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Conserved domains on  [gi|557948119|ref|NP_001273718|]
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carbonyl reductase [NADPH] 1 isoform 2 [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 ...
 6-131 2.86e-76

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 cd05324:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 225  Bit Score: 227.12  E-value: 2.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  86 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP 131
Cdd:cd05324   81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKK 127
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-131 2.86e-76

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: 227.12  E-value: 2.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  86 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP 131
Cdd:cd05324   81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKK 127
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-132 5.79e-31

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: 112.19  E-value: 5.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:COG1028    8 VALVTGGSSGIGRAIARALAA--EGaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAGIafkvADPTPFH-IQAEV---TMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:COG1028   86 ILVNNAGI----TPPGPLEeLTEEDwdrVLDVNLKGPFLLTRAALPHMRER 132
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-134 6.97e-27

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 100.38  E-value: 6.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    7 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:pfam00106   2 VALVTGASSGIGRAIAK---RLAKegAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557948119   85 DVLVNNAGIafkvADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:pfam00106  79 DILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPAMIKGSG 128
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 7-130 1.31e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 85.02  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAE--AGaTVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  86 VLVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIK 130
Cdd:PRK12939  87 GLVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLR 131
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 8-93 5.25e-15

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 69.93  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    8 ALVTGGNKGIGLAIVRDLCRLFSgDVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79


                  ....*..
gi 557948119   87 LVNNAGI 93
Cdd:TIGR01830  80 LVNNAGI 86
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-93 3.19e-08

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: 50.56  E-value: 3.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119     9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTAR---DVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83


                   ....*...
gi 557948119    86 VLVNNAGI 93
Cdd:smart00822  84 GVIHAAGV 91
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-131 2.86e-76

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: 227.12  E-value: 2.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  86 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP 131
Cdd:cd05324   81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKK 127
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-132 5.79e-31

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: 112.19  E-value: 5.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:COG1028    8 VALVTGGSSGIGRAIARALAA--EGaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAGIafkvADPTPFH-IQAEV---TMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:COG1028   86 ILVNNAGI----TPPGPLEeLTEEDwdrVLDVNLKGPFLLTRAALPHMRER 132
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-134 7.10e-30

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 109.57  E-value: 7.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   1 MSSGIHVALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:COG0300    1 MSLTGKTVLITGASSGIGRALARALAAR--GaRVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557948119  80 EYGGLDVLVNNAGIAF--KVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:COG0300   79 RFGPIDVLVNNAGVGGggPFEELDLEDLRR--VFEVNVFGPVRLTRALLPLMRARGR 133
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-134 6.97e-27

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 100.38  E-value: 6.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    7 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:pfam00106   2 VALVTGASSGIGRAIAK---RLAKegAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557948119   85 DVLVNNAGIafkvADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:pfam00106  79 DILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPAMIKGSG 128
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-132 3.08e-26

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: 99.67  E-value: 3.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQqLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAR--EGaKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557948119  87 LVNNAGIAFkvaDPTPFHIQAEV---TMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd05233   78 LVNNAGIAR---PGPLEELTDEDwdrVLDVNLTGVFLLTRAALPHMKKQ 123
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-134 3.88e-24

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: 94.09  E-value: 3.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   1 MSSGIHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:COG4221    1 MSDKGKVALITGASSGIGAATARALAA--AGaRVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVA 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557948119  80 EYGGLDVLVNNAGIAF--KVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:COG4221   76 EFGRLDVLVNNAGVALlgPLEELDPEDWDR--MIDVNVKGVLYVTRAALPAMRARGS 130
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-132 1.30e-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: 90.22  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDvtrgQAAVQQLQAEglSPRFH--QLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:COG3967    9 LITGGTSGIGLALAKRLHAR--GnTVIITGRR----EEKLEEAAAA--NPGLHtiVLDVADPASIAALAEQVTAEFPDLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557948119  86 VLVNNAGI--AFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:COG3967   81 VLINNAGImrAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQ 129
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-135 1.07e-21

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: 88.44  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05327    3 VVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPRL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  85 DVLVNNAGIAFKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIKPQASC 135
Cdd:cd05327   82 DILINNAGIMAPPRRLTKDGF--ELQFAVNYLGHFLLTNLLLPVLKASAPS 130
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 7-130 1.31e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 85.02  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAE--AGaTVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  86 VLVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIK 130
Cdd:PRK12939  87 GLVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLR 131
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-104 1.56e-20

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 84.83  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK05653   7 TALVTGASRGIGRAIALRLAAD--GaKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84

                         90
                 ....*....|....*....
gi 557948119  86 VLVNNAGIafkvADPTPFH 104
Cdd:PRK05653  85 ILVNNAGI----TRDALLP 99
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 6-134 3.36e-20

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: 83.82  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSGDVVL-TARDVTrgqaAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAA--QGYRVIaTARNPD----KLESLGEL-LNDNLEvlELDVTDEESIKAAVKEVIERFG 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557948119  83 GLDVLVNNAGIA-FKVADPTPFHiQAEVTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:cd05374   74 RIDVLVNNAGYGlFGPLEETSIE-EVRELFEVNVFGPLRVTRAFLPLMRKQGS 125
FabG-like PRK07231
SDR family oxidoreductase;
6-119 7.05e-20

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 83.34  E-value: 7.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSpRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAA--EGaRVVVTDRNEEAAERVAAEILAGGRA-IAVAADVSDEADVEAAVAAALERFGSV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 557948119  85 DVLVNNAGI--AFKV---ADPTPFHIQAEVTMKTNFFGTR 119
Cdd:PRK07231  83 DILVNNAGTthRNGPlldVDEAEFDRIFAVNVKSPYLWTQ 122
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 8-133 9.63e-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: 82.35  E-value: 9.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLFSgDVVLTARDvtrgQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:cd05370    8 VLITGGTSGIGLALARKFLEAGN-TVIITGRR----EERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDIL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557948119  88 VNNAGIA--FKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQA 133
Cdd:cd05370   83 INNAGIQrpIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQP 130
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 7-93 7.30e-19

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: 80.28  E-value: 7.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05333    2 VALVTGASRGIGRAIALRLAA--EGaKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:cd05333   80 ILVNNAGI 87
PRK09242 PRK09242
SDR family oxidoreductase;
8-134 1.22e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 80.18  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQL--DIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK09242  12 ALITGASKGIGLAIAREFLGL-GADVLIVARDADALAQARDELAEEFPEREVHGLaaDVSDDEDRRAILDWVEDHWDGLH 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAG--IAFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK09242  91 ILVNNAGgnIRKAAIDYTEDEWRG--IFETNLFSAFELSRYAHPLLKQHAS 139
PRK07326 PRK07326
SDR family oxidoreductase;
1-117 5.92e-18

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 77.74  E-value: 5.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   1 MSSGIHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGlspRFHQL--DIDDLQSIRALRDFL 77
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLA--EGyKVAITARDQKELEEAAAELNNKG---NVLGLaaDVRDEADVQRAVDAI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 557948119  78 RKEYGGLDVLVNNAGIA-FK-VADPTPFHIQAevTMKTNFFG 117
Cdd:PRK07326  77 VAAFGGLDVLIANAGVGhFApVEELTPEEWRL--VIDTNLTG 116
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-94 1.12e-17

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 77.16  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05557   7 VALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDI 86


                 ....*...
gi 557948119  87 LVNNAGIA 94
Cdd:PRK05557  87 LVNNAGIT 94
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-150 1.75e-17

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: 76.39  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLFSGdVVLTARDVTRGQAAVQQLQaeglsPRFHQL--DIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYR-VGICARDEARLAAAAAQEL-----EGVLGLagDVRDEADVRRAVDAMEEAFGGLD 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557948119  86 VLVNNAGIAF--KVADPTPFHIQAEV--TMKTNFFGTRDVcteLLPLIKPQASCVLSAWSCLSQNPSGG 150
Cdd:cd08929   77 ALVNNAGVGVmkPVEELTPEEWRLVLdtNLTGAFYCIHKA---APALLRRGGGTIVNVGSLAGKNAFKG 142
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-94 1.77e-17

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 76.83  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTAR-DVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12825   8 VALVTGAARGLGRAIALRLAR--AGaDVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRI 85

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:PRK12825  86 DILVNNAGIF 95
PRK12826 PRK12826
SDR family oxidoreductase;
7-137 2.21e-17

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 76.49  E-value: 2.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAA--DGaEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557948119  86 VLVNNAGIafkvADPTPFHI----QAEVTMKTNFFGTRDVCTELLP-LIKPQASCVL 137
Cdd:PRK12826  86 ILVANAGI----FPLTPFAEmddeQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIV 138
PRK08264 PRK08264
SDR family oxidoreductase;
7-157 2.43e-17

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 76.08  E-value: 2.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARD---VTRGQAAVQQLqaeglsprfhQLDIDDLQSIRALRDFLrkeyGG 83
Cdd:PRK08264   8 VVLVTGANRGIGRAFVEQLLARGAAKVYAAARDpesVTDLGPRVVPL----------QLDVTDPASVAAAAEAA----SD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  84 LDVLVNNAGIAFK---VADPTPFHIQAEvtMKTNFFGTRDVCTELLPLIKPQASC----VLS--AWSCLSQNPSGGKSKP 154
Cdd:PRK08264  74 VTILVNNAGIFRTgslLLEGDEDALRAE--METNYFGPLAMARAFAPVLAANGGGaivnVLSvlSWVNFPNLGTYSASKA 151


                 ...
gi 557948119 155 LAW 157
Cdd:PRK08264 152 AAW 154
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 7-121 5.47e-17

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: 75.50  E-value: 5.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05341    7 VAIVTGGARGLGLAHARLLVAE-GAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLDV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 557948119  87 LVNNAGIAfkvadpTPFHIQAEV------TMKTN----FFGTRDV 121
Cdd:cd05341   83 LVNNAGIL------TGGTVETTTleewrrLLDINltgvFLGTRAV 121
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-97 9.25e-17

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 75.00  E-value: 9.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTA-RDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAA--AGfDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRI 81

                         90
                 ....*....|...
gi 557948119  85 DVLVNNAGIAFKV 97
Cdd:PRK12745  82 DCLVNNAGVGVKV 94
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-134 1.42e-16

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: 74.00  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   14 NKGIGLAIVRDLCRlfSG-DVVLTARDvTRGQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAG 92
Cdd:pfam13561   5 ESGIGWAIARALAE--EGaEVVLTDLN-EALAKRVEEL-AEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 557948119   93 IAFKVAdpTPFH-IQAE---VTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:pfam13561  81 FAPKLK--GPFLdTSREdfdRALDVNLYSLFLLAKAALPLMKEGGS 124
PRK07201 PRK07201
SDR family oxidoreductase;
4-127 2.23e-16

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 75.76  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   4 GIHVaLVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07201 371 GKVV-LITGASSGIGRATAIKVAEA-GATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGH 448

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  84 LDVLVNNAG--IAFKVADPTP-FHiQAEVTMKTNFFGTRDVCTELLP 127
Cdd:PRK07201 449 VDYLVNNAGrsIRRSVENSTDrFH-DYERTMAVNYFGAVRLILGLLP 494
PRK06914 PRK06914
SDR family oxidoreductase;
7-134 3.11e-16

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 73.90  E-value: 3.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH--QLDIDDLQSIRALRDFLrKEYGGL 84
Cdd:PRK06914   5 IAIVTGASSGFGLLTTLELAKK-GYLVIATMRNPEKQENLLSQATQLNLQQNIKvqQLDVTDQNSIHNFQLVL-KEIGRI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557948119  85 DVLVNNAGIAFK-VADPTP---FHIQAEvtmkTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK06914  83 DLLVNNAGYANGgFVEEIPveeYRKQFE----TNVFGAISVTQAVLPYMRKQKS 132
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 7-130 4.39e-16

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: 72.82  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvtrgQAAVQQLQAEGLSpRFH--QLDIDDLQSIRALRDFLRKeyggL 84
Cdd:cd05354    5 TVLVTGANRGIGKAFVESLLAHGAKKVYAAVRD----PGSAAHLVAKYGD-KVVplRLDVTDPESIKAAAAQAKD----V 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557948119  85 DVLVNNAGIaFKVADPTP--FHIQAEVTMKTNFFGTRDVCTELLPLIK 130
Cdd:cd05354   76 DVVINNAGV-LKPATLLEegALEALKQEMDVNVFGLLRLAQAFAPVLK 122
PRK07774 PRK07774
SDR family oxidoreductase;
7-93 7.22e-16

