMEKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:PLN00015    1 IITGASSGLGLATAKALAETGKwHVVMACRDFLKAERAAKSAGMPKDSYTV--MHLDLASLDSVRQFVDNFRRSGRPLDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGVM----RCPHWTtEDGFEMQFGVNHLGHFLLTNLLLDKLKAS-APSR--II-------------------NLSS 174
Cdd:PLN00015   79 LVCNAAVYlptaKEPTFT-ADGFELSVGTNHLGHFLLSRLLLDDLKKSdYPSKrlIIvgsitgntntlagnvppkaNLGD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 175 LAHVAGhiDFDDLNWQT----RKYNTKAAYCQSKLAIVLFTKELSRRLQGS-GVTVNALHPG-VARTELGR-HTGI 243
Cdd:PLN00015  158 LRGLAG--GLNGLNSSAmidgGEFDGAKAYKDSKVCNMLTMQEFHRRYHEEtGITFASLYPGcIATTGLFReHIPL 231
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 39-237 8.49e-29

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 109.17  E-value: 8.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEERV 118
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALE--ADVSDREAVEALVEKVEAEFGPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVmrcphwtTEDGFEMQF---------GVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnw 189
Cdd:cd05333    79 DILVNNAGI-------TRDNLLMRMseedwdaviNVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPG------ 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462495797 190 qtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05333   146 -------QANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 41-249 9.66e-28

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 106.23  E-value: 9.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILA-CRDMEkceaAAKDIRGETLNHH-VNARHLDLASL--KSIREFAAKIieEEE 116
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIAtCRDPS----AATELAALGASHSrLHILELDVTDEiaESAEAVAERL--GDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVM---RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAhvaGHI-DFDDLNWqtr 192
Cdd:cd05325    75 GLDVLINNAGILhsyGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRV---GSIgDNTSGGW--- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFS 249
Cdd:cd05325   149 -----YSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKGPIT 200
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 38-237 1.79e-27

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 106.05  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRdmeKCEAAAKDIRGETLNHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:PRK05557    5 GKVALVTGASRGIGRAIAERLAAQGANVVINYA---SSEAGAEALVAEIGALGGKALAVqgDVSDAESVERAVDEAKAEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRcphWT-----TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwq 190
Cdd:PRK05557   82 GGVDILVNNAGITR---DNllmrmKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNP-------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 191 trkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK05557  151 -----GQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
FabG-like PRK07231
SDR family oxidoreductase;
38-237 1.98e-27

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 106.07  E-value: 1.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAakiIEEEER 117
Cdd:PRK07231    5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAIAVAADVSDEADVEAAVAAA---LERFGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP---HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLNWqtrky 194
Cdd:PRK07231   82 VDILVNNAGTTHRNgplLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVAS---TAGLRPRPGLGW----- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 ntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK07231  154 -----YNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGL 191
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 39-236 2.51e-27

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 105.78  E-value: 2.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirgetlnHHVNARH--LDLASLKSIREFAAKIIEEEE 116
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGEL-------LNDNLEVleLDVTDEESIKAAVKEVIERFG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVM-RCP-HWTTEDGFEMQFGVNHLGHflltnllLDKLKASAP-------SRIINLSSLAHVAGHidfddl 187
Cdd:cd05374    74 RIDVLVNNAGYGlFGPlEETSIEEVRELFEVNVFGP-------LRVTRAFLPlmrkqgsGRIVNVSSVAGLVPT------ 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 188 nwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd05374   141 -------PFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTG 182
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 37-237 9.80e-27

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 104.28  E-value: 9.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK12939    6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA--GGRAHAIAADLADPASVQRFFDAAAAALG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahvaghidfDDLNWQTRKY 194
Cdd:PRK12939   84 GLDGLVNNAGITNSKSATelDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLAS----------DTALWGAPKL 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12939  154 ---GAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
PRK12826 PRK12826
SDR family oxidoreductase;
38-236 2.61e-26

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 103.07  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12826    6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGK--ARARQVDVRDRAALKAAVAAGVEDFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV-MRCPHW-TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGhidfddlnwQTRKYN 195
Cdd:PRK12826   84 LDILVANAGIfPLTPFAeMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSS---VAG---------PRVGYP 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK12826  152 GLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTP 192
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
38-242 3.51e-26

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 102.55  E-value: 3.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK05653    5 GKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRA--AGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMR---CPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrky 194
Cdd:PRK05653   83 LDILVNNAGITRdalLPRMSEED-WDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQ---------- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTG 242
Cdd:PRK05653  152 ---TNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLP 196
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-236 3.54e-26

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 102.64  E-value: 3.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACR-DMEKCEAAAKDIRGetlnHHVNAR--HLDLASLKSIREFAAKI 111
Cdd:PRK12825    3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEA----LGRRAQavQADVTDKAALEAAVAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 112 IEEEERVDILINNAGVM-RCPHW-TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnW 189
Cdd:PRK12825   79 VERFGRIDILVNNAGIFeDKPLAdMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPG--------W 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 190 QTRkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK12825  151 PGR-----SNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTD 192
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 38-239 4.47e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 99.73  E-value: 4.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06841   15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGG-----NAKGLVCDVSDSQSVEAAVAAVISAFGR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhIDfddlnwqtrkyn 195
Cdd:PRK06841   90 IDILVNSAGVALLapAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVA-LE------------ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK06841  157 RHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGK 200
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
37-237 2.20e-24

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 97.91  E-value: 2.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCeaaAKDIRGE--TLNHHVNARHLDLASLKSIREFAAKIIEE 114
Cdd:PRK12824    1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDC---AKDWFEEygFTEDQVRLKELDVTDTEECAEALAEIEEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwqtr 192
Cdd:PRK12824   78 EGPVDILVNNAGITRDSvfKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQF---------- 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 193 kynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12824  148 ---GQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPM 189
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 36-242 1.22e-23

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 95.55  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGG-NIILACRDMekceAAAKDIRGETLNHhVNARHLDLASLKSIREFAAKIIEe 114
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDP----GSAAHLVAKYGDK-VVPLRLDVTDPESIKAAAAQAKD- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 eerVDILINNAGVMRcPHWTTEDGF----EMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVaghidfddlnwq 190
Cdd:cd05354    75 ---VDVVINNAGVLK-PATLLEEGAlealKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASL------------ 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 191 tRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTG 242
Cdd:cd05354   139 -KNFPAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAG 189
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 38-237 1.85e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 95.72  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12429    4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA--GGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAG---VMRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrky 194
Cdd:PRK12429   82 VDILVNNAGiqhVAPIEDFPTEK-WKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMAS---VHGLVGSAG-------- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 ntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12429  150 --KAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPL 190
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
38-237 6.74e-23

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 94.10  E-value: 6.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDmEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08226    6 GKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGR--GHRCTAVVADVRDPASVAAAIKRAKEKEGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrkyn 195
Cdd:PRK08226   83 IDILVNNAGVCRLGSFldMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSS---VTGDMVADP--------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK08226  151 GETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 38-237 7.88e-23

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 94.05  E-value: 7.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlnHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:cd08940     2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAK--HGVKVLYHgaDLSKPAAIEDMVAYAQRQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwqtrk 193
Cdd:cd08940    80 GGVDILVNNAGIQHVAPIEDfpTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASAN---------- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 194 yntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd08940   150 ---KSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPL 190
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 38-244 1.22e-22

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 92.92  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:COG3967     5 GNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPG------LHTIVLDVADPASIAALAEQVTAEFPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGF------EMQfgVNHLG----------HFlltnllldklKASAPSRIINLSS-LAHVAG 180
Cdd:COG3967    79 LNVLINNAGIMRAEDLLDEAEDladaerEIT--TNLLGpirltaaflpHL----------KAQPEAAIVNVSSgLAFVPL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 181 HIdfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIH 244
Cdd:COG3967   147 AV--------------TPTYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGD 196
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 38-237 3.70e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 91.70  E-value: 3.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhvnarhLDLASLKSIREFAAkiieEEER 117
Cdd:PRK07060    9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLR-------LDVGDDAAIRAALA----AAGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAG--VMRCPHWTTEDGFEMQFGVNHLGHFlltnlllDKLKASAPSR--------IINLSSlahVAGHIDFDDL 187
Cdd:PRK07060   78 FDGLVNCAGiaSLESALDMTAEGFDRVMAVNARGAA-------LVARHVARAMiaagrggsIVNVSS---QAALVGLPDH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 188 nwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK07060  148 ----------LAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 39-236 4.69e-22

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 91.57  E-value: 4.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPV-KVLPLQLDVSDRESIEAALENLPEEFRDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGV---MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHidfddlnwqtRKYN 195
Cdd:cd05346    80 DILVNNAGLalgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGS---IAGR----------YPYA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd05346   147 GGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 36-245 9.61e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 91.16  E-value: 9.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK07825    3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGL------VVGGPLDVTDPASFAAFLDAVEADL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGhflltnlLLDKLKASAP---SR----IINLSSLAhvaGHIDFDD 186
Cdd:PRK07825   77 GPIDVLVNNAGVMPVGPFldEPDAVTRRILDVNVYG-------VILGSKLAAPrmvPRgrghVVNVASLA---GKIPVPG 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462495797 187 LnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHG 245
Cdd:PRK07825  147 M----------ATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGAK 195
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 38-243 1.04e-21

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 90.93  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLN-HHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:cd05364     3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSeKKILLVVADLTEEEGQDRIISTTLAKFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCPHWTTED--GFEMQFGVNHLGHFLLTNLLLDKLKASAPSrIINLSSlahVAGHIDFDDLnwqtrky 194
Cdd:cd05364    83 RLDILVNNAGILAKGGGEDQDieEYDKVMNLNLRAVIYLTKLAVPHLIKTKGE-IVNVSS---VAGGRSFPGV------- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGI 243
Cdd:cd05364   152 ---LYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGM 197
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 38-231 1.07e-21

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 90.62  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR--GETLNHHVnarhlDLASLKSIREFAAKIIEEE 115
Cdd:cd08942     6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSayGECIAIPA-----DLSSEEGIEALVARVAERS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMrcphWTT------EDGFEMQFGVNHLGHFLLTNLLLDKLKASA----PSRIINLSSLAHVAGhidfd 185
Cdd:cd08942    81 DRLDVLVNNAGAT----WGApleafpESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenPARVINIGSIAGIVV----- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 186 dlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd08942   152 -------SGLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 37-238 1.62e-21

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 90.63  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhhvnARHL---DLASLKSIREFAAKIiE 113
Cdd:cd08951     6 PMKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPG--------AAGVligDLSSLAETRKLADQV-N 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVMRCPH-WTTEDGFEMQFGVNHLGHFLLTNllldklKASAPSRIINLSSLAHVAGHIDFDDLNWQTR 192
Cdd:cd08951    77 AIGRFDAVIHNAGILSGPNrKTPDTGIPAMVAVNVLAPYVLTA------LIRRPKRLIYLSSGMHRGGNASLDDIDWFNR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 193 KYNTKAAYCQSKLAIVLFTKELSRRLQgsGVTVNALHPGVARTELG 238
Cdd:cd08951   151 GENDSPAYSDSKLHVLTLAAAVARRWK--DVSSNAVHPGWVPTKMG 194
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 38-240 2.04e-21

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 89.90  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd08934     3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAE--GGKALVLELDVTDEQQVDAAVERTVEALGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQ--FGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqtrKYN 195
Cdd:cd08934    81 LDILVNNAGIMLLGPVEDADTTDWTrmIDTNLLGLMYTTHAALPHHLLRNKGTIVNISS---VAGRV----------AVR 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:cd08934   148 NSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDH 192
PRK06949 PRK06949
SDR family oxidoreductase;
38-240 2.11e-21

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 90.21  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06949    9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVS--LDVTDYQSIKAAVAHAETEAGT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV---MRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASA--------PSRIINLSSLA--HVAGHIdf 184
Cdd:PRK06949   87 IDILVNNSGVsttQKLVDVTPAD-FDFVFDTNTRGAFFVAQEVAKRMIARAkgagntkpGGRIINIASVAglRVLPQI-- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 185 ddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK06949  164 -------------GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHH 206
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 36-241 2.42e-21

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 89.95  E-value: 2.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR--GETLNHHVnarHLDLASLKSIREFAAKIIE 113
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLelGAPSPHVV---PLDMSDLEDAEQVVEEALK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGV-MRCP-HWTTEDGFEMQFGVNHLGhflltnlLLDKLKASAPS-------RIINLSSlahVAGHIdf 184
Cdd:cd05332    78 LFGGLDILINNAGIsMRSLfHDTSIDVDRKIMEVNYFG-------PVALTKAALPHliersqgSIVVVSS---IAGKI-- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 185 ddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 241
Cdd:cd05332   146 --------GVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNA 194
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 37-236 2.97e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 89.73  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlnhhVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK12829   10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAK----VTATVADVADPAQVERVFDTAVERFG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRcPHWTTEDGFEMQF----GVNHLGHFLLTNLLLDKLKASAPSR-IINLSSLAHVAGhidfddlnwqt 191
Cdd:PRK12829   86 GLDVLVNNAGIAG-PTGGIDEITPEQWeqtlAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLG----------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 192 rkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK12829  154 --YPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGP 196
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 39-237 3.82e-21

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 90.14  E-value: 3.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIG-----KQTALELARRGGNIILACRDMEKCEAAAKDIrgetLNHHVNAR------HLDLASLKSIREF 107
Cdd:cd08941     2 KVVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRAL----LASHPDARvvfdyvLVDLSNMVSVFAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAGVMRCP--HWT---------------------------------TEDGFEMQFGVNHLGHFL 152
Cdd:cd08941    78 AKELKKRYPRLDYLYLNAGIMPNPgiDWIgaikevltnplfavtnptykiqaegllsqgdkaTEDGLGEVFQTNVFGHYY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 153 LTNLLLDKLKASA-PSRIINLSSLAHVAGHIDFDDlnWQTRkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd08941   158 LIRELEPLLCRSDgGSQIIWTSSLNASPKYFSLED--IQHL--KGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPG 233


                  ....*.
gi 2462495797 232 VARTEL 237
Cdd:cd08941   234 ICTTNL 239
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 38-236 5.83e-21

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 88.46  E-value: 5.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARH--LDLASLKSIREFAAKIIEEE 115
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGQKVSYisADLSDYEEVEQAFAQAVEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrk 193
Cdd:cd08939    81 GPPDLVVNCAGISIPGLFEdlTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGY--------- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 194 yntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd08939   152 ----SAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 38-242 1.41e-20

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 87.80  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05347     5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVE--ATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwqtrkyn 195
Cdd:cd05347    83 IDILVNNAGIIRRHPAeeFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGP------------- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTG 242
Cdd:cd05347   150 PVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVV 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 37-237 1.47e-20

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 87.82  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEK-CEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:cd05366     1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEaAKSTIQEI--SEAGYNAVAVGADVTDKDDVEALIDQAVEKF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtr 192
Cdd:cd05366    79 GSFDVMVNNAGIAPITPLltITEEDLKKVYAVNVFGvLFGIQAAARQFKKLGHGGKIINASS---IAGVQGFPNL----- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05366   151 -----GAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
38-236 1.72e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 87.78  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgetlnHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07067    6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIG-----PAAIAVSLDVTRQDSIDRIVAAAVERFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGH-FLLTNLLLDKLKASAPSRIINLSSLAhvaghidfddlnwQTRKY 194
Cdd:PRK07067   81 IDILFNNAALfdMAPILDISRDSYDRLFAVNVKGLfFLMQAVARHMVEQGRGGKIINMASQA-------------GRRGE 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 195 NTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK07067  148 ALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTP 189
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 36-237 2.26e-20

