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Conserved domains on  [gi|158256544|dbj|BAF84245|]
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unnamed protein product [Homo sapiens]

Protein Classification

3 beta-hydroxysteroid dehydrogenase family protein( domain architecture ID 10176861)

3 beta-hydroxysteroid dehydrogenase family protein plays a crucial role in the biosynthesis of all classes of hormonal steroids; similar to 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1/2 and 3 beta-hydroxysteroid dehydrogenase type 7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 0e+00

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 618.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVKEKE-LKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 164 KAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNP-VYVGNVAWAHILALRALQD 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 243 PKKApsIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLD-SRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVT 321
Cdd:cd09811  241 PDKA--IRGQFYFISDDTPHNSYSDFNYELLKELGLRLKtSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158256544 322 LSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWV 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
 
Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 0e+00

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 618.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVKEKE-LKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 164 KAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNP-VYVGNVAWAHILALRALQD 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 243 PKKApsIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLD-SRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVT 321
Cdd:cd09811  241 PDKA--IRGQFYFISDDTPHNSYSDFNYELLKELGLRLKtSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158256544 322 LSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWV 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 1.91e-158

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 446.04  E-value: 1.91e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTkltVLEGDILDEPFLKRACQDVSVIIHTACII 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNVIK---YIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   87 DVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  167 LAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGIL-SSVGKFSTVNPVYVGNVAWAHILALRALQDPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKfKTGDDNNLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 158256544  246 APSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSrWSFPL 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLPS-ISLPL 279
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-356 1.75e-45

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 157.83  E-value: 1.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKafgpeLREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACII 86
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGH--EVVGLDR-----SPPGAANLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  87 DVfGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNsykeiiqngheEEPLENTWPA----PYPHSKKLA 162
Cdd:COG0451   76 GV-GEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDG-----------EGPIDEDTPLrpvsPYGASKLAA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 163 EKAVLA-ANGWNLKnggtlyTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFS-TVNPVYVGNVAWAHILALRAl 240
Cdd:COG0451  144 ELLARAyARRYGLP------VTILRPGNVYGPGDRGVLPRLIRRALAGEPVPVFGDGDqRRDFIHVDDVARAIVLALEA- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 241 qdpkkaPSIRGQFYYISDDTPhqsydnlnytlskefglrldsrwsfpLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIV 320
Cdd:COG0451  217 ------PAAPGGVYNVGGGEP--------------------------VTLRELAEAIAEALGRPPEIVYPARPGDVRPRR 264
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158256544 321 tLSNSvftfsykKAQRDLAYKPLYSWEEAKQKTVEW 356
Cdd:COG0451  265 -ADNS-------KARRELGWRPRTSLEEGLRETVAW 292
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-215 6.48e-12

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 66.28  E-value: 6.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPE---------LREEFSKLQNKT--KLTVLEGDI------LDEPFL 69
Cdd:TIGR01746   3 LLTGATGFLGAYLLEELLRRSTRAKVICLVRADSEEhamerlreaLRSYRLWHENLAmeRIEVVAGDLskprlgLSDAEW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   70 KRACQDVSVIIHTACIIDVFGvtHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQngHEEEPLEN 149
Cdd:TIGR01746  83 ERLAENVDTIVHNGALVNHVY--PYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVT--EDDATVTP 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158256544  150 --TWPAPYPHSKKLAEKAVLAANgwNLKNGGTLYtcalRPMYIygegsrfLSASINEALNNNGILSSV 215
Cdd:TIGR01746 159 ypGLAGGYTQSKWVAELLVREAS--DRGLPVTIV----RPGRI-------LGDSYTGAWNSSDILWRM 213
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
7-168 2.72e-07

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 52.44  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDK----AFGPELREEFSKLQNK-TKLTVLEGDILDepFLKRAcQDVSVIIH 81
Cdd:PLN02260  10 LITGAAGFIASHVANRLIRNYPDYKIVVLDKldycSNLKNLNPSKSSPNFKfVKGDIASADLVN--YLLIT-EGIDTIMH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  82 TACIIDV---FGVTHrESIMNvNVKGTQLLLEAC-VQASVPVFIYTSSIEVAGPNSYKEIIQNgHEEEPLENTwpAPYPH 157
Cdd:PLN02260  87 FAAQTHVdnsFGNSF-EFTKN-NIYGTHVLLEACkVTGQIRRFIHVSTDEVYGETDEDADVGN-HEASQLLPT--NPYSA 161
                        170
                 ....*....|.
gi 158256544 158 SKKLAEKAVLA 168
Cdd:PLN02260 162 TKAGAEMLVMA 172
 
Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 0e+00

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 618.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVKEKE-LKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 164 KAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNP-VYVGNVAWAHILALRALQD 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 243 PKKApsIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLD-SRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVT 321
Cdd:cd09811  241 PDKA--IRGQFYFISDDTPHNSYSDFNYELLKELGLRLKtSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158256544 322 LSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWV 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 1.91e-158

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 446.04  E-value: 1.91e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTkltVLEGDILDEPFLKRACQDVSVIIHTACII 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNVIK---YIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   87 DVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  167 LAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGIL-SSVGKFSTVNPVYVGNVAWAHILALRALQDPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKfKTGDDNNLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 158256544  246 APSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSrWSFPL 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLPS-ISLPL 279
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
5-356 4.15e-108

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 320.15  E-value: 4.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVkEKELKEIRVLDKAFgpeLREEFSKlQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTAC 84
Cdd:cd05241    1 SVLVTGGSGFFGERLVKQLL-ERGGTYVRSFDIAP---PGEALSA-WQHPNIEFLKGDITDRNDVEQALSGADCVFHTAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVFGvtHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPnsyKEIIQNGHEEEPLENTWPAPYPHSKKLAEK 164
Cdd:cd05241   76 IVPLAG--PRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFG---GQNIHNGDETLPYPPLDSDMYAETKAIAEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 165 AVLAANGwnlknGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVG-KFSTVNPVYVGNVAWAHILALRALQDP 243
Cdd:cd05241  151 IVLEANG-----RDDLLTCALRPAGIFGPGDQGLVPILFEWAEKGLVKFVFGrGNNLVDFTYVHNLAHAHILAAAALVKG 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 244 KKapsIRGQFYYISDDTPHQSYDNLNYTLSK-EFGLRLDSRWSFPlsLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVTl 322
Cdd:cd05241  226 KT---ISGQTYFITDAEPHNMFELLRPVWKAlGFGSRPKIRLSGP--LAYCAALLSELVSFMLGPYFVFSPFYVRALVT- 299
                        330       340       350
                 ....*....|....*....|....*....|....
gi 158256544 323 snsVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEW 356
Cdd:cd05241  300 ---PMYFSIAKAQKDLGYAPRYSNEEGLIETLNW 330
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
5-356 1.62e-60

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 198.35  E-value: 1.62e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVkEKELKEIRVLDKAFGPELREEFSKlqnktKLTVLEGDILDEPFLKRA--CQDVSVIIHT 82
Cdd:cd09813    1 SCLVVGGSGFLGRHLVEQLL-RRGNPTVHVFDIRPTFELDPSSSG-----RVQFHTGDLTDPQDLEKAfnEKGPNVVFHT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  83 ACiiDVFGVtHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSievAGPNSYKEIIQNGHEeeplenTWPAP------YP 156
Cdd:cd09813   75 AS--PDHGS-NDDLYYKVNVQGTRNVIEACRKCGVKKLVYTSS---ASVVFNGQDIINGDE------SLPYPdkhqdaYN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 157 HSKKLAEKAVLAANGwnlkNGGTLYTCALRPMYIYGEGSRFLSASINEALNNN------GILSSVGKFStvnpvYVGNVA 230
Cdd:cd09813  143 ETKALAEKLVLKAND----PESGLLTCALRPAGIFGPGDRQLVPGLLKAAKNGktkfqiGDGNNLFDFT-----YVENVA 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 231 WAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNyTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIyt 310
Cdd:cd09813  214 HAHILAADALLSSSHAETVAGEAFFITNDEPIYFWDFAR-AIWEGLGYERPPSIKLPRPVALYLASLLEWTCKVLGKE-- 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 158256544 311 yrPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEW 356
Cdd:cd09813  291 --PTFTPFRVALLCSTRYFNIEKAKKRLGYTPVVTLEEGIERTLQW 334
3b-HSD_like_1_SDR_e cd09812
3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An ...
5-356 2.50e-50