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 72.47  E-value: 7.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07774   8 VAIVTGAAGGIGQAYAEALARE-GASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDY 86


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK07774  87 LVNNAAI 93
PRK06124 PRK06124
SDR family oxidoreductase;
7-92 7.42e-16

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 72.44  E-value: 7.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06124  13 VALVTGSARGLGFEIARALAG--AGaHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLD 90


                 ....*..
gi 557948119  86 VLVNNAG 92
Cdd:PRK06124  91 ILVNNVG 97
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-132 8.67e-16

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: 71.90  E-value: 8.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSP----RFHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd08939    3 HVLITGGSSGIGKALAKELVKE-GANVIIVARSESKLEEAVEEIEAEANASgqkvSYISADLSDYEEVEQAFAQAVEKGG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557948119  83 GLDVLVNNAGIA----FKVADPTPFHIQaevtMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd08939   82 PPDLVVNCAGISipglFEDLTAEEFERG----MDVNYFGSLNVAHAVLPLMKEQ 131
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-132 9.32e-16

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: 72.31  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSgDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05344    3 VALVTAASSGIGLAIARALAREGA-RVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557948119  87 LVNNAGiafkVADPTPFhiqAEVT-------MKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd05344   82 LVNNAG----GPPPGPF---AELTdedwleaFDLKLLSVIRIVRAVLPGMKER 127
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 7-119 1.06e-15

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: 71.92  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05362    5 VALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDI 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 557948119  87 LVNNAGIAFK--VADPTP--FHIQAEVTMKTNFFGTR 119
Cdd:cd05362   85 LVNNAGVMLKkpIAETSEeeFDRMFTVNTKGAFFVLQ 121
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-133 1.28e-15

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: 71.72  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTA--RDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAA--RGFDIAINdlPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 557948119  85 DVLVNNAGIAFKV------ADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQA 133
Cdd:cd05337   81 DCLVNNAGIAVRPrgdlldLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFD 135
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-132 1.31e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 73.34  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTA-RDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06484   7 VVLVTGAAGGIGRAACQRFAR--AGDQVVVAdRNVERARERADSL---GPDHHALAMDVSDEAQIREGFEQLHREFGRID 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAGI----AFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:PRK06484  82 VLVNNAGVtdptMTATLDTTLEEFAR--LQAINLTGAYLVAREALRLMIEQ 130
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 6-134 2.06e-15

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: 71.03  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAE-GAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLD 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557948119  86 VLVNNAGI----AFKVADPTPFhiqaEVTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:cd08934   83 ILVNNAGImllgPVEDADTTDW----TRMIDTNLLGLMYTTHAALPHHLLRNK 131
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 8-150 2.77e-15

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: 70.79  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAvQQLQAEGLSPRFHQLDIDDL--QSIRALRDFLRKeyGGLD 85
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATEL-AALGASHSRLHILELDVTDEiaESAEAVAERLGD--AGLD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAGIA--FKVADPTPfHIQAEVTMKTNFFGTRDVCTELLPLIKPQASCVL----SAWSCLSQNPSGG 150
Cdd:cd05325   78 VLINNAGILhsYGPASEVD-SEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIinisSRVGSIGDNTSGG 147
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 7-93 2.92e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 71.07  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK12429   6 VALVTGAASGIGLEIALALAK--EGaKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:PRK12429  84 ILVNNAGI 91
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-132 3.61e-15

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: 70.46  E-value: 3.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05347    7 VALVTGASRGIGFGIASGLAE-AGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  87 LVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd05347   86 LVNNAGII-RRHPAEEFPEAEwRDVIDVNLNGVFFVSQAVARHMIKQ 131
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-99 3.68e-15

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 70.54  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12937   7 VAIVTGASRGIGAAIARRLAA--DGfAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRI 84

                         90
                 ....*....|....*..
gi 557948119  85 DVLVNNAGIAF--KVAD 99
Cdd:PRK12937  85 DVLVNNAGVMPlgTIAD 101
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 7-132 4.08e-15

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: 70.55  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTA-RDVTRGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd08940    4 VALVTGSTSGIGLGIARALAAA-GANIVLNGfGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557948119  85 DVLVNNAGIAFkVADPTPFHIQA-----EVTMKTNFFGTRDVctelLPLIKPQ 132
Cdd:cd08940   83 DILVNNAGIQH-VAPIEDFPTEKwdaiiALNLSAVFHTTRLA----LPHMKKQ 130
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 8-93 5.25e-15

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 69.93  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    8 ALVTGGNKGIGLAIVRDLCRLFSgDVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79


                  ....*..
gi 557948119   87 LVNNAGI 93
Cdd:TIGR01830  80 LVNNAGI 86
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 8-130 5.63e-15

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: 70.17  E-value: 5.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG-LDV 86
Cdd:cd05329    9 ALVTGGTKGIGYAIVEELAG-LGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGGkLNI 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAG--IAFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIK 130
Cdd:cd05329   88 LVNNAGtnIRKEAKDYTEEDYSL--IMSTNFEAAYHLSRLAHPLLK 131
PRK06181 PRK06181
SDR family oxidoreductase;
7-117 5.86e-15

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 70.01  E-value: 5.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARA-GAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDI 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAGI----AF-KVADPTPFhiqaEVTMKTNFFG 117
Cdd:PRK06181  82 LVNNAGItmwsRFdELTDLSVF----ERVMRVNYLG 113
PRK07063 PRK07063
SDR family oxidoreductase;
7-93 8.18e-15

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 69.69  E-value: 8.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK07063   9 VALVTGAAQGIGAAIAR----AFAREgaaVALADLDAALAERAAAAIARDVAGARvlAVPADVTDAASVAAAVAAAEEAF 84

                         90
                 ....*....|..
gi 557948119  82 GGLDVLVNNAGI 93
Cdd:PRK07063  85 GPLDVLVNNAGI 96
PRK07856 PRK07856
SDR family oxidoreductase;
7-92 1.12e-14

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 69.19  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvtrgqaavQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07856   8 VVLVTGGTRGIGAGIARAFLAA-GATVVVCGRR--------APETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDV 78


                 ....*.
gi 557948119  87 LVNNAG 92
Cdd:PRK07856  79 LVNNAG 84
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 7-93 1.27e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 69.26  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06198   8 VALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDA 87


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK06198  88 LVNAAGL 94
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 8-138 1.44e-14

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: 68.92  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAER-GADVVINyRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAGI-AFK-VADPTPFHIQAEVTM--KTNFFGTRDVcTELLPLIKPQASCVLS 138
Cdd:cd05359   80 LVSNAAAgAFRpLSELTPAHWDAKMNTnlKALVHCAQQA-AKLMRERGGGRIVAIS 134
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 7-132 2.39e-14

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: 68.38  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVTRGQAAVQQLQAEG-LSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05332    5 VVIITGASSGIGEELAYHLARL--GaRLVLSARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLFGGL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557948119  85 DVLVNNAGIA-FKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd05332   83 DILINNAGISmRSLFHDTSIDVDRKI-MEVNYFGPVALTKAALPHLIER 130
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 8-114 2.47e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 68.26  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK07523  13 ALVTGSSQGIGYALAEGLAQ-AGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDIL 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 557948119  88 VNNAGIAFKvadpTP---FHIQA-EVTMKTN 114
Cdd:PRK07523  92 VNNAGMQFR----TPledFPADAfERLLRTN 118
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-116 3.07e-14

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: 68.08  E-value: 3.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTardVTRGQAAVQQLQAE---GLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVL---LARSEEPLQELKEElrpGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557948119  84 LDVLVNNAGIAFKVADPTPFHIQAEVT-MKTNFF 116
Cdd:cd05367   78 RDLLINNAGSLGPVSKIEFIDLDELQKyFDLNLT 111
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 7-127 3.24e-14

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: 67.77  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvtrgQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08932    2 VALVTGASRGIGIEIARALARD-GYRVSLGLRN----PEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 557948119  87 LVNNAGIAFK--VADPTPFHIQAevTMKTNFFGTRDVCTELLP 127
Cdd:cd08932   77 LVHNAGIGRPttLREGSDAELEA--HFSINVIAPAELTRALLP 117
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
6-95 4.76e-14

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 68.72  E-value: 4.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVTRGQAAVQQLQAEGlSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAE--GaCVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFGGV 499

                         90
                 ....*....|.
gi 557948119  85 DVLVNNAGIAF 95
Cdd:PRK08324 500 DIVVSNAGIAI 510
PRK06128 PRK06128
SDR family oxidoreductase;
8-150 9.74e-14

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 67.19  E-value: 9.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLT--------ARDVtrgqaaVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK06128  58 ALITGADSGIGRATAIAFARE-GADIALNylpeeeqdAAEV------VQLIQAEGRKAVALPGDLKDEAFCRQLVERAVK 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557948119  80 EYGGLDVLVNNAG--IAFK-VADPTpfHIQAEVTMKTNFFGTRDVCTELLPLIKPQASCVLSAwSCLSQNPSGG 150
Cdd:PRK06128 131 ELGGLDILVNIAGkqTAVKdIADIT--TEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTG-SIQSYQPSPT 201
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 7-130 1.05e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 66.62  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvtrgQAAVQQLQAE--GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12829  13 RVLVTGGASGIGRAIAEAFAEA-GARVHVCDVS----EAALAATAARlpGAKVTATVADVADPAQVERVFDTAVERFGGL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557948119  85 DVLVNNAGIA---FKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIK 130
Cdd:PRK12829  88 DVLVNNAGIAgptGGIDEITPEQWEQ--TLAVNLNGQFYFARAAVPLLK 134
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 7-93 1.19e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 66.97  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAE--GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06197  18 VAVVTGANTGLGYETAAALAAK-GAHVVLAVRNLDKGKAAAARITAAtpGADVTLQELDLTSLASVRAAADALRAAYPRI 96


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:PRK06197  97 DLLINNAGV 105
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 7-129 1.24e-13

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: 66.36  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08944    5 VAIVTGAGAGIGAACAARLARE-GARVVVADIDGGAAQAVVAQIAGGALALR---VDVTDEQQVAALFERAVEEFGGLDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAGIAfkVADPTPFHIQAEV---TMKTNFFGTRDVCTELLPLI 129
Cdd:cd08944   81 LVNNAGAM--HLTPAIIDTDLAVwdqTMAINLRGTFLCCRHAAPRM 124
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 8-156 1.68e-13

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: 66.77  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDAL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  88 VNNAGIAFKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIK----PQASCVLSawSCLSQNPS--GGKSKPLA 156
Cdd:cd09810   84 VCNAAVYLPTAKEPRFTADGfELTVGVNHLGHFLLTNLLLEDLQrsenASPRIVIV--GSITHNPNtlAGNVPPRA 157
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-92 1.74e-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: 66.02  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08945    5 VALVTGATSGIGLAIARRLGKE-GLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83


                 ....*.
gi 557948119  87 LVNNAG 92
Cdd:cd08945   84 LVNNAG 89
PRK05854 PRK05854
SDR family oxidoreductase;
8-130 2.01e-13

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 66.63  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRdlcRLFSG--DVVLTARDVTRGQAAVQQLQAEglSPR----FHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK05854  17 AVVTGASDGLGLGLAR---RLAAAgaEVILPVRNRAKGEAAVAAIRTA--VPDaklsLRALDLSSLASVAALGEQLRAEG 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557948119  82 GGLDVLVNNAGIAfkvadpTPFHIQA-----EVTMKTNFFGTRDVCTELLPLIK 130
Cdd:PRK05854  92 RPIHLLINNAGVM------TPPERQTtadgfELQFGTNHLGHFALTAHLLPLLR 139
PRK05650 PRK05650
SDR family oxidoreductase;
9-134 2.60e-13

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 65.83  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAI----VRDLCRLFSGDVvltarDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK05650   4 MITGAASGLGRAIalrwAREGWRLALADV-----NEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557948119  85 DVLVNNAGIAF--KVADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK05650  79 DVIVNNAGVASggFFEELSL--EDWDWQIAINLMGVVKGCKAFLPLFKRQKS 128
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 3.43e-13

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 65.25  E-value: 3.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDI 86


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK05565  87 LVNNAGI 93
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 7-92 4.26e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 64.97  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08213  14 TALVTGGSRGLGLQIAEAL-GEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92


                 ....*.
gi 557948119  87 LVNNAG 92
Cdd:PRK08213  93 LVNNAG 98
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 7-118 5.12e-13