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 86.95  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILA-CRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEE 114
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAA--GGKAIAVQADVSDPSQVARLFDAAEKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTnllldklKASAP-----SRIINLSSLAHVAGHIDFddl 187
Cdd:cd05362    79 FGGVDILVNNAGVMLKKPIaeTSEEEFDRMFTVNTKGAFFVL-------QEAAKrlrdgGRIINISSSLTAAYTPNY--- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 188 nwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05362   149 ----------GAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 41-240 2.27e-20

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 86.67  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgeTLNHHVNARHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:cd05360     3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVR--ELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddLNWQtrkyntkA 198
Cdd:cd05360    81 WVNNAGVAVFGRFedVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRS------APLQ-------A 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 199 AYCQSKLAIVLFTKELSRRLQ--GSGVTVNALHPGV--------ARTELGRH 240
Cdd:cd05360   148 AYSASKHAVRGFTESLRAELAhdGAPISVTLVQPTAmntpffghARSYMGKK 199
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 39-237 3.47e-20

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 86.74  E-value: 3.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEI--NQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVmrCP----HWTTEDGFEMQFGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrk 193
Cdd:TIGR02415  79 DVMVNNAGV--APitpiLEITEEELKKVYNVNVKGvLFGIQAAARQFKKQGHGGKIINAASIAGHEG------------- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 194 YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:TIGR02415 144 NPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPM 187
PRK06484 PRK06484
short chain dehydrogenase; Validated
 37-237 5.02e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.14  E-value: 5.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAaakdiRGETLNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARE-----RADSLGPDHHALAMDVSDEAQIREGFEQLHREFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGV----MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAP-SRIINLSSLAHVAGHidfddlnwqt 191
Cdd:PRK06484   79 RIDVLVNNAGVtdptMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHgAAIVNVASGAGLVAL---------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 192 rkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06484  149 ---PKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 38-231 6.44e-20

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 85.79  E-value: 6.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAG--VLAVVADLTDPEDIDRLVEKAGDAFGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNwqtrkyn 195
Cdd:cd05344    79 VDILVNNAGGPPPgpFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSN------- 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462495797 196 tkaaycQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd05344   152 ------VARAGLIGLVKTLSRELAPDGVTVNSVLPG 181
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 38-231 7.53e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 85.77  E-value: 7.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARhlDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08213   12 GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAA--DVADEADIERLAEETLERFGH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMrcphW--TTED----GFEMQFGVNHLGHF-LLTNLLLDKLKASAPSRIINLSSLAHVAGHiDFDDLNwq 190
Cdd:PRK08213   90 VDILVNNAGAT----WgaPAEDhpveAWDKVMNLNVRGLFlLSQAVAKRSMIPRGYGRIINVASVAGLGGN-PPEVMD-- 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 191 TRKYNTkaaycqSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK08213  163 TIAYNT------SKGAVINFTRALAAEWGPHGIRVNAIAPG 197
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 40-244 8.58e-20

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 85.37  E-value: 8.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIEEEERVD 119
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVH--YYKCDVSKREEVYEAAKKIKKEVGDVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 120 ILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFlltnlllDKLKASAPSR-------IINLSSlahVAGHIDFDDLnwq 190
Cdd:cd05339    79 ILINNAGVVSGKKLleLPDEEIEKTFEVNTLAHF-------WTTKAFLPDMlernhghIVTIAS---VAGLISPAGL--- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 191 trkyntkAAYCQSKLAIVLFTKELS---RRLQGSGVTVNALHPGVARTELGRHTGIH 244
Cdd:cd05339   146 -------ADYCASKAAAVGFHESLRlelKAYGKPGIKTTLVCPYFINTGMFQGVKTP 195
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 36-239 8.87e-20

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 85.97  E-value: 8.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR---GETLNHHVNArhLDLASLKSIREfaaKII 112
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITalgGRAIALAADV--LDRASLERARE---EIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 113 EEEERVDILINNAGVMRcPHWTTED-----------------GFEMQFGVNHLGHFLLTNL-LLDKLKASAPSrIINLSS 174
Cdd:cd08935    78 AQFGTVDILINGAGGNH-PDATTDPehyepeteqnffdldeeGWEFVFDLNLNGSFLPSQVfGKDMLEQKGGS-IINISS 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 175 LahvAGHIDFddlnwqtrkynTK-AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:cd08935   156 M---NAFSPL-----------TKvPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNR 207
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 36-239 9.20e-20

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 85.05  E-value: 9.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:cd05370     3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN------IHTIVLDVGDAESVEALAEALLSEY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRcPH-----WTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS-LAHVAghidfddlnw 189
Cdd:cd05370    77 PNLDILINNAGIQR-PIdlrdpASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSgLAFVP---------- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 190 qtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:cd05370   146 ----MAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHE 191
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 49-239 9.60e-20

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 85.17  E-value: 9.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  49 GIGKQTALELARRGGNIILACRDmekcEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVm 128
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLN----EALAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGF- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 129 rCPHW------TTEDGFEMQFGVNHLGHFLLTnllldklKASAP-----SRIINLSSlahVAGHIDFDDLNWqtrkyntk 197
Cdd:pfam13561  82 -APKLkgpfldTSREDFDRALDVNLYSLFLLA-------KAALPlmkegGSIVNLSS---IGAERVVPNYNA-------- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 198 aaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:pfam13561 143 --YGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAAS 182
PRK12743 PRK12743
SDR family oxidoreductase;
39-231 1.01e-19

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 85.47  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNI-ILACRDMEKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSHGVRAEI--RQLDLSDLPEGAQALDKLIQRLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMrcphwTTEDGFEMQF-------GVNHLGHF-LLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnw 189
Cdd:PRK12743   81 IDVLVNNAGAM-----TKAPFLDMDFdewrkifTVDVDGAFlCSQIAARHMVKQGQGGRIINITS---VHEHTPLPG--- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 190 qtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK12743  150 -------ASAYTAAKHALGGLTKAMALELVEHGILVNAVAPG 184
PRK06914 PRK06914
SDR family oxidoreductase;
38-235 1.02e-19

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 85.85  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFaAKIIEEEER 117
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIHNF-QLVLKEIGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAG------VMRCPhwttEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqt 191
Cdd:PRK06914   82 IDLLVNNAGyanggfVEEIP----VEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISS---ISGRVGFPGL---- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 192 rkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK06914  151 ------SPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
PRK05855 PRK05855
SDR family oxidoreductase;
6-245 1.29e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 87.73  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797   6 LPLSALGTVAGAAVLLKDYVTGGAcPSKA-----------TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEK 74
Cdd:PRK05855  273 LPMSHPQVLAAAVAEFVDAVEGGP-PARAllrarvgrprgPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  75 CEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-MRCPHW-TTEDGFEMQFGVNHLG--H 150
Cdd:PRK05855  352 AERTAELIRAAGAVAH--AYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGIgMAGGFLdTSAEDWDRVLDVNLWGviH 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 151 ----FlltnlLLDKLKASAPSRIINLSSLAHVAghidfddlnwQTRKYNtkaAYCQSKLAIVLFTKELSRRLQGSGVTVN 226
Cdd:PRK05855  430 gcrlF-----GRQMVERGTGGHIVNVASAAAYA----------PSRSLP---AYATSKAAVLMLSECLRAELAAAGIGVT 491

                         250
                  ....*....|....*....
gi 2462495797 227 ALHPGVARTELGRHTGIHG 245
Cdd:PRK05855  492 AICPGFVDTNIVATTRFAG 510
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 38-237 3.38e-19

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 83.97  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRD----MEKCEAAAKDIRGETLNHHVnarhlDLASLKSIREFAAKIIE 113
Cdd:cd05358     3 GKVALVTGASSGIGKAIAIRLATAGANVVVNYRSkedaAEEVVEEIKAVGGKAIAVQA-----DVSKEEDVVALFQSAIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS-RIINLSSLAHV---AGHidfddl 187
Cdd:cd05358    78 EFGTLDILVNNAGLQgdASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKgKIINMSSVHEKipwPGH------ 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 188 nwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05358   152 ----------VNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPI 191
PRK06181 PRK06181
SDR family oxidoreductase;
38-237 3.51e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 84.26  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgetlNHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELA----DHGGEALVVptDVSDAEACERLIEAAVARF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGV-MRCPHWTTED--GFEMQFGVNHLGHFLLTNLLLDKLKASApSRIINLSSLAHVAGhidfddlnwqtr 192
Cdd:PRK06181   77 GGIDILVNNAGItMWSRFDELTDlsVFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTG------------ 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 193 kYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06181  144 -VPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDI 187
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 37-239 4.04e-19

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 83.78  E-value: 4.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIIlacrdmekceaaAKDIRGETLNH-HVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK08220    7 SGKTVWVTGAAQGIGYAVALAFVEAGAKVI------------GFDQAFLTQEDyPFATFVLDVSDAAAVAQVCQRLLAET 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS-LAHVAghidfddlnwqtR 192
Cdd:PRK08220   75 GPLDVLVNAAGILRMgaTDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSnAAHVP------------R 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 193 KynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK08220  143 I--GMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQR 187
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 36-243 6.88e-19

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 82.81  E-value: 6.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEV--EAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrk 193
Cdd:PRK07666   83 GSIDILINNAGISKFGKFLelDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKG------------- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 194 YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGI 243
Cdd:PRK07666  150 AAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGL 199
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 38-235 9.19e-19

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 82.52  E-value: 9.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKdirgetlNHHVNARHLDLASLKSIREFAAkiieEEER 117
Cdd:cd05368     2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER-------GPGITTRVLDVTDKEQVAALAK----EEGR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVmrCPHWT----TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrk 193
Cdd:cd05368    71 IDVLFNCAGF--VHHGSildcEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSS---VASSIKGVP------- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 194 ynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:cd05368   139 --NRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDT 178
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-239 9.96e-19

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 82.58  E-value: 9.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILAC-RDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK05565    5 GKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEE--GGDAIAVKADVSSEEDVENLVEQIVEKFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLahvaghidfddlnW-QTRK 193
Cdd:PRK05565   83 KIDILVNNAGISNFGLVTdmTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSI-------------WgLIGA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 194 YNTkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK05565  150 SCE-VLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
38-236 2.10e-18

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 82.09  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEkCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06935   15 GKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTN-WDETRRLI--EKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM-RCP--HWTTED-GFEMQFGVNHLGHFLLTNLLLDKLKASApsRIINLSSLahvaghidfddLNWQTRK 193
Cdd:PRK06935   92 IDILVNNAGTIrRAPllEYKDEDwNAVMDINLNSVYHLSQAVAKVMAKQGSG--KIINIASM-----------LSFQGGK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 194 YntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK06935  159 F--VPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 38-240 2.11e-18

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 81.99  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05352     8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKY-GVKTKAYKCDVSSQESVEKTFKQIQKDFGK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLNWqtrkyn 195
Cdd:cd05352    87 IDILIANAGITVHKPALdyTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITAS---MSGTIVNRPQPQ------ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 196 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:cd05352   158 --AAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDF 200
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 39-237 2.45e-18

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 81.58  E-value: 2.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirgeTLNHHVNARHL--DLASLKSIREFAAKIIEEEE 116
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQ----AINPKVKATFVqcDVTSWEQLAAAFKKAIEKFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRcPHWTTEDGFEMQ-----FGVNHLGHFLLTNLLLDKLKASAP---SRIINLSSLAHVAGHIDFddln 188
Cdd:cd05323    77 RVDILINNAGILD-EKSYLFAGKLPPpwektIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQF---- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 189 wqtrkyntkAAYCQSKLAIVLFTKEL-SRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05323   152 ---------PVYSASKHGVVGFTRSLaDLLEYKTGVRVNAICPGFTNTPL 192
PRK09242 PRK09242
SDR family oxidoreductase;
35-237 2.67e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 81.72  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEE 114
Cdd:PRK09242    6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAG--VMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFddlnwqtr 192
Cdd:PRK09242   86 WDGLHILVNNAGgnIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGS---VSGLTHV-------- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 193 kyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK09242  155 --RSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPL 197
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 38-237 2.99e-18

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 81.38  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd08944     3 GKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAG-----GALALRVDVTDEQQVAALFERAVEEFGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHW---TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwqtrky 194
Cdd:cd08944    78 LDLLVNNAGAMHLTPAiidTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDP------------ 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 nTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd08944   146 -GYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPL 187
PRK07454 PRK07454
SDR family oxidoreductase;
39-237 3.02e-18

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 81.16  E-value: 3.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgeTLNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELR--STGVKAAAYSIDLSNPEAIAPGIAELLEQFGCP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVMRcphwtTEDGFEMQFG-------VNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnWqt 191
Cdd:PRK07454   85 DVLINNAGMAY-----TGPLLEMPLSdwqwviqLNLTSVFQCCSAVLPGMRARGGGLIINVSS---IAARNAFPQ--W-- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 192 rkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK07454  153 ------GAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 34-237 3.15e-18

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 81.48  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  34 ATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR--GETLNHHVnarhLDLASLKSIREFAAKI 111
Cdd:PRK13394    3 SNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINkaGGKAIGVA----MDVTNEDAVNAGIDKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 112 IEEEERVDILINNAG---VMRCPHWTTEDGFEMQfGVNHLGHFLLTNLL-LDKLKASAPSRIINLSSL-AHVAGHIdfdd 186
Cdd:PRK13394   79 AERFGSVDILVSNAGiqiVNPIENYSFADWKKMQ-AIHVDGAFLTTKAAlKHMYKDDRGGVVIYMGSVhSHEASPL---- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK13394  154 ----------KSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPL 194
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 38-231 3.28e-18

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 81.23  E-value: 3.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVnARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd08930     2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVI-ALELDITSKESIKELIESYLEKFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV-----MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHiDFDdlNWQTR 192
Cdd:cd08930    81 IDILINNAYPspkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAP-DFR--IYENT 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462495797 193 KYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd08930   158 QMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 38-239 3.29e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 81.00  E-value: 3.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLnhHVNArhLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12828    7 GKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADAL--RIGG--IDLVDPQAARRAVDEVNRQFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRcphWTT-EDG----FEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVaghidfddlnwqtR 192
Cdd:PRK12828   83 LDALVNIAGAFV---WGTiADGdadtWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAAL-------------K 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 193 KYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK12828  147 AGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNR 193
PRK07201 PRK07201
SDR family oxidoreductase;
33-126 3.81e-18

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 83.46  E-value: 3.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  33 KATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKII 112
Cdd:PRK07201  366 RGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAH--AYTCDLTDSAAVDHTVKDIL 443

                          90
                  ....*....|....
gi 2462495797 113 EEEERVDILINNAG 126
Cdd:PRK07201  444 AEHGHVDYLVNNAG 457
PRK07774 PRK07774
SDR family oxidoreductase;
38-241 3.97e-18

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 80.94  E-value: 3.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07774    6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGT--AIAVQVDVSDPDSAKAMADATVSAFGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM---------RCPhWtteDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAhvaghidfddlN 188
Cdd:PRK07774   84 IDYLVNNAAIYggmkldlliTVP-W---DYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTA-----------A 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462495797 189 WQTRKYntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 241
Cdd:PRK07774  149 WLYSNF-----YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTV 196
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 36-240 7.28e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 81.51  E-value: 7.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK07109    6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRA--AGGEALAVVADVADAEAVQAAADRAEEEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGV-MRCPHW-TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddLNWQtrk 193
Cdd:PRK07109   84 GPIDTWVNNAMVtVFGPFEdVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRS------IPLQ--- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 194 yntkAAYCQSKLAIVLFTKELSRRLQ--GSGVTVNALHPGV--------ARTELGRH 240
Cdd:PRK07109  155 ----SAYCAAKHAIRGFTDSLRCELLhdGSPVSVTMVQPPAvntpqfdwARSRLPVE 207
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 38-235 7.90e-18