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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: 187672 [Multi-domain]  Cd Length: 339  Bit Score: 171.92  E-value: 2.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVKEKE---LKEIRVLDKAFGPELReefsklqnktkltVLEGDILDEPFLKRACQDVSVIIH 81
Cdd:cd09812    1 SVLITGGGGYFGFRLGCALAKSGVhviLFDIRRPQQELPEGIK-------------FIQADVRDLSQLEKAVAGVDCVFH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  82 TACiidvFGVT-----HRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNsykEIIQNGHEEEPL--ENTWPAP 154
Cdd:cd09812   68 IAS----YGMSgreqlNRELIEEINVRGTENIIQVCVRRRVPRLIYTSTFNVIFGG---QPIRNGDESLPYlpLDLHVDH 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 155 YPHSKKLAEKAVLAANGWNLKN-GGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKF-STVNPVYVGNVAWA 232
Cdd:cd09812  141 YSRTKSIAEQLVLKANNMPLPNnGGVLRTCALRPAGIYGPGEQRHLPRIVSYIEKGLFMFVYGDPkSLVEFVHVDNLVQA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 233 HILALRALQDPKKAPSiRGQFYYISDDTPHQSYDNLNyTLSKEFGLRLDSrWSFPLSLMYWIGFLLEIVSFLLRPIYTYR 312
Cdd:cd09812  221 HILAAEALTTAKGYIA-SGQAYFISDGRPVNNFEFFR-PLVEGLGYSFPS-LRLPLSLVYFFAFLTEMVHFALGPICNFQ 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 158256544 313 PPFNRHIVTLSNSVFTFSYKKAQRDLAYKP-LYSWEEAkqktVEW 356
Cdd:cd09812  298 PLLTRTEVYKTGVTHYFSIEKARAELGYEPqPFDLQDA----VEW 338
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-356 1.75e-45

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 157.83  E-value: 1.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKafgpeLREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACII 86
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGH--EVVGLDR-----SPPGAANLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  87 DVfGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNsykeiiqngheEEPLENTWPA----PYPHSKKLA 162
Cdd:COG0451   76 GV-GEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDG-----------EGPIDEDTPLrpvsPYGASKLAA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 163 EKAVLA-ANGWNLKnggtlyTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFS-TVNPVYVGNVAWAHILALRAl 240
Cdd:COG0451  144 ELLARAyARRYGLP------VTILRPGNVYGPGDRGVLPRLIRRALAGEPVPVFGDGDqRRDFIHVDDVARAIVLALEA- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 241 qdpkkaPSIRGQFYYISDDTPhqsydnlnytlskefglrldsrwsfpLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIV 320
Cdd:COG0451  217 ------PAAPGGVYNVGGGEP--------------------------VTLRELAEAIAEALGRPPEIVYPARPGDVRPRR 264
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158256544 321 tLSNSvftfsykKAQRDLAYKPLYSWEEAKQKTVEW 356
Cdd:COG0451  265 -ADNS-------KARRELGWRPRTSLEEGLRETVAW 292
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
7-356 3.80e-42

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 149.74  E-value: 3.80e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVL--DKAFGPELREEfsklqnktKLTVLEGDILDEPFLKRACQDVSVIIHTAC 84
Cdd:cd05228    2 LVTGATGFLGSNLVRALLAQGY--RVRALvrSGSDAVLLDGL--------PVEVVEGDLTDAASLAAAMKGCDRVFHLAA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVFGvTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNG-HEEEPLENtwpaPYPHSKKLAE 163
Cdd:cd05228   72 FTSLWA-KDRKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTpWNERPFPN----DYYRSKLLAE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 164 KAVLAAngwnLKNGgtLYTCALRPMYIYGEGSRFLSAS---INEALNnngilssvGKFSTVNP-----VYVGNVAWAHIL 235
Cdd:cd05228  147 LEVLEA----AAEG--LDVVIVNPSAVFGPGDEGPTSTgldVLDYLN--------GKLPAYPPggtsfVDVRDVAEGHIA 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 236 ALRALQdpkkapsiRGQFYYISDdtPHQSYDNLNYTLSKEFGLRLdSRWSFPLSLMYWIGFLLEIVSFLlrpiyTYRPP- 314
Cdd:cd05228  213 AMEKGR--------RGERYILGG--ENLSFKQLFETLAEITGVKP-PRRTIPPWLLKAVAALSELKARL-----TGKPPl 276
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 158256544 315 FNRHIVTLSNSVFTFSYKKAQRDLAYKPlYSWEEAKQKTVEW 356
Cdd:cd05228  277 LTPRTARVLRRNYLYSSDKARRELGYSP-RPLEEALRDTLAW 317
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
7-246 2.42e-24