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: 64.63  E-value: 5.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLtarDVTRGQAAVQQLQA--EGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05323    2 VAIITGGASGIGLATAKLLLKKGAKVAIL---DRNENPGAAAELQAinPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 557948119  85 DVLVNNAGIA-----FKVADPTPfhiQAEVTMKTNFFGT 118
Cdd:cd05323   79 DILINNAGILdeksyLFAGKLPP---PWEKTIDVNLTGV 114
PRK08628 PRK08628
SDR family oxidoreductase;
6-93 5.16e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 64.98  E-value: 5.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSGDV-VLTARDvTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAE--EGAIpVIFGRS-APDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRI 84


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:PRK08628  85 DGLVNNAGV 93
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-93 7.65e-13

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: 64.33  E-value: 7.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05358    5 VALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDI 84


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:cd05358   85 LVNNAGL 91
PRK06138 PRK06138
SDR family oxidoreductase;
7-92 9.83e-13

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 64.02  E-value: 9.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVTrGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK06138   7 VAIVTGAGSGIGRATAK----LFAREgarVVVADRDAE-AAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGR 81


                 ....*....
gi 557948119  84 LDVLVNNAG 92
Cdd:PRK06138  82 LDVLVNNAG 90
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-127 1.24e-12

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 63.55  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07666   9 NALITGAGRGIGRAVAIALAK--EGvNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSID 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 557948119  86 VLVNNAGIA-F-KVADPTPfhIQAEVTMKTNFFGTRDVCTELLP 127
Cdd:PRK07666  87 ILINNAGISkFgKFLELDP--AEWEKIIQVNLMGVYYATRAVLP 128
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-132 2.68e-12

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: 62.80  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRG------------QAAVQQLQAEGLSPRFHQLDIDDLQSIRALR 74
Cdd:cd05338    5 VAFVTGASRGIGRAIALRLAKA-GATVVVAAKTASEGdngsakslpgtiEETAEEIEAAGGQALPIVVDVRDEDQVRALV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  75 DFLRKEYGGLDVLVNNAGIAF--KVADpTPFHiQAEVTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd05338   84 EATVDQFGRLDILVNNAGAIWlsLVED-TPAK-RFDLMQRVNLRGTYLLSQAALPHMVKA 141
PRK05866 PRK05866
SDR family oxidoreductase;
9-117 4.12e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 62.84  E-value: 4.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLV 88
Cdd:PRK05866  44 LLTGASSGIGEAAAEQFARR-GATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILI 122

                         90       100       110
                 ....*....|....*....|....*....|..
gi 557948119  89 NNAG--IAFKVADPTP-FHiQAEVTMKTNFFG 117
Cdd:PRK05866 123 NNAGrsIRRPLAESLDrWH-DVERTMVLNYYA 153
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-117 4.28e-12

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: 62.26  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLtarDVTRGQAAVQQLQAEGLSPRFH--QLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVIL---DINEKGAEETANNVRKAGGKVHyyKCDVSKREEVYEAAKKIKKEVGDV 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 557948119  85 DVLVNNAGIafkVADPTPFHIQ---AEVTMKTNFFG 117
Cdd:cd05339   78 TILINNAGV---VSGKKLLELPdeeIEKTFEVNTLA 110
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 7-92 4.35e-12

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: 62.22  E-value: 4.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRF-HQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05369    5 VAFITGGGTGIGKAIAKAFAEL-GASVAIAGRKPEVLEAAAEEISSATGGRAHpIQCDVRDPEAVEAAVDETLKEFGKID 83


                 ....*..
gi 557948119  86 VLVNNAG 92
Cdd:cd05369   84 ILINNAA 90
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 7-91 4.54e-12

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 62.33  E-value: 4.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08265   8 VAIVTGGATLIGAAVARALVA-AGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVDI 83


                 ....*
gi 557948119  87 LVNNA 91
Cdd:PRK08265  84 LVNLA 88
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 7-123 5.37e-12

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: 61.96  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdLCRLFSGDVVLTARDVTRGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05352   10 VAIVTGGSRGIGLAIAR-ALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 557948119  86 VLVNNAGIAF-KVADPTPFHIQAEVtMKTNFFGTRDVCT 123
Cdd:cd05352   89 ILIANAGITVhKPALDYTYEQWNKV-IDVNLNGVFNCAQ 126
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 7-95 5.84e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 61.98  E-value: 5.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdlcrLFS---GDVVLTARDVTRGQAAVQQLQAEGLSprfHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK06841  17 VAVVTGGASGIGHAIAE----LFAakgARVALLDRSEDVAEVAAQLLGGNAKG---LVCDVSDSQSVEAAVAAVISAFGR 89

                         90
                 ....*....|..
gi 557948119  84 LDVLVNNAGIAF 95
Cdd:PRK06841  90 IDILVNSAGVAL 101
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-93 6.92e-12

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: 62.38  E-value: 6.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTAR-----DVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKE 80
Cdd:cd08953  206 GVYLVTGGAGGIGRALARALARRYGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRER 285

                         90
                 ....*....|...
gi 557948119  81 YGGLDVLVNNAGI 93
Cdd:cd08953  286 YGAIDGVIHAAGV 298
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 7-92 7.39e-12

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: 61.78  E-value: 7.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGL-SPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd08933   11 VVIVTGGSRGIGRGIVRAFVE--NGaKVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGRI 88


                 ....*...
gi 557948119  85 DVLVNNAG 92
Cdd:cd08933   89 DCLVNNAG 96
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-127 8.85e-12

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: 61.14  E-value: 8.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIvrdlCRLFSG---DVVLTARDVTRGQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd05346    3 VLITGASSGIGEAT----ARRFAKagaKLILTGRRAERLQELADELGAK-FPVKVLplQLDVSDRESIEAALENLPEEFR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  83 GLDVLVNNAGIAFKVADPTPFHIQAEVTM-KTNFFGTRDVCTELLP 127
Cdd:cd05346   78 DIDILVNNAGLALGLDPAQEADLEDWETMiDTNVKGLLNVTRLILP 123
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 7-137 9.54e-12

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: 61.25  E-value: 9.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVTRGQAAVQQLQAEGLsprFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05345    7 VAIVTGAGSGFGEGIAR----RFAQEgarVVIADINADGAERVAADIGEAAI---AIQADVTKRADVEAMVEAALSKFGR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 557948119  84 LDVLVNNAGIAFKVA-----DPTPFHIQAEVTMKTNFFGTRdvctELLPLIKPQASCVL 137
Cdd:cd05345   80 LDILVNNAGITHRNKpmlevDEEEFDRVFAVNVKSIYLSAQ----ALVPHMEEQGGGVI 134
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-93 9.85e-12

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: 61.33  E-value: 9.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRF--HQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd09807    3 TVIITGANTGIGKETARELARR-GARVIMACRDMAKCEEAAAEIRRDTLNHEVivRHLDLASLKSIRAFAAEFLAEEDRL 81


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:cd09807   82 DVLINNAGV 90
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 7-96 1.52e-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: 60.60  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRF-HQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05343    8 VALVTGASVGIGAAVARALVQ-HGMKVVGCARRVDKIEALAAECQSAGYPTLFpYQCDLSNEEQILSMFSAIRTQHQGVD 86

                         90
                 ....*....|.
gi 557948119  86 VLVNNAGIAFK 96
Cdd:cd05343   87 VCINNAGLARP 97
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-118 1.93e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 61.09  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   1 MSSGIHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFAR--RGaKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 557948119  80 EYGGLDVLVNNAGIA-FKVADPTPFHIQAEVTmKTNFFGT 118
Cdd:PRK07109  82 ELGPIDTWVNNAMVTvFGPFEDVTPEEFRRVT-EVTYLGV 120
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 8-92 2.07e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 60.44  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAivrdLCRLFSGD---VVLTARDVTRGQAAVQQLQAE-GLSPRFHQLDIDDLQSiralRDFLRKEYGG 83
Cdd:PRK06125  10 VLITGASKGIGAA----AAEAFAAEgchLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEA----REQLAAEAGD 81


                 ....*....
gi 557948119  84 LDVLVNNAG 92
Cdd:PRK06125  82 IDILVNNAG 90
PRK06949 PRK06949
SDR family oxidoreductase;
7-102 2.47e-11

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 60.16  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGdVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06949  11 VALVTGASSGLGARFAQVLAQAGAK-VVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                         90
                 ....*....|....*...
gi 557948119  87 LVNNAGIAF--KVADPTP 102
Cdd:PRK06949  90 LVNNSGVSTtqKLVDVTP 107
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 2.53e-11

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 61.01  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLtARDVTRGQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08261 212 VALVTGAARGIGAAIAEVLAR--DGAHVV-CLDVPAAGEALAAV-ANRVGGTALALDITAPDAPARIAEHLAERHGGLDI 287


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK08261 288 VVHNAGI 294
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 6-132 2.56e-11

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: 60.10  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLtarDVtrgQAAVQQLQAEGLSPRFH----QLDIDDLQSIRALRDFLRKEY 81
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVA---DI---DPEIAEKVAEAAQGGPRalgvQCDVTSEAQVQSAFEQAVLEF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557948119  82 GGLDVLVNNAGIAFkvadPTPFhiqAEVTMKT-------NFFGTRDVCTELLPLIKPQ 132
Cdd:cd08943   76 GGLDIVVSNAGIAT----SSPI---AETSLEDwnrsmdiNLTGHFLVSREAFRIMKSQ 126
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
7-93 2.72e-11

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 59.78  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTArDVTRGQAAVQQLQAEGLSP---RFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK12824   4 IALVTGAKRGIGSAIARELLN--DGYRVIAT-YFSGNDCAKDWFEEYGFTEdqvRLKELDVTDTEECAEALAEIEEEEGP 80

                         90
                 ....*....|
gi 557948119  84 LDVLVNNAGI 93
Cdd:PRK12824  81 VDILVNNAGI 90
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-91 3.03e-11

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 59.73  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08063   6 VALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDV 85


                 ....*
gi 557948119  87 LVNNA 91
Cdd:PRK08063  86 FVNNA 90
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 16-150 3.06e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 59.97  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  16 GIGLAIVRDLCRLFS---GDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAG 92
Cdd:PRK07890  12 GVGPGLGRTLAVRAAragADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAF 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557948119  93 I--AFK-VADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQASCVL---SAWSCLSQNPSGG 150
Cdd:PRK07890  92 RvpSMKpLADADFAHWRA--VIELNVLGTLRLTQAFTPALAESGGSIVminSMVLRHSQPKYGA 153
PRK08219 PRK08219
SDR family oxidoreductase;
7-130 3.20e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 59.56  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTARDVTRGQAAVQQL-QAEGLsprfhQLDIDDLQSIRALRDFLrkeyGGLD 85
Cdd:PRK08219   5 TALITGASRGIGAAIARELAP--THTLLLGGRPAERLDELAAELpGATPF-----PVDLTDPEAIAAAVEQL----GRLD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  86 VLVNNAGIAF--KVADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIK 130
Cdd:PRK08219  74 VLVHNAGVADlgPVAESTV--DEWRATLEVNVVAPAELTRLLLPALR 118
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 7-94 3.28e-11

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: 60.09  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVrdlCRLFSGD-------VVLTARDVTRGQAAVQQLQAeglsprFH----------QLDIDDLQS 69
Cdd:cd08941    3 VVLVTGANSGLGLAIC---ERLLAEDdenpeltLILACRNLQRAEAACRALLA------SHpdarvvfdyvLVDLSNMVS 73

                         90       100
                 ....*....|....*....|....*
gi 557948119  70 IRALRDFLRKEYGGLDVLVNNAGIA 94
Cdd:cd08941   74 VFAAAKELKKRYPRLDYLYLNAGIM 98
PRK07035 PRK07035
SDR family oxidoreductase;
7-92 3.65e-11

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 59.64  E-value: 3.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07035  10 IALVTGASRGIGEAIAKLLAQ-QGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88


                 ....*.
gi 557948119  87 LVNNAG 92
Cdd:PRK07035  89 LVNNAA 94
PRK05693 PRK05693
SDR family oxidoreductase;
7-92 3.67e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 59.80  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVrDLCRLFSGDVVLTARDVtrgqAAVQQLQAEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05693   3 VVLITGCSSGIGRALA-DAFKAAGYEVWATARKA----EDVEALAAAGFTAV--QLDVNDGAALARLAEELEAEHGGLDV 75