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 80.12  E-value: 7.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlnhhvnAR--HLDLASLKSIREFAAKIIEEE 115
Cdd:cd05341     5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDA-------ARffHLDVTDEDGWTAVVDTAREAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGV---MRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtr 192
Cdd:cd05341    78 GRLDVLVNNAGIltgGTVETTTLEE-WRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPAL-------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKE--LSRRLQGSGVTVNALHPGVART 235
Cdd:cd05341   149 -----AAYNASKGAVRGLTKSaaLECATQGYGIRVNSVHPGYIYT 188
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 36-238 8.99e-18

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 80.13  E-value: 8.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEA-AAKDIRG--ETLNHHVNAR-------HLDLASLKSIR 105
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNgSAKSLPGtiEETAEEIEAAggqalpiVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 106 EFAAKIIEEEERVDILINNAGVMrcphWTT--EDG----FEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS---LA 176
Cdd:cd05338    81 ALVEATVDQFGRLDILVNNAGAI----WLSlvEDTpakrFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPplsLR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 177 HVAGHidfddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 238
Cdd:cd05338   157 PARGD----------------VAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPA 202
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 39-231 9.80e-18

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 79.33  E-value: 9.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirgetlNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS------GGDVEAVPYDARDPEDARALVDALRDRFGRI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVMRcpHWTTEDG----FEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHidfddlnwqtrky 194
Cdd:cd08932    75 DVLVHNAGIGR--PTTLREGsdaeLEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVL------------- 139

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462495797 195 NTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd08932   140 AGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPG 176
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 41-259 1.50e-17

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 79.44  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKdirgetlnhHVNARHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGD---------PLRLTPLDVADAAAVREVCSRLLAEHGPIDA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkA 198
Cdd:cd05331    72 LVNCAGVLRpgATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISM-------------A 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 199 AYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRhTGIHGSTFSSTTLASKPQT 259
Cdd:cd05331   139 AYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQR-TLWHDEDGAAQVIAGVPEQ 198
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 38-239 2.05e-17

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 79.05  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirgetlNHHVNARHLDLASLKSIREFAAKIIEeeer 117
Cdd:cd05351     7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRE------CPGIEPVCVDLSDWDATEEALGSVGP---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASA-PSRIINLSSlahVAGHIDFDDLnwqtrky 194
Cdd:cd05351    77 VDLLVNNAAVaiLQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSS---QASQRALTNH------- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:cd05351   147 ---TVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGR 188
PRK07035 PRK07035
SDR family oxidoreductase;
38-235 2.08e-17

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 78.90  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHldLASLKSIREFAAKIIEEEER 117
Cdd:PRK07035    8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACH--IGEMEQIDALFAHIRERHGR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMrcPHW-----TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHV-AGHidfddlnWQt 191
Cdd:PRK07035   86 LDILVNNAAAN--PYFghildTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVsPGD-------FQ- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 192 rkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK07035  156 ------GIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK08589 PRK08589
SDR family oxidoreductase;
39-237 2.16e-17

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 79.44  E-value: 2.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIIlaCRDM-EKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08589    7 KVAVITGASTGIGQASAIALAQEGAYVL--AVDIaEAVSETVDKIKSNGGKAK--AYHVDISDEQQVKDFASEIKEQFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP---HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSrIINLSSLAHVAGhidfdDLNwqtrky 194
Cdd:PRK08589   83 VDVLFNNAGVDNAAgriHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGS-IINTSSFSGQAA-----DLY------ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 ntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK08589  151 --RSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPL 191
PRK06138 PRK06138
SDR family oxidoreductase;
38-239 2.65e-17

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 78.65  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06138    5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA---GGRAFARQGDVGSAEAVEALVDFVAARWGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwqtrkyn 195
Cdd:PRK06138   82 LDVLVNNAGFGCGGTVvtTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRG------------ 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 196 tKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK06138  150 -RAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFR 192
PRK08264 PRK08264
SDR family oxidoreductase;
36-240 2.70e-17

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 78.39  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGniilacrdmEKCEAAAKDIRGETLNHH-VNARHLDLASLKSIREFAAKIIEe 114
Cdd:PRK08264    4 IKGKVVLVTGANRGIGRAFVEQLLARGA---------AKVYAAARDPESVTDLGPrVVPLQLDVTDPASVAAAAEAASD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 eerVDILINNAGVMRCPHW---TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqt 191
Cdd:PRK08264   74 ---VTILVNNAGIFRTGSLlleGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLS---VLSWVNFPNL---- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 192 rkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK08264  144 ------GTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAG 186
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 35-237 2.79e-17

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 78.64  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLnhHVNARHLDLaSLKSIREFAAKIIEE 114
Cdd:cd05329     3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGF--KVEGSVCDV-SSRSERQELMDTVAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 --EERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFddlnwq 190
Cdd:cd05329    80 hfGGKLNILVNNAGTNIRKEAKdyTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISS---VAGVIAV------ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 191 trkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05329   151 ----PSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPL 193
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 35-237 8.70e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 77.35  E-value: 8.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRD-MEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIE 113
Cdd:PRK12935    3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSsKEAAENLVNELGKE--GHDVYAVQADVSKVEDANRLVEEAVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhiDFDDLNwqt 191
Cdd:PRK12935   81 HFGKVDILVNNAGITRDRTFKklNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAG--GFGQTN--- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 192 rkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12935  156 --------YSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 38-237 1.07e-16

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 76.98  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIIL-----ACRDMEKCEAAAKDIRGETLNHHVNArhldLASLKSIrEFAAKII 112
Cdd:cd05353     5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggDRKGSGKSSSAADKVVDEIKAAGGKA----VANYDSV-EDGEKIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 113 E----EEERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfdd 186
Cdd:cd05353    80 KtaidAFGRVDILVNNAGILRdrSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFG--- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGvARTEL 237
Cdd:cd05353   157 ----------QANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRM 196
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 40-237 1.77e-16

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 76.73  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGGNI-ILACRDMEkceaAAKDIRGETLNHHVNAR--HLDLASLKSIREFAAKIIEEEE 116
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIaINDLPDDD----QATEVVAEVLAAGRRAIyfQADIGELSDHEALLDQAWEDFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCPHW----TTEDGFEMQFGVNHLGHF------LLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfdd 186
Cdd:cd05337    79 RLDCLVNNAGIAVRPRGdlldLTEDSFDRLIAINLRGPFfltqavARRMVEQPDRFDGPHRSIIFVTSINAYLVSPN--- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05337   156 ----------RGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM 196
PRK09072 PRK09072
SDR family oxidoreductase;
36-237 2.54e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 76.13  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgeTLNHHVNARHLDLASLKSIREFAAKiIEEE 115
Cdd:PRK09072    3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL---PYPGRHRWVVADLTSEAGREAVLAR-AREM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDfddlnwqtrk 193
Cdd:PRK09072   79 GGINVLINNAGVNHFALLEdqDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGS---TFGSIG---------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 194 YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK09072  146 YPGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
38-230 2.63e-16

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 78.35  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlnhHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08324  422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD---RALGVACDVTDEAAVQAAFEEAALAFGG 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASA-PSRIINLSSLAHVAGHIDFddlnwqtrky 194
Cdd:PRK08324  499 VDIVVSNAGIAisGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNF---------- 568

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 230
Cdd:PRK08324  569 ---GAYGAAKAAELHLVRQLALELGPDGIRVNGVNP 601
PRK07832 PRK07832
SDR family oxidoreductase;
39-245 2.67e-16

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 76.23  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR--GETLNHHvnaRHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARalGGTVPEH---RALDISDYDAVAAFAADIHAAHG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVmrcPHWTTEDGFEMQ-----FGVNHLG--HfLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddLNW 189
Cdd:PRK07832   78 SMDVVMNIAGI---SAWGTVDRLTHEqwrrmVDVNLMGpiH-VIETFVPPMVAAGRGGHLVNVSSAAGLVA------LPW 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 190 QtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHG 245
Cdd:PRK07832  148 H-------AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAG 196
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 34-237 3.12e-16

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 75.55  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  34 ATIPGKTVIVTGANTGIGKQTALELARRG--------GNIILACRDMEKCEAAAkdirGETLnhhvnARHLDLASLKSIR 105
Cdd:PRK12937    1 MTLSNKVAIVTGASRGIGAAIARRLAADGfavavnyaGSAAAADELVAEIEAAG----GRAI-----AVQADVADAAAVT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 106 EFAAKIIEEEERVDILINNAGVMRCPHWTTED--GFEMQFGVNHLGHFLLTnllldklKASAP-----SRIINLSSlahv 178
Cdd:PRK12937   72 RLFDAAETAFGRIDVLVNNAGVMPLGTIADFDleDFDRTIATNLRGAFVVL-------REAARhlgqgGRIINLST---- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462495797 179 aghidfddlNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12937  141 ---------SVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 38-237 6.51e-16

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 75.41  E-value: 6.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDME--KCEAAAKDIRGETLNHHVNARhlDLASLKSIREFAAKIIEEE 115
Cdd:cd05355    26 GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEedDAEETKKLIEEEGRKCLLIPG--DLGDESFCRDLVKEVVKEF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGvMRCPHWTTED----GFEMQFGVNHLGHFlltnlllDKLKASAP-----SRIINLSSLAHVAGHIDFDD 186
Cdd:cd05355   104 GKLDILVNNAA-YQHPQESIEDitteQLEKTFRTNIFSMF-------YLTKAALPhlkkgSSIINTTSVTAYKGSPHLLD 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05355   176 -------------YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
PRK06484 PRK06484
short chain dehydrogenase; Validated
 27-235 1.05e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 76.43  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  27 GGACPSKATIP----GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLnhhvnARHLDLASLK 102
Cdd:PRK06484  254 GPASTAQAPSPlaesPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHL-----SVQADITDEA 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 103 SIREFAAKIIEEEERVDILINNAG---VMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLkaSAPSRIINLSSlahVA 179
Cdd:PRK06484  329 AVESAFAQIQARWGRLDVLVNNAGiaeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGS---IA 403

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 180 GHIDFDDLNwqtrkyntkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK06484  404 SLLALPPRN----------AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06182 PRK06182
short chain dehydrogenase; Validated
 39-239 1.46e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 74.23  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKdirgetlnHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS--------LGVHPLSLDVTDEASIKAAVDTIIAEEGRI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAG------VMRCPhwtTEDGfEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdFDDLNwqtr 192
Cdd:PRK06182   76 DVLVNNAGygsygaIEDVP---IDEA-RRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISS---MGGKI-YTPLG---- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK06182  144 -----AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGD 185
PRK07775 PRK07775
SDR family oxidoreductase;
39-238 1.50e-15

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 74.41  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR---GETLNHhvnarHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK07775   11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRadgGEAVAF-----PLDVTDPDSVKSFVAQAEEAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahvaghidfdDLNWQTRK 193
Cdd:PRK07775   86 GEIEVLVSGAGDTYfgKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGS-----------DVALRQRP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 194 YntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 238
Cdd:PRK07775  155 H--MGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMG 197
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 39-241 1.79e-15

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 73.31  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhhvNARHL--DLASLKSIREFAAKIIEEEE 116
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELE-------GVLGLagDVRDEADVRRAVDAMEEAFG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVaghidfddlnwqtRKY 194
Cdd:cd08929    74 GLDALVNNAGVgvMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGK-------------NAF 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 195 NTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 241
Cdd:cd08929   141 KGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSP 187
PRK06500 PRK06500
SDR family oxidoreductase;
38-237 2.96e-15

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 73.07  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAakdirGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06500    6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAA-----RAELGESALVIRADAGDVAAQKALAQALAEAFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV---MRCPHWtTEDGFEMQFGVNHLGHFLLTNLLLDKLKASApSRIINLSSLAHVAghidfddlnwqtrkY 194
Cdd:PRK06500   81 LDAVFINAGVakfAPLEDW-DEAMFDRSFNTNVKGPYFLIQALLPLLANPA-SIVLNGSINAHIG--------------M 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 NTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06500  145 PNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPL 187
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 38-237 2.98e-15

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 73.19  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrGETLnHHVNArhlDLASLKSIREFAAKIIEEEER 117
Cdd:cd05345     5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI-GEAA-IAIQA---DVTKRADVEAMVEAALSKFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWT---TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLNWqtrky 194
Cdd:cd05345    80 LDILVNNAGITHRNKPMlevDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIAS---TAGLRPRPGLTW----- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 ntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05345   152 -----YNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-237 3.00e-15

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 73.28  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARhldlaslKSIREFAAKIIEEEER 117
Cdd:PRK06463    7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGVFTIKCDVGNR-------DQVKKSKEVVEKEFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAghidfddlnwqTRKYN 195
Cdd:PRK06463   80 VDVLVNNAGIMYLMPFEEfdEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIG-----------TAAEG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 196 TkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06463  149 T-TFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
PRK07326 PRK07326
SDR family oxidoreductase;
38-241 3.65e-15

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 72.74  E-value: 3.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirgetLNHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:PRK07326    6 GKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAE-----LNNKGNVLGLaaDVRDEADVQRAVDAIVAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFlltnlllDKLKASAPS------RIINLSSLAhvaghidfddl 187
Cdd:PRK07326   81 GGLDVLIANAGVghFAPVEELTPEEWRLVIDTNLTGAF-------YTIKAAVPAlkrgggYIINISSLA----------- 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 188 nwQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 241
Cdd:PRK07326  143 --GTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHT 194
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 31-240 3.67e-15

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 73.40  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR---GETLNHHVNArhLDLASLKSIREf 107
Cdd:PRK08277    3 PNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKaagGEALAVKADV--LDKESLEQARQ- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 aaKIIEEEERVDILINNAGVMRcPHWTT------------------EDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRI 169
Cdd:PRK08277   80 --QILEDFGPCDILINGAGGNH-PKATTdnefhelieptktffdldEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 170 INLSSLAhvaghiDFDDLnwqtrkynTK-AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK08277  157 INISSMN------AFTPL--------TKvPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRA 214
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 38-238 4.00e-15

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 72.62  E-value: 4.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLN----HHVNARHLDlaslkSIREFAAKIIE 113
Cdd:cd05369     3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGrahpIQCDVRDPE-----AVEAAVDETLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNA-GVMRCPhwtTED----GFEMQFGVNHLGHFLLTNLLLDK-LKASAPSRIINLSSlahvaghidfdDL 187
Cdd:cd05369    78 EFGKIDILINNAaGNFLAP---AESlspnGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISA-----------TY 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 188 NWQTRKYNTKAAycQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 238
Cdd:cd05369   144 AYTGSPFQVHSA--AAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEG 192
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 38-237 5.65e-15

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 72.25  E-value: 5.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgetLNHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIE---EKYGVETKTIaaDFSAGDDIYERIEKELEGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ErVDILINNAGVmrCPH----WTTEDGFEMQ-------FGVNHLGHFlltnlLLDKLKASAPSRIINLSSLAhvaghidf 184
Cdd:cd05356    78 D-IGILVNNVGI--SHSipeyFLETPEDELQdiinvnvMATLKMTRL-----ILPGMVKRKKGAIVNISSFA-------- 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462495797 185 ddlNWQTRKYntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05356   142 ---GLIPTPL--LATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKM 189
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 38-240 6.94e-15

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 72.10  E-value: 6.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgetlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05326     4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELG----DPDISFVHCDVTVEADVRAAVDTAVARFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHW----TTEDGFEMQFGVNHLGHFlltNLLLDKLKASAPSR---IINLSSLAHVAGHIdfddlnwq 190
Cdd:cd05326    80 LDIMFNNAGVLGAPCYsileTSLEEFERVLDVNVYGAF---LGTKHAARVMIPAKkgsIVSVASVAGVVGGL-------- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 191 trkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:cd05326   149 -----GPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTA 193
PRK07063 PRK07063
SDR family oxidoreductase;
38-146 2.05e-14