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: 99.68  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKafgpelREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVS--VIIHTAC 84
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKGY--EVIGLDR------LTSASNTARLADLRFVEGDLTDRDALEKLLADVRpdAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   85 IIDVF-GVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSykeiIQNGHEEEPLENTWP-APYPHSKKLA 162
Cdd:pfam01370  74 VGGVGaSIEDPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGA----EIPQEETTLTGPLAPnSPYAAAKLAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  163 EKAVLAangWNLKNGgtLYTCALRPMYIYGEG------SRFLSASINEALNNNGILssvgKFSTVNP----VYVGNVAWA 232
Cdd:pfam01370 150 EWLVLA---YAAAYG--LRAVILRLFNVYGPGdnegfvSRVIPALIRRILEGKPIL----LWGDGTQrrdfLYVDDVARA 220
                         250
                  ....*....|....
gi 158256544  233 HILALRALQDPKKA 246
Cdd:pfam01370 221 ILLALEHGAVKGEI 234
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
6-356 3.24e-24

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 101.14  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   6 CLVTGAGGFLGQRIIRLLVKEKElkEIRVLDKaFGPELREEFSklQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACI 85
Cdd:cd05256    2 VLVTGGAGFIGSHLVERLLERGH--EVIVLDN-LSTGKKENLP--EVKPNVKFIEGDIRDDELVEFAFEGVDYVFHQAAQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  86 IDVfgvthRESIMN------VNVKGTQLLLEACVQASVPVFIYTSSIEVAGpnsykeiiqnGHEEEPLENTWPA----PY 155
Cdd:cd05256   77 ASV-----PRSIEDpikdheVNVLGTLNLLEAARKAGVKRFVYASSSSVYG----------DPPYLPKDEDHPPnplsPY 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 156 PHSKKLAEkavLAANGWNLKNGgtLYTCALRPMYIYGEGSR-----------FLSASI-NEALNNNGilssVGKfSTVNP 223
Cdd:cd05256  142 AVSKYAGE---LYCQVFARLYG--LPTVSLRYFNVYGPRQDpnggyaavipiFIERALkGEPPTIYG----DGE-QTRDF 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 224 VYVGNVAWAHILALRAlqdpkkapSIRGQFYYISDDTPHQsydnLNYTLSKefglrldsrwsfplslmywigfLLEIVSF 303
Cdd:cd05256  212 TYVEDVVEANLLAATA--------GAGGEVYNIGTGKRTS----VNELAEL----------------------IREILGK 257
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158256544 304 LLRPIYT-YRPPFNRHivTLSNSvftfsyKKAQRDLAYKPLYSWEEAKQKTVEW 356
Cdd:cd05256  258 ELEPVYApPRPGDVRH--SLADI------SKAKKLLGWEPKVSFEEGLRLTVEW 303
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-257 2.72e-23

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 95.83  E-value: 2.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   6 CLVTGAGGFLGQRIIRLLVKEKelKEIRVLDkafgpelreefsklqnktkltvlegdILDepflkracqdvsVIIHTACI 85
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERG--HEVVVID--------------------------RLD------------VVVHLAAL 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  86 IDV-FGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIqnghEEEPLENTWpaPYPHSKKLAEK 164
Cdd:cd08946   41 VGVpASWDNPDEDFETNVVGTLNLLEAARKAGVKRFVYASSASVYGSPEGLPEE----EETPPRPLS--PYGVSKLAAEH 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 165 AVLAANgwnlkNGGTLYTCALRPMYIYGEG-----SRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRa 239
Cdd:cd08946  115 LLRSYG-----ESYGLPVVILRLANVYGPGqrprlDGVVNDFIRRALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALE- 188
                        250
                 ....*....|....*...
gi 158256544 240 lqdpkkAPSIRGQFYYIS 257
Cdd:cd08946  189 ------NPLEGGGVYNIG 200
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
6-193 2.42e-18