                 ....*.
gi 557948119  87 LVNNAG 92
Cdd:PRK05693  76 LINNAG 81
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 7-93 8.08e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 58.80  E-value: 8.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVtrgqaAVQQLQAEGLSP-RFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07825   7 VVAITGGARGIGLATARALAAL-GARVAIGDLDE-----ALAKETAAELGLvVGGPLDVTDPASFAAFLDAVEADLGPID 80


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:PRK07825  81 VLVNNAGV 88
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 7-94 8.40e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 58.59  E-value: 8.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVTRGQAAVQQLqaEGLsprFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06057   9 VAVITGGGSGIGLATAR---RLAAegATVVVGDIDPEAGKAAADEV--GGL---FVPTDVTDEDAVNALFDTAAETYGSV 80

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:PRK06057  81 DIAFNNAGIS 90
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-148 9.55e-11

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: 58.35  E-value: 9.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAK-AGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557948119  87 LVNNAGIAFKVADPTPFHI-QAEVTMKTNFFGTRDVCTELLP-LIKPQASCVLSAWSCLSQNPS 148
Cdd:cd05365   80 LVNNAGGGGPKPFDMPMTEeDFEWAFKLNLFSAFRLSQLCAPhMQKAGGGAILNISSMSSENKN 143
PRK06196 PRK06196
oxidoreductase; Provisional
 7-141 1.07e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 58.93  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCrLFSGDVVLTARDVTRGQAAVQQLqaEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06196  28 TAIVTGGYSGLGLETTRALA-QAGAHVIVPARRPDVAREALAGI--DGVE--VVMLDLADLESVRAFAERFLDSGRRIDI 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAGIafkVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQASCVLSAWS 141
Cdd:PRK06196 103 LINNAGV---MACPeTRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALS 155
PRK06182 PRK06182
short chain dehydrogenase; Validated
 7-134 1.12e-10

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 58.43  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfsGDVVL-TARDVTRgqaaVQQLQAEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQ--GYTVYgAARRVDK----MEDLASLGVHPL--SLDVTDEASIKAAVDTIIAEEGRID 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 557948119  86 VLVNNAGI-AFKVADPTPFHiQAEVTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK06182  77 VLVNNAGYgSYGAIEDVPID-EARRQFEVNLFGAARLTQLVLPHMRAQRS 125
PRK07062 PRK07062
SDR family oxidoreductase;
7-92 1.22e-10

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 58.13  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVTRGQAAVQQL-----QAEGLSPRFHQLDIDDlqsIRALRDFLRKE 80
Cdd:PRK07062  10 VAVVTGGSSGIGLATVELL--LEAGaSVAICGRDEERLASAEARLrekfpGARLLAARCDVLDEAD---VAAFAAAVEAR 84

                         90
                 ....*....|..
gi 557948119  81 YGGLDVLVNNAG 92
Cdd:PRK07062  85 FGGVDMLVNNAG 96
PRK09072 PRK09072
SDR family oxidoreductase;
9-134 1.24e-10

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 58.41  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvtrgQAAVQQLQAEGLSPRFHQL---DIDDLQSIRALRDFLRkEYGGLD 85
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAA-GARLLLVGRN----AEKLEALAARLPYPGRHRWvvaDLTSEAGREAVLARAR-EMGGIN 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAGIA-FK-VADPTPFHIQAEVTmkTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK09072  83 VLINNAGVNhFAlLEDQDPEAIERLLA--LNLTAPMQLTRALLPLLRAQPS 131
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-93 1.46e-10

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 58.21  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDvTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06935  17 VAIVTGGNTGLGQGYAVALAK--AGaDIIITTHG-TNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKID 93


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:PRK06935  94 ILVNNAGT 101
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-94 1.89e-10

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: 57.77  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRG-QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05366    4 VAIITGAAQGIGRAIAERLAA--DGfNIVLADLNLEEAaKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:cd05366   82 DVMVNNAGIA 91
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 7-93 2.54e-10

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 57.60  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK13394   9 TAVVTGAASGIGKEIALELARA-GAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK13394  88 LVSNAGI 94
PRK07454 PRK07454
SDR family oxidoreductase;
8-95 2.65e-10

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 57.28  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07454   9 ALITGASSGIGKATALAFAK--AGwDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86


                 ....*....
gi 557948119  87 LVNNAGIAF 95
Cdd:PRK07454  87 LINNAGMAY 95
PRK12743 PRK12743
SDR family oxidoreductase;
7-98 2.67e-10

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 57.35  E-value: 2.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12743   4 VAIVTASDSGIGKACALLLAQ--QGfDIGITwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81

                         90
                 ....*....|....
gi 557948119  85 DVLVNNAGIAFKVA 98
Cdd:PRK12743  82 DVLVNNAGAMTKAP 95
PRK05855 PRK05855
SDR family oxidoreductase;
8-117 2.70e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 58.07  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFARE-GAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIV 396

                         90       100       110
                 ....*....|....*....|....*....|..
gi 557948119  88 VNNAGI--AFKVADPTPFHIQAevTMKTNFFG 117
Cdd:PRK05855 397 VNNAGIgmAGGFLDTSAEDWDR--VLDVNLWG 426
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-124 2.91e-10

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: 57.47  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08935    7 VAVITGGTGVLGGAMARALAQA-GAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDI 85

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 557948119  87 LVNNAGIAFKVADPTPFHIQAEVTmkTNFFGTRDVCTE 124
Cdd:cd08935   86 LINGAGGNHPDATTDPEHYEPETE--QNFFDLDEEGWE 121
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-169 3.49e-10

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 57.55  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfsGD-VVLTARDVTRGQAAVQQLQAEGLSprfHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAA--GDrLLIIDRDAEGAKKLAEALGDEHLS---VQADITDEAAVESAFAQIQARWGRLD 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  86 VLVNNAGIA---FKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIKpQASCVLSAWSCLSQNPSGGKSKPLAWFTEMS 162
Cdd:PRK06484 346 VLVNNAGIAevfKPSLEQSAEDF--TRVYDVNLSGAFACARAAARLMS-QGGVIVNLGSIASLLALPPRNAYCASKAAVT 422


                 ....*..
gi 557948119 163 IICRCLT 169
Cdd:PRK06484 423 MLSRSLA 429
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 7-173 3.51e-10

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: 57.04  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK---EYGG 83
Cdd:cd05364    5 VAIITGSSSGIGAGTAILFARL-GARLALTGRDAERLEETRQSCLQAGVSEKKILLVVADLTEEEGQDRIISTtlaKFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  84 LDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQASCVLSAWSCLSQ-----NPSGGKSK-PLAW 157
Cdd:cd05364   84 LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGrsfpgVLYYCISKaALDQ 163

                        170
                 ....*....|....*.
gi 557948119 158 FTEmsiiCRCLTLGPF 173
Cdd:cd05364  164 FTR----CTALELAPK 175
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 7-147 5.14e-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: 56.31  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFhqlDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05349    2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGERAIAIQA---DVRDRDQVQAMIEEAKNHFGPVDT 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557948119  87 LVNNAGIAFKV---ADPTP-------FHIQAEVTMKtnffGTRDVCTELLP-LIKPQASCVLSAWSCLSQNP 147
Cdd:cd05349   79 IVNNALIDFPFdpdQRKTFdtidwedYQQQLEGAVK----GALNLLQAVLPdFKERGSGRVINIGTNLFQNP 146
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-130 5.21e-10

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 56.33  E-value: 5.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvtrgQAAVQQLQAEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06463   9 VALITGGTRGIGRAIAEAFLREGAKVAVLYNSA----ENEAKELREKGVF--TIKCDVGNRDQVKKSKEVVEKEFGRVDV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557948119  87 LVNNAGIAFKVadptPF----HIQAEVTMKTNFFGTRDVCTELLPLIK 130
Cdd:PRK06463  83 LVNNAGIMYLM----PFeefdEEKYNKMIKINLNGAIYTTYEFLPLLK 126
PRK06500 PRK06500
SDR family oxidoreductase;
8-137 5.29e-10

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 56.50  E-value: 5.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVrdlcRLFSGD---VVLTARDVTRGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06500   9 ALITGGTSGIGLETA----RQFLAEgarVAITGRDPASLEAARAELGESALVIR---ADAGDVAAQKALAQALAEAFGRL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557948119  85 DVLVNNAGiafkVADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLIKPQASCVL 137
Cdd:PRK06500  82 DAVFINAG----VAKFAPLEDWDEAmfdrSFNTNVKGPYFLIQALLPLLANPASIVL 134
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 5.38e-10

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 56.51  E-value: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08217   7 VIVITGGAQGLGRAMAEYLAQ--KGaKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:PRK08217  85 GLINNAGI 92
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
7-98 5.61e-10

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 56.19  E-value: 5.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07067   8 VALLTGAASGIGEAVAERYLAE-GARVVIADIKPARARLAALEIGPAAIAVS---LDVTRQDSIDRIVAAAVERFGGIDI 83

                         90
                 ....*....|..
gi 557948119  87 LVNNAGIaFKVA 98
Cdd:PRK07067  84 LFNNAAL-FDMA 94
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 7-134 6.91e-10

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: 56.15  E-value: 6.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAV--QQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05355   28 KALITGGDSGIGRAVAIAFAR--EGaDVAINYLPEEEDDAEEtkKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGK 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557948119  84 LDVLVNNAG---IAFKVADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:cd05355  106 LDILVNNAAyqhPQESIEDITT--EQLEKTFRTNIFSMFYLTKAALPHLKKGSS 157
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-94 7.13e-10

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 56.27  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVrdlCRLFSG--DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK08643   4 VALVTGAGQGIGFAIA---KRLVEDgfKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:PRK08643  81 NVVVNNAGVA 90
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-134 8.15e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 56.06  E-value: 8.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDL----CRLFSgdvvlTARDVTRgqaavqqlqAEGLSP-RFHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLaragYRVFG-----TSRNPAR---------AAPIPGvELLELDVTDDASVQAAVDEVIARA 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557948119  82 GGLDVLVNNAGIAFkVADPTPFHI-QAEVTMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK06179  72 GRIDVLVNNAGVGL-AGAAEESSIaQAQALFDTNVFGILRMTRAVLPHMRAQGS 124
PRK07074 PRK07074
SDR family oxidoreductase;
7-102 8.16e-10

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 55.93  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcrLFSGDVVLTA-RDVTRGQAAVQQLQAEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07074   4 TALVTGAAGGIGQALARRF--LAAGDRVLALdIDAAALAAFADALGDARFVPV--ACDLTDAASLAAALANAAAERGPVD 79

                         90
                 ....*....|....*....
gi 557948119  86 VLVNNAGIAFKV--ADPTP 102
Cdd:PRK07074  80 VLVANAGAARAAslHDTTP 98
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 7-130 8.47e-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: 55.93  E-value: 8.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIV----RDLCRLFSgdVVLTARDVTRGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKey 81
Cdd:cd09806    2 VVLITGCSSGIGLHLAvrlaSDPSKRFK--VYATMRDLKKKGRLWEAAGALaGGTLETLQLDVCDSKSVAAAVERVTE-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557948119  82 GGLDVLVNNAGIAFKvadpTPFHIQAEVTMK----TNFFGTRDVCTELLPLIK 130
Cdd:cd09806   78 RHVDVLVCNAGVGLL----GPLEALSEDAMAsvfdVNVFGTVRMLQAFLPDMK 126
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 7-93 1.15e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 55.40  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcrLFSGDVVLTArDVTRGQAAVQQLQaeglsprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06171  11 IIIVTGGSSGIGLAIVKEL--LANGANVVNA-DIHGGDGQHENYQ-------FVPTDVSSAEEVNHTVAEIIEKFGRIDG 80


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK06171  81 LVNNAGI 87
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 7-94 1.26e-09

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: 55.37  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLtardVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05371    4 VAVVTGGASGLGLATVERLLAQ-GAKVVI----LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDI 78


                 ....*...
gi 557948119  87 LVNNAGIA 94
Cdd:cd05371   79 VVNCAGIA 86
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 8-93 1.30e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 55.53  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAE-YGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVL 90


                 ....*.
gi 557948119  88 VNNAGI 93
Cdd:PRK08085  91 INNAGI 96
PRK08017 PRK08017
SDR family oxidoreductase;
9-132 1.60e-09

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 55.09  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRlfSGDVVLTArdvTRGQAAVQQLQAEGLSPRfhQLDIDDLQSI-RALRDFLRKEYGGLDVL 87
Cdd:PRK08017   6 LITGCSSGIGLEAALELKR--RGYRVLAA---CRKPDDVARMNSLGFTGI--LLDLDDPESVeRAADEVIALTDNRLYGL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  88 VNNAGiaFKVADP--TPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:PRK08017  79 FNNAG--FGVYGPlsTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPH 123
PRK07806 PRK07806
SDR family oxidoreductase;
7-91 1.78e-09