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 70.85  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07063    7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFGP 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462495797 118 VDILINNAG--VMRCPHWTTEDGFEMQFGVN 146
Cdd:PRK07063   87 LDVLVNNAGinVFADPLAMTDEDWRRCFAVD 117
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 39-237 2.68e-14

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 70.38  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNI-ILACRDMEKCEAAAKDIRGetlnHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLaINDRPDDEELAATQQELRA----LGVEVIFFpaDVADLSAHEAMLDAAQAAW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHW----TTEDGFEMQFGVNHLGHF-----LLTNLLLDKLKASAPSR-IINLSSLAHVAGHIDfd 185
Cdd:PRK12745   79 GRIDCLVNNAGVGVKVRGdlldLTPESFDRVLAINLRGPFfltqaVAKRMLAQPEPEELPHRsIVFVSSVNAIMVSPN-- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 186 dlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12745  157 -----------RGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 38-231 2.79e-14

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 70.33  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirgetLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12936    6 GRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAE-----LGERVKIFPANLSDRDEVKALGQKAEADLEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMR---CPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHidfddlnwqtrky 194
Cdd:PRK12936   81 VDILVNNAGITKdglFVRMSDED-WDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGN------------- 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462495797 195 NTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK12936  147 PGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPG 183
PRK05867 PRK05867
SDR family oxidoreductase;
38-237 3.47e-14

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 70.06  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK05867    9 GKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGT--SGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTTEDGFEMQF--GVNHLGHFLLtnllldklkASAPSRII-------NLSSLAHVAGHIdfddLN 188
Cdd:PRK05867   87 IDIAVCNAGIITVTPMLDMPLEEFQRlqNTNVTGVFLT---------AQAAAKAMvkqgqggVIINTASMSGHI----IN 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 189 WQTRkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK05867  154 VPQQ----VSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 38-231 3.97e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 69.99  E-value: 3.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07890    5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDD--LGRRALAVPTDITDEDQCANLVALALERFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNA---GVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSrIINLSSLahVAGHidfddlnwQTRKY 194
Cdd:PRK07890   83 VDALVNNAfrvPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGS-IVMINSM--VLRH--------SQPKY 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK07890  152 ---GAYKMAKGALLAASQSLATELGPQGIRVNSVAPG 185
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 39-231 4.14e-14

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 69.61  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRdmeKCEAAAKDIRGEtlnhhVNARHL-------DLASLKSIREFAAKI 111
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYN---RSEAEAQRLKDE-----LNALRNsavlvqaDLSDFAACADLVAAA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 112 IEEEERVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSslahvaghidfDDLNW 189
Cdd:cd05357    73 FRAFGRCDVLVNNASAFypTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINII-----------DAMTD 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 190 QTRKYNTkaAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 231
Cdd:cd05357   142 RPLTGYF--AYCMSKAALEGLTRSAALEL-APNIRVNGIAPG 180
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 35-126 4.79e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 69.69  E-value: 4.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlNHHVNARHLDLASLKSIREFAAKIIEe 114
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAH-GVDVAVHALDLSSPEAREQLAAEAGD- 81

                          90
                  ....*....|..
gi 2462495797 115 eerVDILINNAG 126
Cdd:PRK06125   82 ---IDILVNNAG 90
PRK07577 PRK07577
SDR family oxidoreductase;
37-257 4.86e-14

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 69.37  E-value: 4.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDmekceaAAKDIRGETLNhhvnarhLDLASLKSIREFAAKIIEEEe 116
Cdd:PRK07577    2 SSRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGELFA-------CDLADIEQTAATLAQINEIH- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMR--------CPHWTTEDGFEMQFGVNHLGHFLLTNllldklKASAPSRIINLSSLAhVAGHIDfddln 188
Cdd:PRK07577   68 PVDAIVNNVGIALpqplgkidLAALQDVYDLNVRAAVQVTQAFLEGM------KLREQGRIVNICSRA-IFGALD----- 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462495797 189 wqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFSSTTLASKP 257
Cdd:PRK07577  136 --------RTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVLASIP 196
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 38-236 7.34e-14

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 69.18  E-value: 7.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgetlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05363     3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI-----GPAACAISLDVTDQASIDRCVAALVDRWGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS-RIINLSSLAHVAGHIdfddlnwqtrky 194
Cdd:cd05363    78 IDILVNNAALfdLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGgKIINMASQAGRRGEA------------ 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 195 nTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd05363   146 -LVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 38-240 7.76e-14

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 69.24  E-value: 7.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAK-DIRGETLnhhvnarHLDLASLKSIREFAAKIIEEEE 116
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKlGDNCRFV-------PVDVTSEKDVKAALALAKAKFG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVM----------RCPHwTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASAPSR------IINLSSLAHVAG 180
Cdd:cd05371    75 RLDIVVNCAGIAvaaktynkkgQQPH-SLEL-FQRVINVNLIGTFNVIRLAAGAMGKNEPDQggergvIINTASVAAFEG 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 181 HIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:cd05371   153 QIG-------------QAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAG 199
PRK06172 PRK06172
SDR family oxidoreductase;
34-239 8.02e-14

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 69.01  E-value: 8.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  34 ATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDM---EKCEAAAKDIRGETLnhhvnARHLDLASLKSIREFAAK 110
Cdd:PRK06172    3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEAL-----FVACDVTRDAEVKALVEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 111 IIEEEERVDILINNAGVMRCPHWT---TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddl 187
Cdd:PRK06172   78 TIAAYGRLDYAFNNAGIEIEQGRLaegSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKM--- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 188 nwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK06172  155 ----------SIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFR 196
PRK06128 PRK06128
SDR family oxidoreductase;
38-237 9.70e-14

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 69.50  E-value: 9.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06128   55 GRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAG----VMRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASApsRIINLSSLahvaghidfddlnwqtRK 193
Cdd:PRK06128  135 LDILVNIAGkqtaVKDIADITTEQ-FDATFKTNVYAMFWLCKAAIPHLPPGA--SIINTGSI----------------QS 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 194 YNTKAA---YCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06128  196 YQPSPTlldYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 39-235 1.01e-13

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 69.10  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVE--ADGRTCDVRSVPEIEALVAAAVARYGPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGvmRCPHWTTED-GFEMQFGV---NHLGHFLLTNLLLDK--LKASAPSRIINLSSLAHVAGHIdfddlnwqtr 192
Cdd:cd08945    82 DVLVNNAG--RSGGGATAElADELWLDVvetNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVV---------- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 193 kynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:cd08945   150 ---HAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVET 189
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 41-237 1.20e-13

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 68.51  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCeaaaKDIRGETL--NHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRL----DELKAELLnpNPSVEVEILDVTDEERNQLVIAELEAELGGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGV---MRCPHWTTEDGFEMqFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrkYN 195
Cdd:cd05350    77 DLVIINAGVgkgTSLGDLSFKAFRET-IDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRG-------------LP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd05350   143 GAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 41-240 1.21e-13

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 68.53  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRdmeKCEAAAKDIRGETLNHHVNARHL--DLASLKSIREFAAKIIEEEERV 118
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYR---KSKDAAAEVAAEIEELGGKAVVVraDVSQPQDVEEMFAAVKERFGRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNA--GVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAhvaghidfddlnwQTRKYNT 196
Cdd:cd05359    78 DVLVSNAaaGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLG-------------SIRALPN 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 197 KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:cd05359   145 YLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAH 188
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 38-236 1.47e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 68.49  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILAC-RDMEKCEAAAKDIR-GETLNHHVNArhlDLASLKSIREFAAKIIEEE 115
Cdd:PRK06198    6 GKVALVTGGTQGLGAAIARAFAERGAAGLVICgRNAEKGEAQAAELEaLGAKAVFVQA---DLSDVEDCRRVVAAADEAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVM-RCPHW-TTEDGFEMQFGVNHLGHFLLTNLLLDKLKA-SAPSRIINLSSLAHVAGHIDFddlnwqtr 192
Cdd:PRK06198   83 GRLDALVNAAGLTdRGTILdTSPELFDRHFAVNVRAPFFLMQEAIKLMRRrKAEGTIVNIGSMSAHGGQPFL-------- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK06198  155 -----AAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK05866 PRK05866
SDR family oxidoreductase;
34-126 1.48e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 69.00  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  34 ATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIE 113
Cdd:PRK05866   36 VDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAM--AVPCDLSDLDAVDALVADVEK 113

                          90
                  ....*....|...
gi 2462495797 114 EEERVDILINNAG 126
Cdd:PRK05866  114 RIGGVDILINNAG 126
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
38-240 1.56e-13

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 68.21  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILA-CRDMEKCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK08063    4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEI--EALGRKALAVKANVGDVEKIKEMFAQIDEEFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNA--GVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLahvaGHIdfddlnwqtRKY 194
Cdd:PRK08063   82 RLDVFVNNAasGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSL----GSI---------RYL 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 195 NTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK08063  149 ENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKH 194
PRK08278 PRK08278
SDR family oxidoreductase;
38-230 1.60e-13

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 68.39  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEK-------CEAAAKDIR---GETLnhhvnARHLDLASLKSIREF 107
Cdd:PRK08278    6 GKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPhpklpgtIHTAAEEIEaagGQAL-----PLVGDVRDEDQVAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAGVMRCPhwTTED----GFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahvaghid 183
Cdd:PRK08278   81 VAKAVERFGGIDICVNNASAINLT--GTEDtpmkRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSP--------- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 184 fdDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 230
Cdd:PRK08278  150 --PLNLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK07814 PRK07814
SDR family oxidoreductase;
36-236 1.83e-13

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 68.27  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEE 115
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVA--ADLAHPEATAGLAGQAVEAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINN-AGVMRCPHWTT-----EDGFEMQFGVNHlghflltnlllDKLKASAPS--------RIINLSS-LAHVAG 180
Cdd:PRK07814   86 GRLDIVVNNvGGTMPNPLLSTstkdlADAFTFNVATAH-----------ALTVAAVPLmlehsgggSVINISStMGRLAG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 181 hidfddlnwqtRKYntkAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPGVARTE 236
Cdd:PRK07814  155 -----------RGF---AAYGTAKAALAHYTRLAALDL-CPRIRVNAIAPGSILTS 195
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 38-237 2.26e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 68.52  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDmEKCEAAakdirgETlNHHVNA---RHL----DLASLKSIREFAAK 110
Cdd:PRK06701   46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLD-EHEDAN------ET-KQRVEKegvKCLlipgDVSDEAFCKDAVEE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 111 IIEEEERVDILINNAGVMRcpHWT-----TEDGFEMQFGVNHLGHFlltnlllDKLKASAP-----SRIINLSSLAHVAG 180
Cdd:PRK06701  118 TVRELGRLDILVNNAAFQY--PQQslediTAEQLDKTFKTNIYSYF-------HMTKAALPhlkqgSAIINTGSITGYEG 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 181 HIDFDDlnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06701  189 NETLID-------------YSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL 232
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
38-235 2.52e-13

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 67.83  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgetlnhHVNARHLDLASLKSIRE--FAA--KIIE 113
Cdd:PRK08643    2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLS------KDGGKAIAVKADVSDRDqvFAAvrQVVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVM-RCPHWT-TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS-RIINLSSLAHVAGHIDFddlnwq 190
Cdd:PRK08643   76 TFGDLNVVVNNAGVApTTPIETiTEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGgKIINATSQAGVVGNPEL------ 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 191 trkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK08643  150 -------AVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
PRK08017 PRK08017
SDR family oxidoreductase;
39-235 2.61e-13

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 67.80  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEaaakdiRGETLNhhVNARHLDLASLKSIREFAAKIIE-EEER 117
Cdd:PRK08017    3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVA------RMNSLG--FTGILLDLDDPESVERAADEVIAlTDNR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV-MRCPHWT-TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwQTRKyn 195
Cdd:PRK08017   75 LYGLFNNAGFgVYGPLSTiSRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSS---VMGLI-------STPG-- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462495797 196 tKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK08017  143 -RGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
PRK06124 PRK06124
SDR family oxidoreductase;
38-236 3.03e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 67.43  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06124   11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGA--AEALAFDIADEEAVAAAFARIDAEHGR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM-RCP--HWTTEDGFEMqFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqTRKY 194
Cdd:PRK06124   89 LDILVNNVGARdRRPlaELDDAAIRAL-LETDLVAPILLSRLAAQRMKRQGYGRIIAITS---IAGQV--------ARAG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 195 NtkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK06124  157 D--AVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
PRK05650 PRK05650
SDR family oxidoreductase;
41-260 3.20e-13

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 67.76  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:PRK05650    3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFY--QRCDVRDYSQLTALAQACEEKWGGIDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGVmrcphwTTEDGFE--------MQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAgHIDFDDlnwqtr 192
Cdd:PRK05650   81 IVNNAGV------ASGGFFEelsledwdWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLM-QGPAMS------ 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462495797 193 KYNTkaaycqSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELgrhtgihGSTFSSTTLASKPQTG 260
Cdd:PRK05650  148 SYNV------AKAGVVALSETLLVELADDEIGVHVVCPSFFQTNL-------LDSFRGPNPAMKAQVG 202
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 39-235 3.53e-13

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 67.09  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDmekcEAAAKDIRGETLNHHVNARHLDL----ASLKSIREFAAkiiEE 114
Cdd:cd08931     1 KAIFITGAASGIGRETALLFARNGWFVGLYDID----EDGLAALAAELGAENVVAGALDVtdraAWAAALADFAA---AT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRCpHWTTEDGFE---MQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqt 191
Cdd:cd08931    74 GGRLDALFNNAGVGRG-GPFEDVPLAahdRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDL------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 192 rkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:cd08931   146 ------AVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDT 183
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 38-235 4.82e-13

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 66.83  E-value: 4.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlnhHVNARHLDL----ASLKSIREFAAKIIE 113
Cdd:cd05340     4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEG---GRQPQWFILdlltCTSENCQQLAQRIAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVM--RCP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlNWq 190
Cdd:cd05340    81 NYPRLDGVLHNAGLLgdVCPlSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRA-----NW- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 191 trkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:cd05340   155 -------GAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 38-237 4.92e-13

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 66.96  E-value: 4.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIIL--ACRD----------MEKCEAAAKDIRGETLNHHVNARhlDLASLksiR 105
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAvdLCADdpavgyplatRAELDAVAAACPDQVLPVIADVR--DPAAL---A 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 106 EFAAKIIEEEERVDILINNAGVMRC--PHWTTEDG-FEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHI 182
Cdd:TIGR04504  76 AAVALAVERWGRLDAAVAAAGVIAGgrPLWETTDAeLDLLLDVNLRGVWNLARAAVPAMLARPDPRGGRFVAVASAAATR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462495797 183 DFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:TIGR04504 156 GLPHL----------AAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAM 200
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 38-237 6.67e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 67.01  E-value: 6.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIIL---------ACRDMEKCEAAAKDIR---GETLNHHVNARHLDLAslKSIR 105
Cdd:PRK07791    6 GRVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgSASGGSAAQAVVDEIVaagGEAVANGDDIADWDGA--ANLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 106 EFAakiIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAP------SRIINLSSLAH 177
Cdd:PRK07791   84 DAA---VETFGGLDVLVNNAGILRDRMIanMSEEEWDAVIAVHLKGHFATLRHAAAYWRAESKagravdARIINTSSGAG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 178 VAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPgVARTEL 237
Cdd:PRK07791  161 LQGSVG-------------QGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AARTRM 206
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 39-237 7.11e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 66.85  E-value: 7.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMekceAAAKDIRGETLnhhvnaRHLDLASLKSIREFAAKIIEEEERV 118
Cdd:PRK06179    5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNP----ARAAPIPGVEL------LELDVTDDASVQAAVDEVIARAGRI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVM---RCPHWTTEDGFEMqFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqTRKYN 195
Cdd:PRK06179   75 DVLVNNAGVGlagAAEESSIAQAQAL-FDTNVFGILRMTRAVLPHMRAQGSGRIINISS---VLGFL--------PAPYM 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 196 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06179  143 --ALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
38-236 7.66e-13