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 54.73  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07806   8 TALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGLDA 87


                 ....*
gi 557948119  87 LVNNA 91
Cdd:PRK07806  88 LVLNA 92
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-130 1.90e-09

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 54.73  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDVTRG----QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:PRK12827   8 RVLITGGSGGLGRAIAVRL-AADGADVIVLDIHPMRGraeaDAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557948119  83 GLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELL-PLIK 130
Cdd:PRK12827  87 RLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIR 135
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 8-92 2.28e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 54.52  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAvqqlqaeglSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK06523  12 ALVTGGTKGIGAATVARLLEA-GARVVTTARSRPDDLPE---------GVEFVAADLTTAEGCAAVARAVLERLGGVDIL 81


                 ....*
gi 557948119  88 VNNAG 92
Cdd:PRK06523  82 VHVLG 86
PRK06172 PRK06172
SDR family oxidoreductase;
7-93 4.33e-09

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 53.99  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06172   9 VALVTGGAAGIGRATALAFARE-GAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDY 87


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK06172  88 AFNNAGI 94
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-94 6.23e-09

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: 53.35  E-value: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDVTRGqaaVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd09761    3 VAIVTGGGHGIGKQICLDF--LEAGDkVVFADIDEERG---ADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRID 77


                 ....*....
gi 557948119  86 VLVNNAGIA 94
Cdd:cd09761   78 VLVNNAARG 86
PRK07831 PRK07831
SDR family oxidoreductase;
7-93 1.10e-08

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 52.73  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGG-NKGIGLAIVRDlCRLFSGDVVLTARDVTRGQAAVQQLQAE-GLSPRFHQL-DIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07831  19 VVLVTAAaGTGIGSATARR-ALEEGARVVISDIHERRLGETADELAAElGLGRVEAVVcDVTSEAQVDALIDAAVERLGR 97

                         90
                 ....*....|
gi 557948119  84 LDVLVNNAGI 93
Cdd:PRK07831  98 LDVLVNNAGL 107
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-96 1.25e-08

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: 52.28  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDV-TRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05357    2 VALVTGAAKRIGRAIAEALAA--EGyRVVVHYNRSeAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRC 79

                         90
                 ....*....|..
gi 557948119  85 DVLVNNAGIAFK 96
Cdd:cd05357   80 DVLVNNASAFYP 91
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 7-93 1.25e-08

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 52.70  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12935   8 VAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDI 87


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK12935  88 LVNNAGI 94
PRK07832 PRK07832
SDR family oxidoreductase;
8-94 1.32e-08

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 52.74  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQ-LDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAA-QGAELFLTDRDADGLAQTVADARALGGTVPEHRaLDISDYDAVAAFAADIHAAHGSMDV 81


                 ....*...
gi 557948119  87 LVNNAGIA 94
Cdd:PRK07832  82 VMNIAGIS 89
PRK09135 PRK09135
pteridine reductase; Provisional
 1-104 1.55e-08

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 52.24  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   1 MSSGIHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARdvtRGQAAVQQLQAEgL------SPRFHQLDIDDLQSIRAL 73
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHA--AGyRVAIHYH---RSAAEADALAAE-LnalrpgSAAALQADLLDPDALPEL 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 557948119  74 RDFLRKEYGGLDVLVNNAGIAFkvadPTPFH 104
Cdd:PRK09135  76 VAACVAAFGRLDALVNNASSFY----PTPLG 102
PRK09730 PRK09730
SDR family oxidoreductase;
7-96 1.57e-08

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 52.16  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAA 82

                         90
                 ....*....|
gi 557948119  87 LVNNAGIAFK 96
Cdd:PRK09730  83 LVNNAGILFT 92
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-132 1.63e-08

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: 52.09  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRdlcRLFSGDVVLTARDVtrgqaAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:cd05331    1 VIVTGAAQGIGRAVAR---HLLQAGATVIALDL-----PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  88 VNNAGIaFKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:cd05331   73 VNCAGV-LRPGATDPLSTEDwEQTFAVNVTGVFNLLQAVAPHMKDR 117
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 7-93 1.77e-08

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: 52.07  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05326    6 VAIITGGASGIGEATARLFAK-HGARVVIADIDDDAGQAVAAELGDPDIS--FVHCDVTVEADVRAAVDTAVARFGRLDI 82


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:cd05326   83 MFNNAGV 89
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-93 1.80e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 51.99  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVV--LTARDVTRGQAAvqqLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK07097  12 IALITGASYGIGFAIAKAYAKAGATIVFndINQELVDKGLAA---YRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVI 88


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:PRK07097  89 DILVNNAGI 97
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-147 1.81e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 52.01  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVltarDVTRGQAAVQQLQAEgLSPRF--HQLDIDDLQSIRALRDFLRKEYG-G 83
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVV----NYHQSEDAAEALADE-LGDRAiaLQADVTDREQVQAMFATATEHFGkP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557948119  84 LDVLVNNAGIAFK---VADPTP-------FHIQAEVTMKtnffGTRDVCTELLP-LIKPQASCVLSAWSCLSQNP 147
Cdd:PRK08642  82 ITTVVNNALADFSfdgDARKKAdditwedFQQQLEGSVK----GALNTIQAALPgMREQGFGRIINIGTNLFQNP 152
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
7-127 1.99e-08

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 52.11  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAvQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08226   8 TALITGALQGIGEGIARVFARH-GANLILLDISPEIEKLA-DELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDI 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  87 LVNNAGI---AFKVADPTP---FHIQaevtmkTNFFGTRDVCTELLP 127
Cdd:PRK08226  86 LVNNAGVcrlGSFLDMSDEdrdFHID------INIKGVWNVTKAVLP 126
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 7-92 2.03e-08

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 52.21  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08277  12 VAVITGGGGVLGGAMAKELAR--AGaKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCD 89


                 ....*..
gi 557948119  86 VLVNNAG 92
Cdd:PRK08277  90 ILINGAG 96
PRK06114 PRK06114
SDR family oxidoreductase;
7-94 2.43e-08

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 51.71  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAA-VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06114  10 VAFVTGAGSGIGQRIAIGLAQA-GADVALFDLRTDDGLAEtAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALT 88


                 ....*....
gi 557948119  86 VLVNNAGIA 94
Cdd:PRK06114  89 LAVNAAGIA 97
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 6-94 2.75e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 51.64  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDvtrgQAAVQQLQAEgLSPRFHQLDIDDLQSIRALRDflrkEYGGL 84
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQ--RGaRVVAAARN----AAALDRLAGE-TGCEPLRLDVGDDAAIRAALA----AAGAF 78

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:PRK07060  79 DGLVNCAGIA 88
PRK06398 PRK06398
aldose dehydrogenase; Validated
 7-93 2.91e-08

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 51.37  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvtRGQAAVQqlqaeglsprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06398   8 VAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE--PSYNDVD----------YFKVDVSNKEQVIKGIDYVISKYGRIDI 75


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK06398  76 LVNNAGI 82
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 7-134 2.93e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 51.58  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDVTRGQAAVQQLQaEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08263   5 VWFITGASRGFGRAWTEAA--LERGDrVVATARDTATLADLAEKYG-DRLLPL--ALDVTDRAAVFAAVETAVEHFGRLD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  86 VLVNNAGIAFkvadptpFHIQAEVT-------MKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK08263  80 IVVNNAGYGL-------FGMIEEVTesearaqIDTNFFGALWVTQAVLPYLREQRS 128
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 7-136 3.11e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 51.57  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGlaivRDLCRLFS---GDVVLT----ARDVTRGQAAVQqlqAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK06701  48 VALITGGDSGIG----RAVAVLFAkegADIAIVyldeHEDANETKQRVE---KEGVKCLLIPGDVSDEAFCKDAVEETVR 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557948119  80 EYGGLDVLVNNAgiAF-----KVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIKPQASCV 136
Cdd:PRK06701 121 ELGRLDILVNNA--AFqypqqSLEDITAEQL--DKTFKTNIYSYFHMTKAALPHLKQGSAII 178
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-93 3.19e-08

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: 50.56  E-value: 3.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119     9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTAR---DVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83


                   ....*...
gi 557948119    86 VLVNNAGI 93
Cdd:smart00822  84 GVIHAAGV 91
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 7-91 3.40e-08

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: 51.29  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVV-LTARDVTRGQAAV-QQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG- 83
Cdd:cd09763    5 IALVTGASRGIGRGIALQLGE--AGATVyITGRTILPQLPGTaEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQGr 82


                 ....*...
gi 557948119  84 LDVLVNNA 91
Cdd:cd09763   83 LDILVNNA 90
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 9-130 3.42e-08

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: 51.44  E-value: 3.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIG----LAIVRDlcrlfSGDVVLTARDVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd09808    5 LITGANSGIGkaaaLAIAKR-----GGTVHMVCRNQTRAEEARKEIETESGNQNifLHIVDMSDPKQVWEFVEEFKEEGK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557948119  83 GLDVLVNNAGIAFKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIK 130
Cdd:cd09808   80 KLHVLINNAGCMVNKRELTEDGL--EKNFATNTLGTYILTTHLIPVLE 125
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 7-103 4.04e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 51.12  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvtrgQAAVQQLQAE-GLSPRFHQL--DIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK05872  11 VVVVTGAARGIGAELARRLHAR-GAKLALVDLE----EAELAALAAElGGDDRVLTVvaDVTDLAAMQAAAEEAVERFGG 85

                         90       100
                 ....*....|....*....|....
gi 557948119  84 LDVLVNNAGIA----FKVADPTPF 103
Cdd:PRK05872  86 IDVVVANAGIAsggsVAQVDPDAF 109
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 7-93 4.12e-08

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 51.04  E-value: 4.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfsGDVVlTARDVTRgqaavqqLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAFVEA--GAKV-IGFDQAF-------LTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDV 79


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK08220  80 LVNAAGI 86
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 7-93 4.87e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 50.95  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLspRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12828   9 VVAITGGFGGLGRATAAWLAAR-GARVALIGRGAAPLSQTLPGVPADAL--RIGGIDLVDPQAARRAVDEVNRQFGRLDA 85


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK12828  86 LVNIAGA 92
PRK08589 PRK08589
SDR family oxidoreductase;
7-93 4.94e-08

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 50.93  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTArDVTRG-QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08589   8 VAVITGASTGIGQASAIALAQ--EGAYVLAV-DIAEAvSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVD 84


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:PRK08589  85 VLFNNAGV 92
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 7-93 6.70e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 50.83  E-value: 6.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLA------------IVRDLCRLFSGdvvlTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALR 74
Cdd:PRK07791   8 VVIVTGAGGGIGRAhalafaaegarvVVNDIGVGLDG----SASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLV 83

                         90
                 ....*....|....*....
gi 557948119  75 DFLRKEYGGLDVLVNNAGI 93
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAGI 102
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-134 9.03e-08

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: 50.02  E-value: 9.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05350    1 VLITGASSGIGRALAREFAK--AGyNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557948119  87 LVNNAGIAFkvadPTPFHI-QAEV---TMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:cd05350   79 VIINAGVGK----GTSLGDlSFKAfreTIDTNLLGAAAILEAALPQFRAKGR 126
PLN02253 PLN02253
xanthoxin dehydrogenase
 7-130 9.96e-08

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 50.21  E-value: 9.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHqLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PLN02253  20 VALVTGGATGIGESIVRLFHK-HGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFH-CDVTVEDDVSRAVDFTVDKFGTLDI 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 557948119  87 LVNNAGIA------FKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIK 130
Cdd:PLN02253  98 MVNNAGLTgppcpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKK 147
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 7-93 1.05e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 49.93  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGlaivRDLCRLFSGD---VVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07478   8 VAIITGASSGIG----RAAAKLFAREgakVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGG 83

                         90
                 ....*....|
gi 557948119  84 LDVLVNNAGI 93
Cdd:PRK07478  84 LDIAFNNAGT 93
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 9-130 1.21e-07

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: 49.97  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfsGDVVLtARDVTRGQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYG--GL 84
Cdd:cd09805    4 LITGCDSGFGNLLAKKLDSL--GFTVL-AGCLTKNGPGAKELRRV-CSDRLRtlQLDVTKPEQIKRAAQWVKEHVGekGL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557948119  85 DVLVNNAGIA--FKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIK 130
Cdd:cd09805   80 WGLVNNAGILgfGGDEELLPMDDYRKC-MEVNLFGTVEVTKAFLPLLR 126
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-134 1.23e-07