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 66.47  E-value: 7.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNII-----LACRDMEKCEAAAKDIrgetlnHHVNArhlDLASLKSIREFAAKII 112
Cdd:PRK12481    8 GKVAIITGCNTGLGQGMAIGLAKAGADIVgvgvaEAPETQAQVEALGRKF------HFITA---DLIQQKDIDSIVSQAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 113 EEEERVDILINNAGVMRcphwtTEDGFEMQ-------FGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDF 184
Cdd:PRK12481   79 EVMGHIDILINNAGIIR-----RQDLLEFGnkdwddvININQKTvFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGIRV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 185 ddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK12481  154 -------------PSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 38-237 8.94e-13

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 66.40  E-value: 8.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEkceaaakdiRGETLNHHVNARHL--------DLASLKSIREFAA 109
Cdd:cd08933     9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEA---------AGQALESELNRAGPgsckfvpcDVTKEEDIKTLIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 110 KIIEEEERVDILINNAGvMRCPHWTTED----GFEMQFGVNHLGHFLLTNLLLDKLKASApSRIINLSSLAHVAGHIDfd 185
Cdd:cd08933    80 VTVERFGRIDCLVNNAG-WHPPHQTTDEtsaqEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQKQ-- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 186 dlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd08933   156 -----------AAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 38-231 1.00e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 66.21  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP---HWTTEDgFEMQFGVNHLGHFL-LTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtRK 193
Cdd:PRK12384   82 VDLLVYNAGIAKAAfitDFQLGD-FDRSLQVNLVGYFLcAREFSRLMIRDGIQGRIIQINSKSGKVG-----------SK 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462495797 194 YNTkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK12384  150 HNS--GYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 41-236 1.16e-12

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 65.67  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAI--GLECNVTSEQDLEAVVKATVSQFGGITI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNA---GVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntk 197
Cdd:cd05365    80 LVNNAgggGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRI------------- 146

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd05365   147 AAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTD 185
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 36-237 1.25e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 65.75  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK08217    3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTE--VRGYAANVTDEEDVEATFAQIAEDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRcphwtteDGF-----------EM---QF----GVNHLGHFLLTNLLLDKLKASAPS-RIINLSSLA 176
Cdd:PRK08217   81 GQLNGLINNAGILR-------DGLlvkakdgkvtsKMsleQFqsviDVNLTGVFLCGREAAAKMIESGSKgVIINISSIA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462495797 177 HvAGHIDfddlnwQTRkyntkaaYCQSKLAIVLFT----KELSRRlqgsGVTVNALHPGVARTEL 237
Cdd:PRK08217  154 R-AGNMG------QTN-------YSASKAGVAAMTvtwaKELARY----GIRVAAIAPGVIETEM 200
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 38-240 1.94e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 65.13  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIIL----ACRDMEKCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIE 113
Cdd:PRK12827    6 SRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGI--EAAGGKALGLAFDVRDFAATRAALDAGVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVMRC---PHWTTEDgFEMQFGVNHLGHFLLTNLLLD-KLKASAPSRIINLSSLAHVAGHidfddlnw 189
Cdd:PRK12827   84 EFGRLDILVNNAGIATDaafAELSIEE-WDDVIDVNLDGFFNVTQAALPpMIRARRGGRIVNIASVAGVRGN-------- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 190 qtRKYntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK12827  155 --RGQ---VNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADN 200
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 36-232 2.27e-12

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 65.03  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIilACRDMEKceaaakdirGETLNHHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANV--VNADIHG---------GDGQHENYQFVPTDVSSAEEVNHTVAEIIEKF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVM-----------RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDf 184
Cdd:PRK06171   76 GRIDGLVNNAGINiprllvdekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEG- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462495797 185 ddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 232
Cdd:PRK06171  155 ------------QSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGI 190
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 31-249 3.32e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 64.99  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIrefAAK 110
Cdd:PRK05872    2 PPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVVADVTDLAAMQAA---AEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 111 IIEEEERVDILINNAGVMRCPHWTTED--GFEMQFGVNHLGHFlltnlllDKLKASAPSRI------INLSSLAHVAGHI 182
Cdd:PRK05872   79 AVERFGGIDVVVANAGIASGGSVAQVDpdAFRRVIDVNLLGVF-------HTVRATLPALIerrgyvLQVSSLAAFAAAP 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 183 DFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFS 249
Cdd:PRK05872  152 GM-------------AAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFR 205
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 39-239 3.94e-12

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 64.61  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACrdMEKCEAAAKDIRGETlNHHVNARHLDLASLKSIREfAAKIIEE---E 115
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGC--LTKNGPGAKELRRVC-SDRLRTLQLDVTKPEQIKR-AAQWVKEhvgE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCP---HWTTEDGFEMQFGVNHLGhflltnlLLDKLKA------SAPSRIINLSSlahVAGHIDFdd 186
Cdd:cd09805    77 KGLWGLVNNAGILGFGgdeELLPMDDYRKCMEVNLFG-------TVEVTKAflpllrRAKGRVVNVSS---MGGRVPF-- 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462495797 187 lnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:cd09805   145 --------PAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITG 189
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-235 4.10e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 64.80  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILacRDM---EKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEE 114
Cdd:PRK07792   12 GKVAVVTGAAAGLGRAEALGLARLGATVVV--NDVasaLDASDVLDEIRA------AGAKAVAVAGDISQRATADELVAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EE---RVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS-------RIINLSSLAHVAGHI 182
Cdd:PRK07792   84 AVglgGLDIVVNNAGITrdRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKAaggpvygRIVNTSSEAGLVGPV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462495797 183 DfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGvART 235
Cdd:PRK07792  164 G-------------QANYGAAKAGITALTLSAARALGRYGVRANAICPR-ART 202
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 38-239 7.16e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 63.62  E-value: 7.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08085    9 GKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAP--FNVTHKQEVEAAIEHIEKDIGP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHidfddlnwqtrkyN 195
Cdd:PRK08085   87 IDVLINNAGIQRRHPFTEfpEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGR-------------D 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK08085  154 TITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTK 197
PRK09291 PRK09291
SDR family oxidoreductase;
38-235 1.28e-11

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 63.09  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDM-------EKCEAAAKDIRGETLNHHVnarHLDlaslksiREFAAk 110
Cdd:PRK09291    2 SKTILITGAGSGFGREVALRLARKGHNVIAGVQIApqvtalrAEAARRGLALRVEKLDLTD---AID-------RAQAA- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 111 iieeEERVDILINNAGVMrcphwttEDG--FEM-------QFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVagh 181
Cdd:PRK09291   71 ----EWDVDVLLNNAGIG-------EAGavVDIpvelvreLFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGL--- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 182 idFDDLNWqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK09291  137 --ITGPFT--------GAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-238 1.33e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 62.82  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACR----DMEKCEAAAKDIRGETLNhhVNArhlDLASLKSIREFAAKIIE 113
Cdd:PRK06077    6 DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKkraeEMNETLKMVKENGGEGIG--VLA---DVSTREGCETLAKATID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGV-MRCPHWTTEDGF-EMQFGVNHLGHFLLTNLLLDKLKASApsRIINLSSLAHVaghidfddlnwqt 191
Cdd:PRK06077   81 RYGVADILVNNAGLgLFSPFLNVDDKLiDKHISTDFKSVIYCSQELAKEMREGG--AIVNIASVAGI------------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 192 RKYNTKAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPGVARTELG 238
Cdd:PRK06077  146 RPAYGLSIYGAMKAAVINLTKYLALEL-APKIRVNAIAPGFVKTKLG 191
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 38-237 1.49e-11

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 62.85  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDME-KCEAAAKDIR---GETLnhhvnARHLDLASLKSIREFAAKIIE 113
Cdd:cd09763     3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEargGKCI-----PVRCDHSDDDEVEALFERVAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEE-RVDILINNA--GVMRCPHWTTEDGFEMQ-------FGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAhvaghid 183
Cdd:cd09763    78 EQQgRLDILVNNAyaAVQLILVGVAKPFWEEPptiwddiNNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTG------- 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 184 fddlnWQTRKYNTkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:cd09763   151 -----GLEYLFNV--AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 31-237 1.77e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 62.58  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNH-HVNArhLDL--ASLKSIREF 107
Cdd:PRK08945    5 PKPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQpAIIP--LDLltATPQNYQQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAGVM--RCP--HWTTEDgFE--MQFGVNhlGHFLLTNLLLDKLKASAPSRIINLSSlahVAGH 181
Cdd:PRK08945   83 ADTIEEQFGRLDGVLHNAGLLgeLGPmeQQDPEV-WQdvMQVNVN--ATFMLTQALLPLLLKSPAASLVFTSS---SVGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 182 idfddlnwQTRKYntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK08945  157 --------QGRAN--WGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK05993 PRK05993
SDR family oxidoreductase;
39-244 1.88e-11

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 62.74  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDirGETlnhhvnARHLDLASLKSIREFAAKIIEEEE-R 117
Cdd:PRK05993    5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE--GLE------AFQLDYAEPESIAALVAQVLELSGgR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINN-----AGVMrcphwttED----GFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS-LAHVAghidfddl 187
Cdd:PRK05993   77 LDALFNNgaygqPGAV-------EDlpteALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSiLGLVP-------- 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 188 nwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELgRHTGIH 244
Cdd:PRK05993  142 ------MKYRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF-RANALA 191
PRK07074 PRK07074
SDR family oxidoreductase;
37-236 2.10e-11

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 62.48  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlnhHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK07074    1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDA----RFVPVACDLTDAASLAAALANAAAERG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSL--AHVAGHidfddlnwqtr 192
Cdd:PRK07074   77 PVDVLVANAGAARAAslHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVngMAALGH----------- 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK07074  146 -----PAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 38-131 2.68e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 62.00  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI--EQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGR 78

                          90
                  ....*....|....*
gi 2462495797 118 VDILINN-AGVMRCP 131
Cdd:PRK07677   79 IDALINNaAGNFICP 93
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 38-231 3.93e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 61.62  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07097   10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAH--GYVCDVTDEDGVQAMVSQIEKEVGV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM-RCP--HWTTEDgFEMQFGVNHLGHFlltnlllDKLKASAPS-------RIINLSSLAHVAGHidfddl 187
Cdd:PRK07097   88 IDILVNNAGIIkRIPmlEMSAED-FRQVIDIDLNAPF-------IVSKAVIPSmikkghgKIINICSMMSELGR------ 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 188 nwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK07097  154 -------ETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPG 190
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 38-236 4.21e-11

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 61.37  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05343     6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAG-YPTLFPYQCDLSNEEQILSMFSAIRTQHQG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRcPHW----TTEDGFEMqFGVNHLGHFLLTNLLLDKLKASAPSR--IINLSSlahVAGHIdfddlnwqT 191
Cdd:cd05343    85 VDVCINNAGLAR-PEPllsgKTEGWKEM-FDVNVLALSICTREAYQSMKERNVDDghIININS---MSGHR--------V 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 192 RKYNTKAAYCQSKLAIVLFTKELSRRLQ--GSGVTVNALHPGVARTE 236
Cdd:cd05343   152 PPVSVFHFYAATKHAVTALTEGLRQELReaKTHIRATSISPGLVETE 198
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 38-237 4.37e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 61.32  E-value: 4.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07523   10 GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQ--GLSAHALAFDVTDHDAVRAAIDAFEAEIGP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM-RCP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLahvaghidfddlnwQTRKYN 195
Cdd:PRK07523   88 IDILVNNAGMQfRTPlEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASV--------------QSALAR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 196 TK-AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK07523  154 PGiAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL 196
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 39-235 6.65e-11

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 61.00  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:cd05330     4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVMRCPHWT---TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVaghidfddlnwqtRKYN 195
Cdd:cd05330    84 DGFFNNAGIEGKQNLTedfGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGI-------------RGVG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:cd05330   151 NQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILT 190
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 24-237 6.76e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 61.78  E-value: 6.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  24 YVTG-----GACPSKATI----P--GKTVIVTGANTGIGKQTALELARRGGNIIlaCRDM----EKCEAAAKDIRGETLn 88
Cdd:PRK08261  185 YVSGqvvrvGAADAAPPAdwdrPlaGKVALVTGAARGIGAAIAEVLARDGAHVV--CLDVpaagEALAAVANRVGGTAL- 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  89 hhvnarHLDLASLKSIREFAAKIIEEEERVDILINNAGV--------MrcphwtTEDGFEMQFGVNHLGHFLLTNLLLDK 160
Cdd:PRK08261  262 ------ALDITAPDAPARIAEHLAERHGGLDIVVHNAGItrdktlanM------DEARWDSVLAVNLLAPLRITEALLAA 329

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 161 LKASAPSRIINLSSLAHVAGHIDfddlnwQTrkyNtkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK08261  330 GALGDGGRIVGVSSISGIAGNRG------QT---N----YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 38-231 7.65e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 60.79  E-value: 7.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAkdirgETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08265    6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVA-----ASLGERARFIATDITDDAAIERAVATVVARFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAgvmrCPHwtTEDGFE-------MQFGVNHLGhflltnlLLDKLKASAP------SRIINLSSL-AHVAghid 183
Cdd:PRK08265   81 VDILVNLA----CTY--LDDGLAssradwlAALDVNLVS-------AAMLAQAAHPhlarggGAIVNFTSIsAKFA---- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462495797 184 fddlnwQTrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK08265  144 ------QT----GRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-235 9.07e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 60.36  E-value: 9.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIIlacrdmekceaaAKDIRGETLNH-HVNARHLDLaslksiREFAAKIIEEEE 116
Cdd:PRK06550    5 TKTVLITGAASGIGLAQARAFLAQGAQVY------------GVDKQDKPDLSgNFHFLQLDL------SDDLEPLFDWVP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVM---RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAH-VAGhidfddlnwqtr 192
Cdd:PRK06550   67 SVDILCNTAGILddyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASfVAG------------ 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 193 kyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK06550  135 --GGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKT 175
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 37-236 1.09e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 60.31  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDmekcEAAAKDIrgETLN-HHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRS----EAARADF--EALHpDRALARLLDVTDFDAIDAVVADAEATF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVmrcPHW-----TTEDGFEMQFGVNHLGhflltnlLLDKLKASAPS-------RIINLSSlahVAGHID 183
Cdd:PRK06180   77 GPIDVLVNNAGY---GHEgaieeSPLAEMRRQFEVNVFG-------AVAMTKAVLPGmrarrrgHIVNITS---MGGLIT 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462495797 184 FDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK06180  144 MPGI----------GYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTD 186
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 39-236 1.47e-10

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 59.78  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELAR---RGGNIILACRDMEKCE---AAAKDIRGETLnhhvNARHLDLASLKSIREFAAKIi 112
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKKKGrlwEAAGALAGGTL----ETLQLDVCDSKSVAAAVERV- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 113 eEEERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhIDFDDLnwq 190
Cdd:cd09806    76 -TERHVDVLVCNAGVglLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQG-LPFNDV--- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 191 trkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd09806   151 ---------YCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTA 187
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 38-233 2.41e-10

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 59.00  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDME-------KCEAAAKDIR---GETLNHHVNARHLDlaslkSIREF 107
Cdd:cd09762     3 GKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgTIYTAAEEIEaagGKALPCIVDIRDED-----QVRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAGVMRCPhwTTEDG----FEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahvaghid 183
Cdd:cd09762    78 VEKAVEKFGGIDILVNNASAISLT--GTLDTpmkrYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSP--------- 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 184 fdDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVA 233
Cdd:cd09762   147 --PLNLNPKWFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPRTA 194
PRK06123 PRK06123
SDR family oxidoreductase;
37-246 2.41e-10