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: 49.79  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGlSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08942    8 IVLVTGGSRGIGRMIAQGFLEA-GARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557948119  87 LVNNAGIAFKVA-DPTP---FHIQAEVTMKTNFFGTrdvcTELLPLIKPQAS 134
Cdd:cd08942   86 LVNNAGATWGAPlEAFPesgWDKVMDINVKSVFFLT----QALLPLLRAAAT 133
PRK06947 PRK06947
SDR family oxidoreductase;
7-99 1.25e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 49.80  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdLCRLFSGDVVLT-ARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06947   4 VVLITGASRGIGRATAV-LAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLD 82

                         90
                 ....*....|....*..
gi 557948119  86 VLVNNAGI---AFKVAD 99
Cdd:PRK06947  83 ALVNNAGIvapSMPLAD 99
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 7-104 1.31e-07

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: 49.64  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDVTRGQAAVQQLQAEGlSPRFH--QLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd08930    4 IILITGAAGLIGKAFCKAL-LSAGARLILADINAPALEQLKEELTNLY-KNRVIalELDITSKESIKELIESYLEKFGRI 81

                         90       100
                 ....*....|....*....|
gi 557948119  85 DVLVNNAGIAFKVaDPTPFH 104
Cdd:cd08930   82 DILINNAYPSPKV-WGSRFE 100
PRK08267 PRK08267
SDR family oxidoreductase;
9-94 1.62e-07

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 49.55  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDvtrgQAAVQQLQAE--GLSPRFHQLDIDDLQSI-RALRDFLRKEYG 82
Cdd:PRK08267   5 FITGAASGIGRATAL----LFAAEgwrVGAYDIN----EAGLAALAAElgAGNAWTGALDVTDRAAWdAALADFAAATGG 76

                         90
                 ....*....|..
gi 557948119  83 GLDVLVNNAGIA 94
Cdd:PRK08267  77 RLDVLFNNAGIL 88
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 9-127 1.64e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 49.53  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDvtrgQAAVQQLqAEGLSPRFH--QLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06180   8 LITGVSSGFGRALAQAA--LAAGHrVVGTVRS----EAARADF-EALHPDRALarLLDVTDFDAIDAVVADAEATFGPID 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 557948119  86 VLVNNAGI----AFKVADPTPFHIQAEVtmktNFFGTRDVCTELLP 127
Cdd:PRK06180  81 VLVNNAGYghegAIEESPLAEMRRQFEV----NVFGAVAMTKAVLP 122
PLN00015 PLN00015
protochlorophyllide reductase
 9-117 1.74e-07

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 49.70  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLV 88
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 557948119  89 NNAGIAFKVA-DPTPFHIQAEVTMKTNFFG 117
Cdd:PLN00015  81 CNAAVYLPTAkEPTFTADGFELSVGTNHLG 110
PRK07814 PRK07814
SDR family oxidoreductase;
7-103 1.88e-07

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 49.39  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07814  12 VAVVTGAGRGLGAAIALAFAEA-GADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI 90

                         90
                 ....*....|....*..
gi 557948119  87 LVNNAGIAFkvadPTPF 103
Cdd:PRK07814  91 VVNNVGGTM----PNPL 103
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 7-93 1.92e-07

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: 49.52  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCrLFSGDVVLTARDVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd09809    3 VIIITGANSGIGFETARSFA-LHGAHVILACRNMSRASAAVSRILEEWHKARveAMTLDLASLRSVQRFAEAFKAKNSPL 81


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:cd09809   82 HVLVCNAAV 90
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-98 2.15e-07

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 48.95  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08936   9 VVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLDV 88

                         90
                 ....*....|..
gi 557948119  87 LVNNAGIAFKVA 98
Cdd:PRK08936  89 MINNAGIENAVP 100
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-94 2.20e-07

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 48.98  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTArdvTRGQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQ--QGHKVIAT---GRRQERLQELKDE-LGDNLYiaQLDVRNRAAIEEMLASLPAEWRNI 75

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:PRK10538  76 DVLVNNAGLA 85
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-93 2.60e-07

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 49.01  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDfLRKEYGGLD 85
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGDISQRATADELVA-TAVGLGGLD 91


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:PRK07792  92 IVVNNAGI 99
PRK06123 PRK06123
SDR family oxidoreductase;
7-93 2.85e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 48.62  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06123   4 VMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDA 83


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK06123  84 LVNNAGI 90
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 7-127 3.16e-07

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: 48.68  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08937    6 VVVVTGAAQGIGRGVAERLAGE-GARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 557948119  87 LVNNAG--IAFKVADPTPF-HIQAEVtmKTNFFGTRDVCTELLP 127
Cdd:cd08937   84 LINNVGgtIWAKPYEHYEEeQIEAEI--RRSLFPTLWCCRAVLP 125
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-131 3.71e-07

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: 48.26  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAiVRDLCRlFSGDVVLTardVTRGQAAVQQlqaeglsprfhqlDIDDLQSIR-ALRDFLRKEYGGLDVL 87
Cdd:cd05328    3 VITGAASGIGAA-TAELLE-DAGHTVIG---IDLREADVIA-------------DLSTPEGRAaAIADVLARCSGVLDGL 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 557948119  88 VNNAGiafkVADPTPfhiqAEVTMKTNFFGTRDVCTELLPLIKP 131
Cdd:cd05328   65 VNCAG----VGGTTV----AGLVLKVNYFGLRALMEALLPRLRK 100
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-91 4.11e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 48.14  E-value: 4.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEE-GANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81


                 ....*
gi 557948119  87 LVNNA 91
Cdd:PRK07677  82 LINNA 86
PRK06953 PRK06953
SDR family oxidoreductase;
6-129 4.25e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 48.14  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSGD-VVLTARDvtrgQAAVQQLQAegLSPRFHQLDIDDLQSIRALRDFLRKEygGL 84
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRA--DGWrVIATARD----AAALAALQA--LGAEALALDVADPASVAGLAWKLDGE--AL 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  85 DVLVNNAGI--AFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLI 129
Cdd:PRK06953  72 DAAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLV 118
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 10-136 4.38e-07

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: 47.83  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  10 VTGGNKGIGLAIVRDLCR--LFSGdvvltARDV-TRGQAAVQ-QLQAEGLSPrfHQLDIDDLQSIR-ALRDFLRKEYGGL 84
Cdd:cd08931    5 ITGAASGIGRETALLFARngWFVG-----LYDIdEDGLAALAaELGAENVVA--GALDVTDRAAWAaALADFAAATGGRL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557948119  85 DVLVNNAGIafkvADPTPFHIQ----AEVTMKTNFFGTRDVCTELLPLIK--PQASCV 136
Cdd:cd08931   78 DALFNNAGV----GRGGPFEDVplaaHDRMVDINVKGVLNGAYAALPYLKatPGARVI 131
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 7-93 5.06e-07

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: 47.92  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08936   12 VALVTASTDGIGLAIARRLAQD-GAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDI 90


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:cd08936   91 LVSNAAV 97
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 8-91 5.13e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 48.03  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK07576  12 VVVVGGTSGINLGIAQAFARA-GANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDVL 90


                 ....
gi 557948119  88 VNNA 91
Cdd:PRK07576  91 VSGA 94
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 7-136 5.82e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 47.71  E-value: 5.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNkGIGLAIVRdlcRLFSGDVVLTA-RDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRkEYGGLD 85
Cdd:PRK06940   4 VVVVIGAG-GIGQAIAR---RVGAGKKVLLAdYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQ-TLGPVT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  86 VLVNNAGIafkvadpTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQASCV 136
Cdd:PRK06940  79 GLVHTAGV-------SPSQASPEAILKVDLYGTALVLEEFGKVIAPGGAGV 122
PRK05993 PRK05993
SDR family oxidoreductase;
9-134 6.73e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 47.71  E-value: 6.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDvtrgQAAVQQLQAEGLSPrfHQLDIDDLQSIRALRD-FLRKEYGGLDV 86
Cdd:PRK05993   8 LITGCSSGIGAYCARALQS--DGwRVFATCRK----EEDVAALEAEGLEA--FQLDYAEPESIAALVAqVLELSGGRLDA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557948119  87 LVNNA--GIAFKVAD-PT-PFHIQAEvtmkTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK05993  80 LFNNGayGQPGAVEDlPTeALRAQFE----ANFFGWHDLTRRVIPVMRKQGQ 127
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 7-117 6.89e-07

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: 47.38  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05360    2 VVVITGASSGIGRATAL----AFAERgakVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGR 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 557948119  84 LDVLVNNAGIA-FKVADPTPFHIQAEVtMKTNFFG 117
Cdd:cd05360   78 IDTWVNNAGVAvFGRFEDVTPEEFRRV-FDVNYLG 111
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 7-94 7.14e-07

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: 47.47  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTardVTRGQAAVQQLQAE--GLSPRfhQLDIDDLQSIRalrdFLRKEYGGL 84
Cdd:cd05351    9 RALVTGAGKGIGRATVKALAK--AGARVVA---VSRTQADLDSLVREcpGIEPV--CVDLSDWDATE----EALGSVGPV 77

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:cd05351   78 DLLVNNAAVA 87
PRK06194 PRK06194
hypothetical protein; Provisional
 7-94 1.16e-06

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 46.93  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfsG-DVVLTarDVTRG--QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK06194   8 VAVITGAASGFGLAFARIGAAL--GmKLVLA--DVQQDalDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGA 83

                         90
                 ....*....|.
gi 557948119  84 LDVLVNNAGIA 94
Cdd:PRK06194  84 VHLLFNNAGVG 94
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-121 1.26e-06

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 46.90  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVTRGQAAVQQLQAEglsprFHQLDIDDLQSI-RALRDFlrkeygglDV 86
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLAR--GhEVVGLDRSPPGAANLAALPGVE-----FVRGDLRDPEALaAALAGV--------DA 67

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAGIA-FKVADPtpfhiqaEVTMKTNFFGTRDV 121
Cdd:COG0451   68 VVHLAAPAgVGEEDP-------DETLEVNVEGTLNL 96
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 1.31e-06

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 46.64  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06077   8 VVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVADI 87


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK06077  88 LVNNAGL 94
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 7-141 1.69e-06

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: 46.42  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEG-LSPRFHQLDIDDL--QSIRALRDFLRKEYGG 83
Cdd:cd05340    6 IILVTGASDGIGREAALTYAR-YGATVILLGRNEEKLRQVADHINEEGgRQPQWFILDLLTCtsENCQQLAQRIAVNYPR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557948119  84 LDVLVNNAGIafkVADPTPFHIQ--------AEVTMKTNFFGTRdvctELLPLIK--PQASCVLSAWS 141
Cdd:cd05340   85 LDGVLHNAGL---LGDVCPLSEQnpqvwqdv*QVNVNATFMLTQ----ALLPLLLksDAGSLVFTSSS 145
PRK08278 PRK08278
SDR family oxidoreductase;
8-92 1.94e-06

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 46.44  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDV--------TRGQAAvQQLQAEGLSPRFHQLDIDDLQSIRALRDFLR 78
Cdd:PRK08278   9 LFITGASRGIGLAIALRAAR--DGaNIVIAAKTAephpklpgTIHTAA-EEIEAAGGQALPLVGDVRDEDQVAAAVAKAV 85

                         90
                 ....*....|....
gi 557948119  79 KEYGGLDVLVNNAG 92
Cdd:PRK08278  86 ERFGGIDICVNNAS 99
PRK07024 PRK07024
SDR family oxidoreductase;
10-133 2.21e-06

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 46.08  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  10 VTGGNKGIGLAIVRDLCRlfSGDVV-LTARDVTRGQAAVQQLQAEGlSPRFHQLDIDDLQSIR-ALRDFLrKEYGGLDVL 87
Cdd:PRK07024   7 ITGASSGIGQALAREYAR--QGATLgLVARRTDALQAFAARLPKAA-RVSVYAADVRDADALAaAAADFI-AAHGLPDVV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  88 VNNAGIAFKV-----ADPTPFhiqaEVTMKTNFFGtrdVCTELLPLIKPQA 133
Cdd:PRK07024  83 IANAGISVGTlteerEDLAVF----REVMDTNYFG---MVATFQPFIAPMR 126
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-97 2.23e-06

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 46.16  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12938   5 IAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84

                         90
                 ....*....|.
gi 557948119  87 LVNNAGIAFKV 97
Cdd:PRK12938  85 LVNNAGITRDV 95
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 8-100 2.26e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 46.10  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK05876   9 AVITGGASGIGLATGTEFARR-GARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVV 87

                         90
                 ....*....|...
gi 557948119  88 VNNAGIAfkVADP 100
Cdd:PRK05876  88 FSNAGIV--VGGP 98
PRK12742 PRK12742
SDR family oxidoreductase;
8-94 2.32e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 45.90  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRdlcRLFS--GDVVLTArdVTRGQAAvQQLQAEGLSPRFhQLDIDDlqsIRALRDFLRkEYGGLD 85
Cdd:PRK12742   9 VLVLGGSRGIGAAIVR---RFVTdgANVRFTY--AGSKDAA-ERLAQETGATAV-QTDSAD---RDAVIDVVR-KSGALD 77


                 ....*....
gi 557948119  86 VLVNNAGIA 94
Cdd:PRK12742  78 ILVVNAGIA 86
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-93 2.50e-06

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 45.86  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDL----CRLFSGDVVLTArDVTRGQAAVQQLQAEGLSPRFhQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMaeqgAKVFLTDINDAA-GLDAFAAEINAAHGEGVAFAA-VQDVTDEAQWQALLAQAADAMGG 79

                         90
                 ....*....|
gi 557948119  84 LDVLVNNAGI 93
Cdd:PRK07069  80 LSVLVNNAGV 89
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 6-99 2.84e-06

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 46.45  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDvtrgQAAVQQLQAEgLSPRFHQLDIDDLQSIRALRDFLRK---- 79
Cdd:COG3347  426 RVALVTGGAGGIGRATAA---RLAAegAAVVVADLD----GEAAEAAAAE-LGGGYGADAVDATDVDVTAEAAVAAafgf 497

                         90       100
                 ....*....|....*....|...
gi 557948119  80 ---EYGGLDVLVNNAGIAFKVAD 99
Cdd:COG3347  498 aglDIGGSDIGVANAGIASSSPE 520
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 6-103 2.99e-06

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 45.61  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQ--AAVQQL--QAEGLSprfhqLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK06113  12 KCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHvvDEIQQLggQAFACR-----CDITSEQELSALADFALSKL 86

                         90       100
                 ....*....|....*....|..
gi 557948119  82 GGLDVLVNNAGiafkVADPTPF 103
Cdd:PRK06113  87 GKVDILVNNAG----GGGPKPF 104
PRK07775 PRK07775
SDR family oxidoreductase;
8-127 6.97e-06

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 44.75  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAA-GFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 557948119  88 VNNAG-IAFKVA---DPTPFHIQAEVtmktNFFGTRDVCTELLP 127
Cdd:PRK07775  92 VSGAGdTYFGKLheiSTEQFESQVQI----HLVGANRLATAVLP 131
PRK08177 PRK08177
SDR family oxidoreductase;
6-94 8.12e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 44.25  E-value: 8.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQA--AVQQLQAEglsprfhQLDIDDLQSIRALRDFLRKEYg 82
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLE--RGwQVTATVRGPQQDTAlqALPGVHIE-------KLDMNDPASLDQLLQRLQGQR- 71

                         90
                 ....*....|..
gi 557948119  83 gLDVLVNNAGIA 94
Cdd:PRK08177  72 -FDLLFVNAGIS 82
PRK07985 PRK07985
SDR family oxidoreductase;
8-148 1.37e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 43.83  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAA-VQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07985  52 ALVTGGDSGIGRAAAIAYARE-GADVAISYLPVEEEDAQdVKKIIEEcGRKAVLLPGDLSDEKFARSLVHEAHKALGGLD 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  86 VLVNNAGIAFKV---ADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQASCVLSAwSCLSQNPS 148
Cdd:PRK07985 131 IMALVAGKQVAIpdiADLTSEQFQK--TFAINVFALFWLTQEAIPLLPKGASIITTS-SIQAYQPS 193
PRK09186 PRK09186
flagellin modification protein A; Provisional
 7-91 1.42e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.83  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCrLFSGDVVLTARDVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK09186   6 TILITGAGGLIGSALVKAIL-EAGGIVIAADIDKEALNELLESLGKEFKSKKlsLVELDITDQESLEEFLSKSAEKYGKI 84


                 ....*..
gi 557948119  85 DVLVNNA 91
Cdd:PRK09186  85 DGAVNCA 91
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-93 1.93e-05

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: 42.93  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVT---RGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLVLLSRSAAprpDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83


                  ....*...
gi 557948119   86 VLVNNAGI 93
Cdd:pfam08659  84 GVIHAAGV 91
PRK12746 PRK12746
SDR family oxidoreductase;
7-136 2.54e-05

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 43.10  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEY----- 81
Cdd:PRK12746   8 VALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELqirvg 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  82 -GGLDVLVNNAGIAFK--VADPTP--FHIQAEVTMKTNFFgtrdVCTELLPLIKPQASCV 136
Cdd:PRK12746  88 tSEIDILVNNAGIGTQgtIENTTEeiFDEIMAVNIKAPFF----LIQQTLPLLRAEGRVI 143
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 7-127 2.64e-05

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). 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: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 42.75  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTR-GQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAA--EGfSVALAARREAKlEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948119  85 DVLVNNAG--IAFKVADPTP--FHIQAEVTMKTNFFGTRDVCTELLP 127
Cdd:cd05373   79 EVLVYNAGanVWFPILETTPrvFEKVWEMAAFGGFLAAREAAKRMLA 125
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 7-93 2.70e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 43.02  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVR--------------------DLCRLFSGDVVLTARDVTRG---QAAVQQlqaeglsprfhqld 63
Cdd:PRK06200   8 VALITGGGSGIGRALVErflaegarvavlersaeklaSLRQRFGDHVLVVEGDVTSYadnQRAVDQ-------------- 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 557948119  64 iddlqsirALRDFlrkeyGGLDVLVNNAGI 93
Cdd:PRK06200  74 --------TVDAF-----GKLDCFVGNAGI 90
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 8-121 5.74e-05

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 41.82  E-value: 5.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSGDVV-LTARDVTRGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12936   9 ALVTGASGGIGEEIARLLHA--QGAIVgLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEGVDI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 557948119  87 LVNNAGIA-----FKVADPTpFHIQAEVTMKTNFFGTRDV 121
Cdd:PRK12936  84 LVNNAGITkdglfVRMSDED-WDSVLEVNLTATFRLTREL 122
PRK09134 PRK09134
SDR family oxidoreductase;
7-93 5.86e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 41.84  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVT-RGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK09134  11 AALVTGAARRIGRAIALDLAA--HGfDVAVHYNRSRdEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGPI 88


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:PRK09134  89 TLLVNNASL 97
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
5-93 5.95e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 41.98  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   5 IHVALVTGGNKGIGLAIVRDLcrLFSGDVVLTardVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSI-RALRDFLR--- 78
Cdd:PRK06924   1 MRYVIITGTSQGLGEAIANQL--LEKGTHVIS---ISRTENKELTKLAEQYNSNltFHSLDLQDVHELeTNFNEILSsiq 75

                         90
                 ....*....|....*.
gi 557948119  79 -KEYGGLdVLVNNAGI 93
Cdd:PRK06924  76 eDNVSSI-HLINNAGM 90
PRK05717 PRK05717
SDR family oxidoreductase;
7-94 6.37e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 41.80  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVTRGQAAVQQLqaeGLSPRFHQLDI-DDLQSIRALRDFLRkEYGGL 84
Cdd:PRK05717  12 VALVTGAARGIGLGIAAWL--IAEGwQVVLADLDRERGSKVAKAL---GENAWFIAMDVaDEAQVAAGVAEVLG-QFGRL 85

                         90
                 ....*....|
gi 557948119  85 DVLVNNAGIA 94
Cdd:PRK05717  86 DALVCNAAIA 95
PRK06482 PRK06482
SDR family oxidoreductase;
9-132 6.81e-05

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 42.02  E-value: 6.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDVtrgqAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06482   6 FITGASSGFGRGMTERL--LARGDrVAATVRRP----DALDDLKARyGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557948119  87 LVNNAGI-----AFKVADPtpfhiQAEVTMKTNFFGTRDVCTELLPLIKPQ 132
Cdd:PRK06482  80 VVSNAGYglfgaAEELSDA-----QIRRQIDTNLIGSIQVIRAALPHLRRQ 125
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 8-104 7.57e-05

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: 41.44  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLtardVTRGQAAVQQLQAE-----GLSPRFHQLDIDDLQSIralRDFLRKEY 81
Cdd:cd05356    4 AVVTGATDGIGKAYAEELAK--RGfNVIL----ISRTQEKLDAVAKEieekyGVETKTIAADFSAGDDI---YERIEKEL 74

                         90       100
                 ....*....|....*....|....*
gi 557948119  82 GGLDV--LVNNAGIAFKVadPTPFH 104
Cdd:cd05356   75 EGLDIgiLVNNVGISHSI--PEYFL 97
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-94 8.38e-05

ketoreductase (KR) and fatty acid synthase (FAS), 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. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. 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. 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: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 41.60  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDV--TRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEyGGLDV 86
Cdd:cd05274  154 LITGGLGGLGLLVARWLAARGARHLVLLSRRGpaPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAAG-GPLAG 232


                 ....*...
gi 557948119  87 LVNNAGIA 94
Cdd:cd05274  233 VIHAAGVL 240
PRK05867 PRK05867
SDR family oxidoreductase;
8-93 9.38e-05

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 41.56  E-value: 9.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVrdLCRLFSG-DVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05867  12 ALITGASTGIGKRVA--LAYVEAGaQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDI 89


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:PRK05867  90 AVCNAGI 96
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-93 9.64e-05

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 41.43  E-value: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVltarDVTRGQAAVQQLQAEGLSPRFHQL--DIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12481  10 VAIITGCNTGLGQGMAIGLAKA-GADIV----GVGVAEAPETQAQVEALGRKFHFItaDLIQQKDIDSIVSQAVEVMGHI 84


                 ....*....
gi 557948119  85 DVLVNNAGI 93
Cdd:PRK12481  85 DILINNAGI 93
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 7-93 1.14e-04

(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: 41.15  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLA------------IVRDLcrlfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSI--RA 72
Cdd:cd05353    7 VVLVTGAGGGLGRAyalafaergakvVVNDL----GGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIvkTA 82

                         90       100
                 ....*....|....*....|.
gi 557948119  73 LrdflrKEYGGLDVLVNNAGI 93
Cdd:cd05353   83 I-----DAFGRVDILVNNAGI 98
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 8-126 1.57e-04

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 40.74  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    8 ALVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVTRGQAAVqqlqaeGLSPRFHQLDIDDlqsIRALRDFLRKEygGLDV 86
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRL--LEKGyEVIGLDRLTSASNTAR------LADLRFVEGDLTD---RDALEKLLADV--RPDA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 557948119   87 LVNNAGIAFKVADptpfHIQAEVTMKTNFFGTRDVCTELL 126
Cdd:pfam01370  68 VIHLAAVGGVGAS----IEDPEDFIEANVLGTLNLLEAAR 103
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 7-109 2.46e-04

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 40.31  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARdvtrgQAAVQQLQAEGLSPRFHQL----DIDDLQSIRALRDFLRKEYG 82
Cdd:PRK12823  10 VVVVTGAAQGIGRGVALRAAAE-GARVVLVDR-----SELVHEVAAELRAAGGEALaltaDLETYAGAQAAMAAAVEAFG 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 557948119  83 GLDVLVNNAG--IAFK-VADPTPFHIQAEV 109
Cdd:PRK12823  84 RIDVLINNVGgtIWAKpFEEYEEEQIEAEI 113
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
47-134 2.80e-04

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 40.11  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  47 VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPF-HIQAE---VTMKTNFFGTRDVC 122
Cdd:PRK08415  47 VEPIAQELGSDYVYELDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFAPKEALEGSFlETSKEafnIAMEISVYSLIELT 126

                         90
                 ....*....|..
gi 557948119 123 TELLPLIKPQAS 134
Cdd:PRK08415 127 RALLPLLNDGAS 138
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 9-136 3.07e-04