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 59.02  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILA-CRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK06123    1 MRKVMIITGASRGIGAATALLAAERGYAVCLNyLRNRDAAEAVVQAIRRQ--GGEALAVAADVADEADVLRLFEAVDREL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGV----MRCPHWtteDGFEMQ--FGVNHLGHFLLTNLLLDKLKASAPSR---IINLSSLAHVAG----HI 182
Cdd:PRK06123   79 GRLDALVNNAGIleaqMRLEQM---DAARLTriFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGspgeYI 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 183 DfddlnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTElgrhtgIHGS 246
Cdd:PRK06123  156 D----------------YAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE------IHAS 197
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 36-237 2.59e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 59.32  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNI-ILACRDMEKCEAAAKDIR---GETLNHHVNarhldLASLKSIREFAAKI 111
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVaIHYGNRKEEAEETVYEIQsngGSAFSIGAN-----LESLHGVEALYSSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 112 IEE------EERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASapSRIINLSSLAHVAGHID 183
Cdd:PRK12747   77 DNElqnrtgSTKFDILINNAGIGPGAfiEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN--SRIINISSAATRISLPD 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 184 FddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12747  155 F-------------IAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 40-239 2.99e-10

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 58.84  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGGNIILAC--RDMEKCEAAAKDIR-GETLNHHVnarhLDLASLKSIREFAAKIIEEEE 116
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSVVVLlaRSEEPLQELKEELRpGLRVTTVK----ADLSDAAGVEQLLEAIRKLDG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRcPH----WTTEDGFEMQFGVN----------HLGHFlltnllldkLKASAPSRIINLSSLAHVaghi 182
Cdd:cd05367    77 ERDLLINNAGSLG-PVskieFIDLDELQKYFDLNltspvcltstLLRAF---------KKRGLKKTVVNVSSGAAV---- 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 183 dfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSrrLQGSGVTVNALHPGVARTELGR 239
Cdd:cd05367   143 ---------NPFKGWGLYCSSKAARDMFFRVLA--AEEPDVRVLSYAPGVVDTDMQR 188
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 38-231 4.10e-10

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 58.36  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDmEKCEAAAKDIRGEtlnhHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADID-EERGADFAEAEGP----NLFFVHGDVADETLVKFVVYAMLEKLGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASApSRIINLSSlahvaghidfddlnwqTRKYN 195
Cdd:cd09761    76 IDVLVNNAARGskGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIAS----------------TRAFQ 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462495797 196 TKA---AYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 231
Cdd:cd09761   139 SEPdseAYAASKGGLVALTHALAMSL-GPDIRVNCISPG 176
PRK06139 PRK06139
SDR family oxidoreductase;
33-127 4.45e-10

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 58.96  E-value: 4.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  33 KATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKII 112
Cdd:PRK06139    2 MGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRA--LGAEVLVVPTDVTDADQVKALATQAA 79

                          90
                  ....*....|....*
gi 2462495797 113 EEEERVDILINNAGV 127
Cdd:PRK06139   80 SFGGRIDVWVNNVGV 94
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
39-237 4.62e-10

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 58.54  E-value: 4.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHvnarHLDLASLKSIREFAAKI---IEEE 115
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLTFH----SLDLQDVHELETNFNEIlssIQED 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDI-LINNAGvMRCPHWTTEDGFEMQFGVN-HLGHFLLTNLLLDKLKASAP----SRIINLSSLAhvaghidfddlnw 189
Cdd:PRK06924   78 NVSSIhLINNAG-MVAPIKPIEKAESEELITNvHLNLLAPMILTSTFMKHTKDwkvdKRVINISSGA------------- 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462495797 190 QTRKYNTKAAYCQSKLAIVLFTK--ELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06924  144 AKNPYFGWSAYCSSKAGLDMFTQtvATEQEEEEYPVKIVAFSPGVMDTNM 193
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 38-126 5.33e-10

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 58.42  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhlDLASLKSIREFAAKIIEEEER 117
Cdd:PRK12823    8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAAGGEALALTA---DLETYAGAQAAMAAAVEAFGR 84


                  ....*....
gi 2462495797 118 VDILINNAG 126
Cdd:PRK12823   85 IDVLINNVG 93
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
38-235 5.33e-10

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 58.35  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGG-----NIILACRDMEKCEAAAK---DIRGetlnhhvnarhlDLASLKSIREFAA 109
Cdd:PRK08993   10 GKVAVVTGCDTGLGQGMALGLAEAGCdivgiNIVEPTETIEQVTALGRrflSLTA------------DLRKIDGIPALLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 110 KIIEEEERVDILINNAGVMRcphwtTEDGFE---------MQFGVNHLgHFLLTNLLLDKLKASAPSRIINLSSLAHVAG 180
Cdd:PRK08993   78 RAVAEFGHIDILVNNAGLIR-----REDAIEfsekdwddvMNLNIKSV-FFMSQAAAKHFIAQGNGGKIINIASMLSFQG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462495797 181 HIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK08993  152 GIRV-------------PSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PRK09186 PRK09186
flagellin modification protein A; Provisional
 38-231 5.60e-10

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 58.08  E-value: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrGETLNHHVNARH-LDLASLKSIREFAAKIIEEEE 116
Cdd:PRK09186    4 GKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESL-GKEFKSKKLSLVeLDITDQESLEEFLSKSAEKYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAgVMRCPHWTT--EDGFEMQFGVN---HLG-HFLLTNLLLDKLKASAPSRIINLSSLAHVAGHiDFDdlNWQ 190
Cdd:PRK09186   83 KIDGAVNCA-YPRNKDYGKkfFDVSLDDFNENlslHLGsSFLFSQQFAKYFKKQGGGNLVNISSIYGVVAP-KFE--IYE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 191 TRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK09186  159 GTSMTSPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
PRK07024 PRK07024
SDR family oxidoreductase;
41-240 6.18e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 58.02  E-value: 6.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETlNHHVNArhLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:PRK07024    5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAA-RVSVYA--ADVRDADALAAAAADFIAAHGLPDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGVMR---CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHV---AGHidfddlnwqtrky 194
Cdd:PRK07024   82 VIANAGISVgtlTEEREDLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVrglPGA------------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 195 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 240
Cdd:PRK07024  149 ---GAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAH 191
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 38-239 7.79e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 57.63  E-value: 7.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR---GETLNHHVNARHLDLAslksiREFAAKIIEE 114
Cdd:PRK07478    6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRaegGEAVALAGDVRDEAYA-----KALVALAVER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRCPHWTTE---DGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS-LAHVAGhidfddlnwq 190
Cdd:PRK07478   81 FGGLDIAFNNAGTLGEMGPVAEmslEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTfVGHTAG---------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 191 trkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK07478  151 ---FPGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGR 196
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 38-239 8.46e-10

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 57.54  E-value: 8.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDmEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd08937     4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILA--AGDAAHVHTADLETYAGAQGVVRAAVERFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAG--VMRCP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHidfddlnwqtrky 194
Cdd:cd08937    81 VDVLINNVGgtIWAKPyEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIY------------- 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 195 ntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:cd08937   148 --RIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRK 190
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 38-235 8.97e-10

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 57.81  E-value: 8.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACR-DMEKCEAAAKDIR---GETLnhhvnARHLDLASLKSIREFAAKIIE 113
Cdd:PRK08936    7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKkagGEAI-----AVKGDVTVESDVVNLIQTAVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGvMRCPHWTTE---DGFEMQFGVNHLGHFLLTNLLLDK-LKASAPSRIINLSSLaHvaghidfDDLNW 189
Cdd:PRK08936   82 EFGTLDVMINNAG-IENAVPSHEmslEDWNKVINTNLTGAFLGSREAIKYfVEHDIKGNIINMSSV-H-------EQIPW 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 190 QTRkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK08936  153 PLF-----VHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 39-236 9.68e-10

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 57.47  E-value: 9.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILA-CRDMEKCEAAAKDIRGETLnhhvnARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNyYRSTESAEAVAAEAGERAI-----AIQADVRDRDQVQAMIEEAKNHFGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNA-------GVMRCPHWTTE-DGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDlnw 189
Cdd:cd05349    76 VDTIVNNAlidfpfdPDQRKTFDTIDwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHD--- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 190 qtrkYNTkaaycqSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:cd05349   153 ----YTT------AKAALLGFTRNMAKELGPYGITVNMVSGGLLKVT 189
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 40-237 1.58e-09

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 56.73  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTAlELARRGGNIILACrdmekceaaakDIRgetlNHHVNArhlDLASLKSIREFAAKIIEEEERV- 118
Cdd:cd05328     1 TIVITGAASGIGAATA-ELLEDAGHTVIGI-----------DLR----EADVIA---DLSTPEGRAAAIADVLARCSGVl 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVmrcPHWTtedGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLN---------- 188
Cdd:cd05328    62 DGLVNCAGV---GGTT---VAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDKLELAkalaagtear 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 189 ----WQTRKYNTKAAYCQSKLAIVLFTKELSRR-LQGSGVTVNALHPGVARTEL 237
Cdd:cd05328   136 avalAEHAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPI 189
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 37-257 1.86e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 56.89  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHH---VNARHLDlaslkSIREFAAKIIE 113
Cdd:PRK05876    5 PGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHgvmCDVRHRE-----EVTHLADEAFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFlltnlllDKLKASAPsRIINLSSLAHVAGHIDFDDLNWQT 191
Cdd:PRK05876   80 LLGHVDVVFSNAGIVVGGPIVemTHDDWRWVIDVDLWGSI-------HTVEAFLP-RLLEQGTGGHVVFTASFAGLVPNA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462495797 192 rkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTG-IHGSTF--SSTTLASKP 257
Cdd:PRK05876  152 ----GLGAYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLVANSErIRGAACaqSSTTGSPGP 216
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 36-237 1.95e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 56.66  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLnhhvnarHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFV-------PTDVTDEDAVNALFDTAAETY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVmrCPhwtTEDGFEMQFG---------VNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfdd 186
Cdd:PRK06057   78 GSVDIAFNNAGI--SP---PEDDSILNTGldawqrvqdVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMG------ 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK06057  147 ------SATSQISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPL 191
PRK08628 PRK08628
SDR family oxidoreductase;
38-230 2.07e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 56.51  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEaAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08628    7 DKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDE-FAEELRALQPRAEFVQ--VDLTDDAQCRDAVEQTVAKFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCPHW-TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSrIINLSSLAHVAGhidfddlnwqtrKYNT 196
Cdd:PRK08628   84 IDGLVNNAGVNDGVGLeAGREAFVASLERNLIHYYVMAHYCLPHLKASRGA-IVNISSKTALTG------------QGGT 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462495797 197 kAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 230
Cdd:PRK08628  151 -SGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK07069 PRK07069
short chain dehydrogenase; Validated
 43-235 2.17e-09

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 56.64  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  43 VTGANTGIGKQTALELARRGGNIILAcrDMEKCEAAAKdirgetLNHHVNARH---------LDLASLKSIREFAAKIIE 113
Cdd:PRK07069    4 ITGAAGGLGRAIARRMAEQGAKVFLT--DINDAAGLDA------FAAEINAAHgegvafaavQDVTDEAQWQALLAQAAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqt 191
Cdd:PRK07069   76 AMGGLSVLVNNAGVGSfgAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISS---VAAFKAEPDY---- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 192 rkyntkAAYCQSKLAIVLFTKELSRRL--QGSGVTVNALHPGVART 235
Cdd:PRK07069  149 ------TAYNASKAAVASLTKSIALDCarRGLDVRCNSIHPTFIRT 188
PRK06947 PRK06947
SDR family oxidoreductase;
39-246 4.04e-09

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 55.58  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNI-ILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAA--GGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMrCPHWTTED----GFEMQFGVNHLGHFLLTNLLL---DKLKASAPSRIINLSSLAHVAGhidfddlnwq 190
Cdd:PRK06947   81 LDALVNNAGIV-APSMPLADmdaaRLRRMFDTNVLGAYLCAREAArrlSTDRGGRGGAIVNVSSIASRLG---------- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462495797 191 trKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTElgrhtgIHGS 246
Cdd:PRK06947  150 --SPNEYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE------IHAS 197
PRK12746 PRK12746
SDR family oxidoreductase;
38-237 4.25e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 55.81  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGniILACRDMEKCEAAAKDIRG-ETLNHHVNARHLDLASLKSIREFAAKIIEE-- 114
Cdd:PRK12746    6 GKVALVTGASRGIGRAIAMRLANDGA--LVAIHYGRNKQAADETIREiESNGGKAFLIEADLNSIDGVKKLVEQLKNElq 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 ----EERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASApsRIINLSSLAHVAGhidfddln 188
Cdd:PRK12746   84 irvgTSEIDILVNNAGIgtQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEG--RVINISSAEVRLG-------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 189 wqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12746  154 -----FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 38-239 4.51e-09

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 55.63  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLAslKSIREFAAKIIEEEER 117
Cdd:cd08936    10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKA--EDRERLVATAVNLHGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMrcPHW-----TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtr 192
Cdd:cd08936    88 VDILVSNAAVN--PFFgnildSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSS---VAAFHPFPGL----- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:cd08936   158 -----GPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSS 199
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 38-236 5.11e-09

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 55.24  E-value: 5.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgeTLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06113   11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQ--QLGGQAFACRCDITSEQELSALADFALSKLGK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRC-PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkynt 196
Cdd:PRK06113   89 VDILVNNAGGGGPkPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINM------------ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462495797 197 kAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK06113  157 -TSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-231 8.31e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 54.70  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGAN--TGIGKQTALELARRGGNIIL---------ACRDMEKCEAAAkdIRGETLNHHVNARHL--DLASLKSI 104
Cdd:PRK12748    5 KKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktMPWGMHDKEPVL--LKEEIESYGVRCEHMeiDLSQPYAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 105 REFAAKIIEEEERVDILINNAGV------------MRCPHWTTE--------DGFEMQFGVNHLGhflltnllldklkas 164
Cdd:PRK12748   83 NRVFYAVSERLGDPSILINNAAYsthtrleeltaeQLDKHYAVNvratmllsSAFAKQYDGKAGG--------------- 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 165 apsRIINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK12748  148 ---RIINLTSGQSLGPMPD-------------ELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 38-235 9.62e-09

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 54.71  E-value: 9.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILAcrDMEkcEAAAKDIRGETLNH-HVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVA--DID--PEIAEKVAEAAQGGpRALGVQCDVTSEAQVQSAFEQAVLEFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKAS--APSRIINLSSLAHVAGhIDFddlnwqtr 192
Cdd:cd08943    77 GLDIVVSNAGIATSSPIaeTSLEDWNRSMDINLTGHFLVSREAFRIMKSQgiGGNIVFNASKNAVAPG-PNA-------- 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP-GVART 235
Cdd:cd08943   148 -----AAYSAAKAAEAHLARCLALEGGEDGIRVNTVNPdAVFRG 186
PRK08267 PRK08267
SDR family oxidoreductase;
39-237 1.02e-08

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 54.56  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDmekcEAAAKDIRGETLNHHVNARHLDL----ASLKSIREFAAkiiEE 114
Cdd:PRK08267    2 KSIFITGAASGIGRATALLFAAEGWRVGAYDIN----EAGLAALAAELGAGNAWTGALDVtdraAWDAALADFAA---AT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtr 192
Cdd:PRK08267   75 GGRLDVLFNNAGILRGGPFEDipLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGL-------- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462495797 193 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK08267  147 -----AVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAM 186
PRK07062 PRK07062
SDR family oxidoreductase;
36-137 1.12e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 54.66  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  36 IPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK07062    6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARF 85

                          90       100
                  ....*....|....*....|....
gi 2462495797 116 ERVDILINNAGVMRCPHW--TTED 137
Cdd:PRK07062   86 GGVDMLVNNAGQGRVSTFadTTDD 109
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 38-127 1.76e-08