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 39.86  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVTRGQAAVQQLQAEGLS-PRFHQLDID--DLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08945  16 LVTGAGDGIGREAALTYAR-HGATVILLGRTEEKLEAVYDEIEAAGGPqPAIIPLDLLtaTPQNYQQLADTIEEQFGRLD 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557948119  86 VLVNNAGIafkVADPTPF-HIQAEV---TMKTNFFGTRDVCTELLPLIK--PQASCV 136
Cdd:PRK08945  95 GVLHNAGL---LGELGPMeQQDPEVwqdVMQVNVNATFMLTQALLPLLLksPAASLV 148
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 7-117 3.78e-04

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: 39.76  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05322    4 VAVVIGGGQTLGEFLCHGLAE--AGyDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFKRV 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557948119  85 DVLVNNAGIAfKVADPTPFHIQA-EVTMKTNFFG 117
Cdd:cd05322   82 DLLVYSAGIA-KSAKITDFELGDfDRSLQVNLVG 114
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 1-91 3.86e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 39.53  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   1 MSSGIhvaLVTGGNKGIGLAIVRDLcrLFSG-DVVLTARdvtRGQAAVQQLQAEGLSprFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK06483   1 MPAPI---LITGAGQRIGLALAWHL--LAQGqPVIVSYR---THYPAIDGLRQAGAQ--CIQADFSTNAGIMAFIDELKQ 70

                         90
                 ....*....|..
gi 557948119  80 EYGGLDVLVNNA 91
Cdd:PRK06483  71 HTDGLRAIIHNA 82
PRK06720 PRK06720
hypothetical protein; Provisional
 7-138 4.30e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 38.80  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06720  18 VAIVTGGGIGIGRNTALLLAKQ-GAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSRIDM 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  87 LVNNAGIaFKVadPTPFHIQAEvtMKTNFFGTRDVCTELLPL----IKPQASCVLS 138
Cdd:PRK06720  97 LFQNAGL-YKI--DSIFSRQQE--NDSNVLCINDVWIEIKQLtssfMKQQEEVVLS 147
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 9-92 4.61e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 39.40  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGL--SPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAA-GAAVMIVGRNPDKLAAAAEEIEALKGagAVRYEPADVTDEDQVARAVDAATAWHGRLHG 89


                 ....*.
gi 557948119  87 LVNNAG 92
Cdd:PRK05875  90 VVHCAG 95
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 8-95 4.99e-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: 39.10  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRlfSGDVVLTArdvtrgqaavqqlqaeGLSPRFHQLDIDDLQSIRALrdFlrKEYGGLDVL 87
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSA--HGHEVITA----------------GRSSGDYQVDITDEASIKAL--F--EKVGHFDAI 58


                 ....*...
gi 557948119  88 VNNAGIAF 95
Cdd:cd11731   59 VSTAGDAE 66
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-98 6.34e-04

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: 39.14  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPrfhQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05363    5 TALITGSARGIGRAFAQAYVRE-GARVAIADINLEAARATAAEIGPAACAI---SLDVTDQASIDRCVAALVDRWGSIDI 80

                         90
                 ....*....|..
gi 557948119  87 LVNNAGiAFKVA 98
Cdd:cd05363   81 LVNNAA-LFDLA 91
PRK09009 PRK09009
SDR family oxidoreductase;
9-93 6.69e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 38.89  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRgqaavQQLQAEGLSprFHQLDIDDLQSIRAlrdfLRKEYGGLDVLV 88
Cdd:PRK09009   4 LIVGGSGGIGKAMVKQLLERYPDATVHATYRHHK-----PDFQHDNVQ--WHALDVTDEAEIKQ----LSEQFTQLDWLI 72


                 ....*
gi 557948119  89 NNAGI 93
Cdd:PRK09009  73 NCVGM 77
PRK07577 PRK07577
SDR family oxidoreductase;
8-94 7.15e-04

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 38.55  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTrgqaavqqlqaEGLSPRFHQLDIDDL-QSIRALRDFLrkEYGGLDV 86
Cdd:PRK07577   6 VLVTGATKGIGLALSLRLANL-GHQVIGIARSAI-----------DDFPGELFACDLADIeQTAATLAQIN--EIHPVDA 71


                 ....*...
gi 557948119  87 LVNNAGIA 94
Cdd:PRK07577  72 IVNNVGIA 79
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
59-136 7.81e-04

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 38.83  E-value: 7.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557948119  59 FHQLDIDDLQSIRALrdfLRKEYGGLDVLVNNAGIAfKVADPtpfhiqaEVTMKTNFFGTRDVCTELLPLIKPQASCV 136
Cdd:PRK12428  27 FIQADLGDPASIDAA---VAALPGRIDALFNIAGVP-GTAPV-------ELVARVNFLGLRHLTEALLPRMAPGGAIV 93
PRK12744 PRK12744
SDR family oxidoreductase;
7-96 9.55e-04

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 38.57  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVL---TARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK12744  10 VVLIAGGAKNLGGLIARDLAAQGAKAVAIhynSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFGR 89

                         90
                 ....*....|...
gi 557948119  84 LDVLVNNAGIAFK 96
Cdd:PRK12744  90 PDIAINTVGKVLK 102
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-93 1.20e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 38.32  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVltARDVTRGQAAVQQLQAEG---LSPRFHQLDIDDLQSI--RALrdflrKE 80
Cdd:PRK08993  12 VAVVTGCDTGLGQGMALGLAE--AGcDIV--GINIVEPTETIEQVTALGrrfLSLTADLRKIDGIPALleRAV-----AE 82

                         90
                 ....*....|...
gi 557948119  81 YGGLDVLVNNAGI 93
Cdd:PRK08993  83 FGHIDILVNNAGL 95
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 7-93 1.46e-03

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: 37.72  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVR--------------------DLCRLFSGDVVLTARDVTrgqaavqqlqaeglsprfhqlDIDD 66
Cdd:cd05348    6 VALITGGGSGLGRALVErfvaegakvavldrsaekvaELRADFGDAVVGVEGDVR---------------------SLAD 64

                         90       100
                 ....*....|....*....|....*..
gi 557948119  67 LQsiRALRDFLRKeYGGLDVLVNNAGI 93
Cdd:cd05348   65 NE--RAVARCVER-FGKLDCFIGNAGI 88
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 6-93 1.49e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. 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. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 38.00  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLtardVTRGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDflrkeyg 82
Cdd:cd05271    1 MVVTVFGATGFIGRYVVNRLAK--RGsQVIV----PYRCEAYARRLLVMGDLGQvlFVEFDLRDDESIRKALE------- 67

                         90
                 ....*....|.
gi 557948119  83 GLDVLVNNAGI 93
Cdd:cd05271   68 GSDVVINLVGR 78
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 10-91 1.82e-03

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: 37.42  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119  10 VTGGNKGIGLAIVRDLCRlFSGDVVLTARD----------VTRGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRK 79
Cdd:cd09762    8 ITGASRGIGKAIALKAAR-DGANVVIAAKTaephpklpgtIYTAAEEIEAAGGKALPCI---VDIRDEDQVRAAVEKAVE 83

                         90
                 ....*....|..
gi 557948119  80 EYGGLDVLVNNA 91
Cdd:cd09762   84 KFGGIDILVNNA 95
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-93 2.01e-03

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: 37.47  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVTRGqAAVQQLQAEGLSprfhqLDIDDLQSIRALRDFLRK--EYGGLD 85
Cdd:cd08951   11 FITGSSDGLGLAAARTL--LHQGhEVVLHARSQKRA-ADAKAACPGAAG-----VLIGDLSSLAETRKLADQvnAIGRFD 82


                 ....*...
gi 557948119  86 VLVNNAGI 93
Cdd:cd08951   83 AVIHNAGI 90
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-92 2.14e-03

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: 37.58  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119    7 VALVTGGNKGIGLAIVRDL--CRLFSG-DVVLTARDvtrgQAAVQQLQAEGLSPRfHQLDID----DLQSIRALRDFLR- 78
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELakCLKSPGsVLVLSARN----DEALRQLKAEIGAER-SGLRVVrvslDLGAEAGLEQLLKa 76

                          90       100
                  ....*....|....*....|.
gi 557948119   79 -------KEYGGLdVLVNNAG 92
Cdd:TIGR01500  77 lrelprpKGLQRL-LLINNAG 96
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 8-92 2.67e-03

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) 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. 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. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. 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. 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: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 36.61  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   8 ALVTGGNKGIGLAIVRDLCRLFSgDVVLTARDVTRGQAAVQQLQAeglsprFHQLDIDDLQSIRALRDflrkeygGLDVL 87
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGH-EVTLLVRNTKRLSKEDQEPVA------VVEGDLRDLDSLSDAVQ-------GVDVV 66


                 ....*
gi 557948119  88 VNNAG 92
Cdd:cd05226   67 IHLAG 71
PRK08251 PRK08251
SDR family oxidoreductase;
9-93 3.36e-03

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 36.84  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGlaivRDLCRLFSG---DVVLTARDVTRGQAAVQQLQAE--GLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK08251   6 LITGASSGLG----AGMAREFAAkgrDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGG 81

                         90
                 ....*....|
gi 557948119  84 LDVLVNNAGI 93
Cdd:PRK08251  82 LDRVIVNAGI 91
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 7-90 3.83e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 36.90  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDvTRGQAA--------------VQQLQAEGLSPRFHQLDIDDlqsIR 71
Cdd:PRK08303  10 VALVAGATRGAGRGIAVELGA--AGaTVYVTGRS-TRARRSeydrpetieetaelVTAAGGRGIAVQVDHLVPEQ---VR 83

                         90
                 ....*....|....*....
gi 557948119  72 ALRDFLRKEYGGLDVLVNN 90
Cdd:PRK08303  84 ALVERIDREQGRLDILVND 102
PRK07102 PRK07102
SDR family oxidoreductase;
9-134 4.23e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 36.44  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRdlcrLFSG---DVVLTARDVTRGQAAVQQLQAEG-LSPRFHQLDIDDLQSIRALrdflrkeYGGL 84
Cdd:PRK07102   5 LIIGATSDIARACAR----RYAAagaRLYLAARDVERLERLADDLRARGaVAVSTHELDILDTASHAAF-------LDSL 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557948119  85 DVLVNNAGIAF------KVADPTPFHIQAEvtMKTNFFGTRDVCTELLPLIKPQAS 134
Cdd:PRK07102  74 PALPDIVLIAVgtlgdqAACEADPALALRE--FRTNFEGPIALLTLLANRFEARGS 127
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-94 4.38e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 36.59  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG--- 83
Cdd:PRK12747   6 VALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQNrtg 85

                         90
                 ....*....|....
gi 557948119  84 ---LDVLVNNAGIA 94
Cdd:PRK12747  86 stkFDILINNAGIG 99
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 7-103 5.23e-03

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 36.17  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVTRGQAAVQQLQAE---GLSPRFhQLDIDDLQSIRALRDFLRKEYG 82
Cdd:PRK12384   4 VAVVIGGGQTLGAFLCHGLAE--EGyRVAVADINSEKAANVAQEINAEygeGMAYGF-GADATSEQSVLALSRGVDEIFG 80

                         90       100
                 ....*....|....*....|.
gi 557948119  83 GLDVLVNNAGIAfKVADPTPF 103
Cdd:PRK12384  81 RVDLLVYNAGIA-KAAFITDF 100
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 7-93 5.60e-03

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: 36.29  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLtARDVTrgQAAVQQLQAEGLSPRfHQLDIDDLQSIRALRdflrKEYGGLDV 86
Cdd:cd05368    4 VALITAAAQGIGRAIALAFAR--EGANVI-ATDIN--EEKLKELERGPGITT-RVLDVTDKEQVAALA----KEEGRIDV 73


                 ....*..
gi 557948119  87 LVNNAGI 93
Cdd:cd05368   74 LFNCAGF 80
PRK07041 PRK07041
SDR family oxidoreductase;
9-91 8.80e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 35.40  E-value: 8.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQaEGLSPRFHQLDIDDLQSIRALrdFlrKEYGGLDVLV 88
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAE-GARVTIASRSRDRLAAAARALG-GGAPVRTAALDITDEAAVDAF--F--AEAGPFDHVV 74


                 ...
gi 557948119  89 NNA 91
Cdd:PRK07041  75 ITA 77
PRK08340 PRK08340
SDR family oxidoreductase;
9-92 8.96e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 35.55  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948119   9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQldidDLQSIRALRDFLRKEY---GGLD 85
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKK-GARVVISSRNEENLEKALKELKEYGEVYAVKA----DLSDKDDLKNLVKEAWellGGID 78


                 ....*..
gi 557948119  86 VLVNNAG 92
Cdd:PRK08340  79 ALVWNAG 85
 
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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