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 54.10  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASlkSIREFAAKIIEEEER 117
Cdd:PLN02780   53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSG--DIDEGVKRIKETIEG 130

                          90
                  ....*....|..
gi 2462495797 118 VD--ILINNAGV 127
Cdd:PLN02780  131 LDvgVLINNVGV 142
PRK09135 PRK09135
pteridine reductase; Provisional
 35-240 2.36e-08

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 53.39  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDmekcEAAAKDIRGETLN----HHVNARHLDLASLKSIREFAAK 110
Cdd:PRK09135    3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHR----SAAEADALAAELNalrpGSAAALQADLLDPDALPELVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 111 IIEEEERVDILINNAGVM-RCP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSrIINLSSLahvagHIDfddln 188
Cdd:PRK09135   79 CVAAFGRLDALVNNASSFyPTPlGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGA-IVNITDI-----HAE----- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 189 WQTRKYntkAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG-------------------VARTELGRH 240
Cdd:PRK09135  148 RPLKGY---PVYCAAKAALEMLTRSLALEL-APEVRVNAVAPGailwpedgnsfdeearqaiLARTPLKRI 214
PRK06398 PRK06398
aldose dehydrogenase; Validated
 38-237 2.70e-08

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 53.30  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDmEKCEAAAKDIRGETLNHhvnarhldlaslKSIREFAAKIIEEEER 117
Cdd:PRK06398    6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIK-EPSYNDVDYFKVDVSNK------------EQVIKGIDYVISKYGR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSL-AHVAghidfddlnwqTRKy 194
Cdd:PRK06398   73 IDILVNNAGIESYGaiHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVqSFAV-----------TRN- 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462495797 195 ntKAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPGVARTEL 237
Cdd:PRK06398  141 --AAAYVTSKHAVLGLTRSIAVDY-APTIRCVAVCPGSIRTPL 180
PRK05693 PRK05693
SDR family oxidoreductase;
39-242 5.18e-08

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 52.49  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACR---DMEKCEAAAkdirgetlnhhVNARHLDLASLKSIREFAAKIIEEE 115
Cdd:PRK05693    2 PVVLITGCSSGIGRALADAFKAAGYEVWATARkaeDVEALAAAG-----------FTAVQLDVNDGAALARLAEELEAEH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAG------VMRCPHwtteDGFEMQFGVNhlgHFLLTNLLLDKLKASAPSR--IINLSSLAHV-----AGhi 182
Cdd:PRK05693   71 GGLDVLINNAGygamgpLLDGGV----EAMRRQFETN---VFAVVGVTRALFPLLRRSRglVVNIGSVSGVlvtpfAG-- 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 183 dfddlnwqtrkyntkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTG 242
Cdd:PRK05693  142 ----------------AYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNAS 185
PRK06194 PRK06194
hypothetical protein; Provisional
 37-127 5.95e-08

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 52.33  E-value: 5.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK06194    5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQ--GAEVLGVRTDVSDAAQVEALADAALERFG 82

                          90
                  ....*....|.
gi 2462495797 117 RVDILINNAGV 127
Cdd:PRK06194   83 AVHLLFNNAGV 93
PRK08703 PRK08703
SDR family oxidoreductase;
35-126 5.96e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 52.24  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIrgetlnhhVNARH-------LDL--ASLKSIR 105
Cdd:PRK08703    3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAI--------VEAGHpepfairFDLmsAEEKEFE 74

                          90       100
                  ....*....|....*....|..
gi 2462495797 106 EFAAKIIEEEE-RVDILINNAG 126
Cdd:PRK08703   75 QFAATIAEATQgKLDGIVHCAG 96
PRK08340 PRK08340
SDR family oxidoreductase;
41-130 6.39e-08

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 52.11  E-value: 6.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhlDLASLKSIREFAAKIIEEEERVDI 120
Cdd:PRK08340    3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVYAVKA---DLSDKDDLKNLVKEAWELLGGIDA 79

                          90
                  ....*....|
gi 2462495797 121 LINNAGVMRC 130
Cdd:PRK08340   80 LVWNAGNVRC 89
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-231 6.66e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 52.10  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  34 ATIPGKTVIVTGAN--TGIGKQTALELARRGGNIILAC-----RDM----EKCEAAAKDIRGETLNHHVNARHLDLASLK 102
Cdd:PRK12859    2 NQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTYwtaydKEMpwgvDQDEQIQLQEELLKNGVKVSSMELDLTQND 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 103 SIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS---LAH 177
Cdd:PRK12859   82 APKELLNKVTEQLGYPHILVNNAAYSTNNDFSnlTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSgqfQGP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 178 VAGHIdfddlnwqtrkyntkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK12859  162 MVGEL----------------AYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 38-257 6.76e-08

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 52.26  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGkqtaLELARR----GGNIILACRDMEKCEAAAKDirgetLNHHVNARHLDLASLKSIREFAAKIIE 113
Cdd:PRK06200    6 GQVALITGGGSGIG----RALVERflaeGARVAVLERSAEKLASLRQR-----FGDHVLVVEGDVTSYADNQRAVDQTVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 114 EEERVDILINNAGV-------MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfdd 186
Cdd:PRK06200   77 AFGKLDCFVGNAGIwdyntslVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPG------ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPGVARTELGrhtGIHGSTFSSTTLASKP 257
Cdd:PRK06200  151 --------GGGPLYTASKHAVVGLVRQLAYEL-APKIRVNGVAPGGTVTDLR---GPASLGQGETSISDSP 209
PRK09730 PRK09730
SDR family oxidoreductase;
39-237 7.02e-08

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 52.16  E-value: 7.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILacrDMEKCEAAAKDIRGETLNHHVNARHL--DLASLKSIREFAAKIIEEEE 116
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAV---NYQQNLHAAQEVVNLITQAGGKAFVLqaDISDENQVVAMFTAIDQHDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVM--RCP-HWTTEDGFEMQFGVNHLGHF---LLTNLLLDKLKASAPSRIINLSSLAHVAG----HIDfdd 186
Cdd:PRK09730   79 PLAALVNNAGILftQCTvENLTAERINRVLSTNVTGYFlccREAVKRMALKHGGSGGAIVNVSSAASRLGapgeYVD--- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 187 lnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK09730  156 -------------YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK06114 PRK06114
SDR family oxidoreductase;
38-235 1.01e-07

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 51.71  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIilACRDMEKCEAAAKDI-RGETLNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK06114    8 GQVAFVTGAGSGIGQRIAIGLAQAGADV--ALFDLRTDDGLAETAeHIEAAGRRAIQIAADVTSKADLRAAVARTEAELG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRC-PHWT-TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrky 194
Cdd:PRK06114   86 ALTLAVNAAGIANAnPAEEmEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGL---------- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 195 nTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK06114  156 -LQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK06720 PRK06720
hypothetical protein; Provisional
 33-129 1.76e-07

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 49.97  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  33 KATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR---GETL-NHHVNARHLDLASLKSIrefa 108
Cdd:PRK06720   11 KMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITnlgGEALfVSYDMEKQGDWQRVISI---- 86

                          90       100
                  ....*....|....*....|.
gi 2462495797 109 akIIEEEERVDILINNAGVMR 129
Cdd:PRK06720   87 --TLNAFSRIDMLFQNAGLYK 105
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 38-126 3.71e-07

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 50.69  E-value: 3.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:COG3347   425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFGFAGLDIGG 504


                  ....*....
gi 2462495797 118 VDILINNAG 126
Cdd:COG3347   505 SDIGVANAG 513
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
43-237 3.95e-07

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 49.63  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  43 VTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDiRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILI 122
Cdd:PRK12938    8 VTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLE-DQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDVLV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 123 NNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHidFDDLNWQTrkyntkaay 200
Cdd:PRK12938   87 NNAGITRdvVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQ--FGQTNYST--------- 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462495797 201 cqSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK12938  156 --AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
PRK08177 PRK08177
SDR family oxidoreductase;
39-238 5.74e-07

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 49.26  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEA--AAKDIRGETlnhhvnarhLDLASLKSIREFAAKIieEEE 116
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTAlqALPGVHIEK---------LDMNDPASLDQLLQRL--QGQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVDILINNAGVMRCPHWTTEDGFEMQFGVNHLghflltnllldkLKASAPSRI-------IN------------LSSLAH 177
Cdd:PRK08177   71 RFDLLFVNAGISGPAHQSAADATAAEIGQLFL------------TNAIAPIRLarrllgqVRpgqgvlafmssqLGSVEL 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 178 VAGhidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 238
Cdd:PRK08177  139 PDG--------------GEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMG 185
PLN02253 PLN02253
xanthoxin dehydrogenase
 28-237 6.52e-07

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 49.44  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  28 GACPSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlnHHVNARHLDLASLKSIREF 107
Cdd:PLN02253    8 ASSLPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGE---PNVCFFHCDVTVEDDVSRA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAGVM--RCPHWTTED--GFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHID 183
Cdd:PLN02253   85 VDFTVDKFGTLDIMVNNAGLTgpPCPDIRNVElsEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462495797 184 fddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PLN02253  165 -------------PHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL 205
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 38-231 7.15e-07

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 49.27  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlnhHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:cd05348     4 GEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGD-----AVVGVEGDVRSLADNERAVARCVERFGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGV-------MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwq 190
Cdd:cd05348    79 LDCFIGNAGIwdystslVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPG---------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462495797 191 trkyNTKAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 231
Cdd:cd05348   149 ----GGGPLYTASKHAVVGLVKQLAYEL-APHIRVNGVAPG 184
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 38-231 8.82e-07

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 49.00  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlnHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:cd05322     2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAE---YGEKAYGFgaDATNEQSVIALSKGVDEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAGVMRCPHWTT---EDgFEMQFGVNHLGHFLLTNLLLDKL-KASAPSRIINLSSLAHVAGhidfddlnwqt 191
Cdd:cd05322    79 KRVDLLVYSAGIAKSAKITDfelGD-FDRSLQVNLVGYFLCAREFSKLMiRDGIQGRIIQINSKSGKVG----------- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462495797 192 RKYNTkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:cd05322   147 SKHNS--GYSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 42-237 1.94e-06

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 47.98  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  42 IVTGANTGIGKQTALELARR----GGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFaAKIIEEEER 117
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQL-LKALRELPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VD-----ILINNAGVMrcphWTTEDGFEmQFG-------VNHLGHFLLTNLLLDKLKA-----SAPSRIINLSSLAHVAg 180
Cdd:TIGR01500  83 PKglqrlLLINNAGTL----GDVSKGFV-DLSdstqvqnYWALNLTSMLCLTSSVLKAfkdspGLNRTVVNISSLCAIQ- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495797 181 hidfddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:TIGR01500 157 ------------PFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM 201
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 38-125 2.86e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 47.26  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGEtlnhhvNARHLDLASlkSIREFAA------KI 111
Cdd:PRK07576    9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQA------GPEGLGVSA--DVRDYAAveaafaQI 80

                          90
                  ....*....|....
gi 2462495797 112 IEEEERVDILINNA 125
Cdd:PRK07576   81 ADEFGPIDVLVSGA 94
PRK07831 PRK07831
SDR family oxidoreductase;
38-126 3.75e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 46.95  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGA-NTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:PRK07831   17 GKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGRVEAVVCDVTSEAQVDALIDAAVERLG 96

                          90
                  ....*....|
gi 2462495797 117 RVDILINNAG 126
Cdd:PRK07831   97 RLDVLVNNAG 106
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 39-237 4.68e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 46.72  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERV 118
Cdd:PRK05875    8 RTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAATAWHGRL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVMRCPHWTTE---DGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyn 195
Cdd:PRK05875   88 HGVVHCAGGSETIGPITQidsDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWF----------- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 196 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK05875  157 --GAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 13-83 6.76e-06

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 45.46  E-value: 6.76e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462495797  13 TVAGAAVLLkdyVTGGACPSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIR 83
Cdd:cd01078     6 TTAAAAVAA---AGKALELMGKDLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLR 73
PRK07102 PRK07102
SDR family oxidoreductase;
38-107 8.65e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 45.69  E-value: 8.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNhHVNARHLDLASLKSIREF 107
Cdd:PRK07102    1 MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAV-AVSTHELDILDTASHAAF 69
PRK07806 PRK07806
SDR family oxidoreductase;
34-125 9.10e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 45.87  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  34 ATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRD-MEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKII 112
Cdd:PRK07806    2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkAPRANKVVAEIEAA--GGRASAVGADLTDEESVAALMDTAR 79

                          90
                  ....*....|...
gi 2462495797 113 EEEERVDILINNA 125
Cdd:PRK07806   80 EEFGGLDALVLNA 92
PRK08416 PRK08416
enoyl-ACP reductase;
38-125 1.12e-05

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 45.53  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEkcEAAAKDIRGETLNHHVNARH--LDLASLKSIREFAAKIIEEE 115
Cdd:PRK08416    8 GKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNV--EEANKIAEDLEQKYGIKAKAypLNILEPETYKELFKKIDEDF 85

                          90
                  ....*....|
gi 2462495797 116 ERVDILINNA 125
Cdd:PRK08416   86 DRVDFFISNA 95
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 38-236 1.16e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 45.28  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRdmekceAAAKDIRGEtlNHHVNArhlDLASLKSIREFAAKIIEEEER 117
Cdd:PRK06523    9 GKRALVTGGTKGIGAATVARLLEAGARVVTTAR------SRPDDLPEG--VEFVAA---DLTTAEGCAAVARAVLERLGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMRCP----------HWTTEdgfemqFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLahvaghidfddl 187
Cdd:PRK06523   78 VDILVHVLGGSSAPaggfaaltdeEWQDE------LNLNLLAAVRLDRALLPGMIARGSGVIIHVTSI------------ 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 188 nwQTR--KYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 236
Cdd:PRK06523  140 --QRRlpLPESTTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 38-237 1.27e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 45.41  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAkdirgETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK08263    3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLA-----EKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNAGVMR-CP-HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrkYN 195
Cdd:PRK08263   78 LDIVVNNAGYGLfGMiEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISA-------------FP 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462495797 196 TKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK08263  145 MSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDW 186
PRK08219 PRK08219
SDR family oxidoreductase;
39-127 1.73e-05

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 44.54  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRgGNIILACRDMEKCEAAAKDIRGETlnhhvnARHLDLASLKSIREFAAKIieeeERV 118
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPGAT------PFPVDLTDPEAIAAAVEQL----GRL 72


                  ....*....
gi 2462495797 119 DILINNAGV 127
Cdd:PRK08219   73 DVLVHNAGV 81
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 41-236 2.04e-05

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 44.75  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAaKDIRGETLnHHVnarHLDLASLKSIREFAAKIIEEEERVDI 120
Cdd:PRK10538    3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQEL-KDELGDNL-YIA---QLDVRNRAAIEEMLASLPAEWRNIDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 121 LINNAGV---MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHvaghidfddlNWqtrKYNTK 197
Cdd:PRK10538   78 LVNNAGLalgLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAG----------SW---PYAGG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462495797 198 AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG-VARTE 236
Cdd:PRK10538  145 NVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGlVGGTE 184
PRK07985 PRK07985
SDR family oxidoreductase;
38-237 3.33e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 44.22  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRDMEkcEAAAKDIRGETLNHHVNARHL--DLASLKSIREFAAKIIEEE 115
Cdd:PRK07985   49 DRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVE--EEDAQDVKKIIEECGRKAVLLpgDLSDEKFARSLVHEAHKAL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 116 ERVDILINNAG----VMRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASApsRIINLSSLAHVAGHIDFDDlnwqt 191
Cdd:PRK07985  127 GGLDIMALVAGkqvaIPDIADLTSEQ-FQKTFAINVFALFWLTQEAIPLLPKGA--SIITTSSIQAYQPSPHLLD----- 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 192 rkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 237
Cdd:PRK07985  199 --------YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK12744 PRK12744
SDR family oxidoreductase;
35-231 3.85e-05

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 43.96  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  35 TIPGKTVIVTGANTGIGKQTALELARRGGNIIL------ACR-DMEKCEAAAKDIRGETLnhhvnARHLDLASLKSIREF 107
Cdd:PRK12744    5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynsaASKaDAEETVAAVKAAGAKAV-----AFQADLTTAAAVEKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 108 AAKIIEEEERVDILINNAG-VMRCPHW-TTEDGFEMQFGVNHLGHFllTNLLLDKLKASAPSRIINL-SSLahVAGHIDF 184
Cdd:PRK12744   80 FDDAKAAFGRPDIAINTVGkVLKKPIVeISEAEYDEMFAVNSKSAF--FFIKEAGRHLNDNGKIVTLvTSL--LGAFTPF 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 185 ddlnwqtrkYntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 231
Cdd:PRK12744  156 ---------Y---SAYAGSKAPVEHFTRAASKEFGARGISVTAVGPG 190
KR_fFAS_like_SDR_c_like cd08928
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ...
 41-238 4.00e-05

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187633 [Multi-domain]  Cd Length: 248  Bit Score: 43.82  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTG-IGKQTALELARRGGNIILACRDMEKCEA-------AAKDIRGETLNhhvnarhLDLASLKSIREFAAKII 112
Cdd:cd08928     1 VLITGAGDGsIGAEVLQGLLNGGAKVYVTTSRFSRQVTkyyqdiyAACGAAGSVLI-------VVPFNQGSKQDVEALAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 113 EEEERVDILINnAGVMRCPHWTT-EDGFEMQF--GVNHLGHFLLTNLLLDklkasaPSRIINLSSLAHVAGHIDFDDLNW 189
Cdd:cd08928    74 GIYDTVNGLGW-DLDLYGPFAAIpETGIEIPAidSKSEVAHRIMLTNLLR------PKGLVKIQKQLRGQETRPAQVILP 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462495797 190 QTRKYNT---KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 238
Cdd:cd08928   147 FSPNHGTfgdDGAYSESKLHLETLFNRWASESWGNDLTVCGAHIGWTRGTLG 198
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 39-235 9.36e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 42.77  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILacrDMEKCEAAAKDIRGEtLNHHVNARHLDLASLKSIREFAAKIIEE-EER 117
Cdd:PRK08642    6 QTVLVTGGSRGLGAAIARAFAREGARVVV---NYHQSEDAAEALADE-LGDRAIALQADVTDREQVQAMFATATEHfGKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 118 VDILINNA-------GVMR-CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDlnw 189
Cdd:PRK08642   82 ITTVVNNAladfsfdGDARkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHD--- 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462495797 190 qtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:PRK08642  159 ----------YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK09134 PRK09134
SDR family oxidoreductase;
31-135 9.58e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 42.61  E-value: 9.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRD-MEKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAA 109
Cdd:PRK09134    2 PPMSMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVHYNRsRDEAEALAAEIRALGRRAV--ALQADLADEAEVRALVA 79

                          90       100
                  ....*....|....*....|....*.
gi 2462495797 110 KIIEEEERVDILINNAGVMRCPHWTT 135
Cdd:PRK09134   80 RASAALGPITLLVNNASLFEYDSAAS 105
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 37-127 1.05e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 42.70  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANtGIGKQtaleLARR---GGNIILACRDMEKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKiIE 113
Cdd:PRK06940    1 MKEVVVVIGAG-GIGQA----IARRvgaGKKVLLADYNEENLEAAAKTLREA--GFDVSTQEVDVSSRESVKALAAT-AQ 72

                          90
                  ....*....|....
gi 2462495797 114 EEERVDILINNAGV 127
Cdd:PRK06940   73 TLGPVTGLVHTAGV 86
PRK06482 PRK06482
SDR family oxidoreductase;
38-239 1.11e-04

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 42.80  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRdmekcEAAAKDirgETLNHHVNARH---LDLASLKSIREFAAKIIEE 114
Cdd:PRK06482    2 SKTWFITGASSGFGRGMTERLLARGDRVAATVR-----RPDALD---DLKARYGDRLWvlqLDVTDSAAVRAVVDRAFAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 115 EERVDILINNAG--VMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLahvAGHIdfddlnwqtr 192
Cdd:PRK06482   74 LGRIDVVVSNAGygLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSE---GGQI---------- 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 193 KYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 239
Cdd:PRK06482  141 AYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGA 187
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
41-126 1.28e-04

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 42.52  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVnarhLDLASLKSIREFAAkiieeeeRVDI 120
Cdd:COG3268     8 IVVYGATGYTGRLVAEYLARRGLRPALAGRNAAKLEAVAAELGAADLPLRV----ADLDDPASLAALLA-------GTRV 76


                  ....*.
gi 2462495797 121 LINNAG 126
Cdd:COG3268    77 VLNTVG 82
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 25-129 1.90e-04

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 42.35  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  25 VTGGACPSKATIPGKTVIVTGANTGIGKQTALELARRGG-NIILACR---DMEKCEAAAKDIRGETLNHHVNARHLDLAS 100
Cdd:cd08953   192 LPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGaRLVLLGRsplPPEEEWKAQTLAALEALGARVLYISADVTD 271

                          90       100
                  ....*....|....*....|....*....
gi 2462495797 101 LKSIREFAAKIIEEEERVDILINNAGVMR 129
Cdd:cd08953   272 AAAVRRLLEKVRERYGAIDGVIHAAGVLR 300
PRK07856 PRK07856
SDR family oxidoreductase;
38-126 2.09e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 41.46  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIILACRdmekceAAAKDIRGETLNHHVnarhLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07856    6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGR------RAPETVDGRPAEFHA----ADVRDPDQVAALVDAIVERHGR 75


                  ....*....
gi 2462495797 118 VDILINNAG 126
Cdd:PRK07856   76 LDVLVNNAG 84
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 41-146 3.75e-04

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 40.64  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILACRDmekceaaakdiRGEtlnhhvnaRHLDLASLKSIREFAAKIieeeERVDI 120
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRS-----------SGD--------YQVDITDEASIKALFEKV----GHFDA 57

                          90       100
                  ....*....|....*....|....*.
gi 2462495797 121 LINNAGVMRCPHWTTEDGFEMQFGVN 146
Cdd:cd11731    58 IVSTAGDAEFAPLAELTDADFQRGLN 83
PRK05717 PRK05717
SDR family oxidoreductase;
31-231 3.91e-04

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 41.03  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKdirgeTLNHHVNARHLDLASLKSIREFAAK 110
Cdd:PRK05717    3 EPNPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAK-----ALGENAWFIAMDVADEAQVAAGVAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 111 IIEEEERVDILINNAGVMRcPHWTTEDGFEMQ-----FGVNHLGHFLLTNLLLDKLKASAPSrIINLSSlahvaghidfd 185
Cdd:PRK05717   78 VLGQFGRLDALVCNAAIAD-PHNTTLESLSLAhwnrvLAVNLTGPMLLAKHCAPYLRAHNGA-IVNLAS----------- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462495797 186 dlnwqTRKYNTKA---AYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 231
Cdd:PRK05717  145 -----TRARQSEPdteAYAASKGGLLALTHALAISL-GPEIRVNAVSPG 187
PRK08251 PRK08251
SDR family oxidoreductase;
39-127 6.09e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 40.30  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAaakdIRGETLNHH----VNARHLDL----ASLKSIREFAAk 110
Cdd:PRK08251    3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEE----LKAELLARYpgikVAVAALDVndhdQVFEVFAEFRD- 77

                          90
                  ....*....|....*..
gi 2462495797 111 iieEEERVDILINNAGV 127
Cdd:PRK08251   78 ---ELGGLDRVIVNAGI 91
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 41-123 7.78e-04

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 38.34  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANtGIGKQTALELARRG--GNIILACRDMEKCEAAAKDIRGETlnhhVNARHLDLASLKSIrefAAKIIEEeerV 118
Cdd:pfam03435   1 VLIIGAG-SVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVR----FIAVAVDADNYEAV---LAALLKE---G 69


                  ....*
gi 2462495797 119 DILIN 123
Cdd:pfam03435  70 DLVVN 74
PRK06953 PRK06953
SDR family oxidoreductase;
39-238 1.16e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 39.28  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  39 KTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAakdirgETLNHHVNArhLDLASLKSIREFAAKIieEEERV 118
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAAL------QALGAEALA--LDVADPASVAGLAWKL--DGEAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 DILINNAGVM-----RCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASA------PSRiinLSSLAHVAGhidfddl 187
Cdd:PRK06953   72 DAAVYVAGVYgprteGVEPITRED-FDAVMHTNVLGPMQLLPILLPLVEAAGgvlavlSSR---MGSIGDATG------- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462495797 188 nwqtrkyNTKAAYCQSKLAIVLFTKELSrrLQGSGVTVNALHPGVARTELG 238
Cdd:PRK06953  141 -------TTGWLYRASKAALNDALRAAS--LQARHATCIALHPGWVRTDMG 182
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
40-86 1.22e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 39.82  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGET 86
Cdd:COG5322   153 TVAVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNP 199
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 39-129 1.24e-03

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.62  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797   39 KTVIVTGANTGIGKQTALELARRGG-NIILACRDMEKCEAAAKDIRG-ETLNHHVNARHLDLASLKSIREFAAKIIEEEE 116
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAElEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80

                           90
                   ....*....|...
gi 2462495797  117 RVDILINNAGVMR 129
Cdd:smart00822  81 PLTGVIHAAGVLD 93
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 38-127 1.50e-03

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 39.29  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRGGNIIlacrdmekceaaAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:PRK07424  178 GKTVAVTGASGTLGQALLKELHQQGAKVV------------ALTSNSDKITLEINGEDLPVKTLHWQVGQEAALAELLEK 245

                          90
                  ....*....|
gi 2462495797 118 VDILINNAGV 127
Cdd:PRK07424  246 VDILIINHGI 255
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 40-129 1.76e-03

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 38.31  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGG-NIILACRDMEKCEAAAKDIRG-ETLNHHVNARHLDLASLKSIREFAAKIIEEEER 117
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQALIAElEARGVEVVVVACDVSDPDAVAALLAEIKAEGPP 81

                          90
                  ....*....|..
gi 2462495797 118 VDILINNAGVMR 129
Cdd:pfam08659  82 IRGVIHAAGVLR 93
PRK07041 PRK07041
SDR family oxidoreductase;
42-119 1.79e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 38.86  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462495797  42 IVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGetlNHHVNARHLDLASLKSIREFAAkiieEEERVD 119
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGG---GAPVRTAALDITDEAAVDAFFA----EAGPFD 71
PRK07023 PRK07023
SDR family oxidoreductase;
42-235 2.02e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 38.46  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  42 IVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAkdiRGETLNHHvnarHLDLASLKSIREFAAKIIEEE-----E 116
Cdd:PRK07023    5 IVTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSLAAA---AGERLAEV----ELDLSDAAAAAAWLAGDLLAAfvdgaS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 117 RVdILINNAGVMRcP--HWTTEDGFEMQ--FGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAH---VAGhidfddlnW 189
Cdd:PRK07023   78 RV-LLINNAGTVE-PigPLATLDAAAIAraVGLNVAAPLMLTAALAQAASDAAERRILHISSGAArnaYAG--------W 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462495797 190 qtrkyntkAAYCQSKLAIVLFTKELSrrLQGS-GVTVNALHPGVART 235
Cdd:PRK07023  148 --------SVYCATKAALDHHARAVA--LDANrALRIVSLAPGVVDT 184
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 37-126 3.23e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.21  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGANTGIGkQTALELAR-RGGNIILACRDMEKCEAAAK---DirgetlnHHVNARHLDLAslKSIREFAAKii 112
Cdd:COG0604   139 PGETVLVHGAAGGVG-SAAVQLAKaLGARVIATASSPEKAELLRAlgaD-------HVIDYREEDFA--ERVRALTGG-- 206

                          90
                  ....*....|....
gi 2462495797 113 eeeERVDILINNAG 126
Cdd:COG0604   207 ---RGVDVVLDTVG 217
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
40-149 5.99e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 37.27  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRgetlnhhVNARHLDLASLKSIREFAakiieeeERVD 119
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPG-------VEFVRGDLRDPEALAAAL-------AGVD 66

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462495797 120 ILINNAGvmrcPHWTTEDGFEMQFGVNHLG 149
Cdd:COG0451    67 AVVHLAA----PAGVGEEDPDETLEVNVEG 92
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 38-125 5.99e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 37.21  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  38 GKTVIVTGANTGIGKQTALELARRG-GNIILACRDMEKCEAAAKDIRGetLNHHVNARHLDLaslkSIREFAA-KIIEEE 115
Cdd:cd05237     2 GKTILVTGGAGSIGSELVRQILKFGpKKLIVFDRDENKLHELVRELRS--RFPHDKLRFIIG----DVRDKERlRRAFKE 75

                          90
                  ....*....|
gi 2462495797 116 ERVDILINNA 125
Cdd:cd05237    76 RGPDIVFHAA 85
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 5-83 6.52e-03

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 37.20  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797   5 LLPLSALGTVAGAAV----------LLKDYVTGGacpskatiPGKTVIVTGANTGIGkQTALELAR-RGGNIILACRDME 73
Cdd:cd08290   112 LIKVPNDVDPEQAATlsvnpctayrLLEDFVKLQ--------PGDWVIQNGANSAVG-QAVIQLAKlLGIKTINVVRDRP 182

                          90
                  ....*....|
gi 2462495797  74 KCEAAAKDIR 83
Cdd:cd08290   183 DLEELKERLK 192
PRK06101 PRK06101
SDR family oxidoreductase;
40-69 6.58e-03

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 37.16  E-value: 6.58e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462495797  40 TVIVTGANTGIGKQTALELARRGGNIIlAC 69
Cdd:PRK06101    3 AVLITGATSGIGKQLALDYAKQGWQVI-AC 31
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 37-126 6.66e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 37.30  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  37 PGKTVIVTGAnTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNArhldlaslksirEFAAKIIEEEE 116
Cdd:cd05188   134 PGDTVLVLGA-GGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEED------------LEEELRLTGGG 200

                          90
                  ....*....|
gi 2462495797 117 RVDILINNAG 126
Cdd:cd05188   201 GADVVIDAVG 210
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 31-124 8.34e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 36.90  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  31 PSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEkceAAAKDI-RGETLNHH-------------VNARHL 96
Cdd:PRK08303    1 PMMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTR---ARRSEYdRPETIEETaelvtaaggrgiaVQVDHL 77

                          90       100
                  ....*....|....*....|....*...
gi 2462495797  97 DLASlksIREFAAKIIEEEERVDILINN 124
Cdd:PRK08303   78 VPEQ---VRALVERIDREQGRLDILVND 102
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 41-235 9.72e-03

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 36.34  E-value: 9.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797  41 VIVTGANTGIGKQTALELARRGGNIILAC--RDMEKCEAAAKDirgetlnhhvNARHLDLASLKSirefaakiieeeERV 118
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRGSPKVLVVsrRDVVVHNAAILD----------DGRLIDLTGSRI------------ERA 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495797 119 dILINNAGVMRCPHWTTEDgfemqfgvnhlghflltnllldkLKASAPSRIINLSSLAHVAGHIdFDDLnwqtrkyntka 198
Cdd:cd02266    59 -IRANVVGTRRLLEAAREL-----------------------MKAKRLGRFILISSVAGLFGAP-GLGG----------- 102

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462495797 199 aYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 235
Cdd:cd02266   103 -YAASKAALDGLAQQWASEGWGNGLPATAVACGTWAG 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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