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 84.34  E-value: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   6 CLVTGAGGFLGQRIIRLLVKEKelKEIRVLDKA-FGPELREEFSKL-QNKTKLTVLEGDI------LDEPFLKRACQDVS 77
Cdd:cd05263    1 VFVTGGTGFLGRHLVKRLLENG--FKVLVLVRSeSLGEAHERIEEAgLEADRVRVLEGDLtqpnlgLSAAASRELAGKVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  78 VIIHTACIIDvFGVThRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNS--YKEiiqngHEEEPlENTWPAPY 155
Cdd:cd05263   79 HVIHCAASYD-FQAP-NEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNREgnIRE-----TELNP-GQNFKNPY 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 158256544 156 PHSKKLAEKAVLAAngwnlknGGTLYTCALRPMYIYGE 193
Cdd:cd05263  151 EQSKAEAEQLVRAA-------ATQIPLTVYRPSIVVGD 181
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
7-257 2.49e-18

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 84.24  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLvkekeLKE-------IRVLDKAfgPELREEFSKLQNKTKLTVLEGDILDEP-FLKRACQDVSV 78
Cdd:cd05227    3 LVTGATGFIASHIVEQL-----LKAgykvrgtVRSLSKS--AKLKALLKAAGYNDRLEFVIVDDLTAPnAWDEALKGVDY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  79 IIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQA-SVPVFIYTSSI-EVAGPNSykeiiqnGHEEEPL-ENTW---- 151
Cdd:cd05227   76 VIHVASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKAAgSVKRVVLTSSVaAVGDPTA-------EDPGKVFtEEDWndlt 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 152 ------PAPYPHSKKLAEKAvlaanGW----NLKNGGTLytCALRPMYIYGEgSRF---LSASiNEALNN--NGILSSVG 216
Cdd:cd05227  149 isksngLDAYIASKTLAEKA-----AWefvkENKPKFEL--ITINPGYVLGP-SLLadeLNSS-NELINKllDGKLPAIP 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 158256544 217 KfsTVNPVYVGN--VAWAHilaLRALQDPKKApsirGQFYYIS 257
Cdd:cd05227  220 P--NLPFGYVDVrdVADAH---VRALESPEAA----GQRFIVS 253
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
6-322 3.23e-18

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: 83.45  E-value: 3.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   6 CLVTGAGGFLGQRIIRLLVKEKElkEIRVLdkafgpeLREEFSKLQNKT-----KLTVLEGDILDEPFLKRAcqdvsvII 80
Cdd:cd05271    3 VTVFGATGFIGRYVVNRLAKRGS--QVIVP-------YRCEAYARRLLVmgdlgQVLFVEFDLRDDESIRKA------LE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  81 HTACIIDVFGV---THRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEvAGPNSykeiiqngheeeplentwPAPYPH 157
Cdd:cd05271   68 GSDVVINLVGRlyeTKNFSFEDVHVEGPERLAKAAKEAGVERLIHISALG-ADANS------------------PSKYLR 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 158 SKKLAEKAVLAANGWnlknggtlyTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHIlal 237
Cdd:cd05271  129 SKAEGEEAVREAFPE---------ATIVRPSVVFGREDRFLNRFAKLLAFLPFPPLIGGGQTKFQPVYVGDVAEAIA--- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 238 RALQDpkkaPSIRGQFYYISDdtPHQsydnlnYTLSK--EFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYtyrPPF 315
Cdd:cd05271  197 RALKD----PETEGKTYELVG--PKV------YTLAElvELLRRLGGRKRRVLPLPLWLARLIARVKLLLLLPE---PPL 261

                 ....*..
gi 158256544 316 NRHIVTL 322
Cdd:cd05271  262 TRDQLER 268
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
7-169 5.29e-18

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 82.95  E-value: 5.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKeIRVL----DKAfgpELREEFSKLQNKTKL---------TVLEGDI------LDEP 67
Cdd:COG3320    4 LLTGATGFLGAHLLRELLRRTDAR-VYCLvrasDEA---AARERLEALLERYGLwleldasrvVVVAGDLtqprlgLSEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  68 FLKRACQDVSVIIHTACIIDVFGvtHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIqnghEEEPL 147
Cdd:COG3320   80 EFQELAEEVDAIVHLAALVNLVA--PYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVF----EEDDL 153
                        170       180
                 ....*....|....*....|....
gi 158256544 148 EN--TWPAPYPHSKKLAEKAVLAA 169
Cdd:COG3320  154 DEgqGFANGYEQSKWVAEKLVREA 177
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
7-246 5.81e-18

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 81.43  E-value: 5.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVL--DKAFGPELREEfsklqnktKLTVLEGDILDEPFLKRACQDVSVIIHTAc 84
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARGH--PVRALvrDPEKAAALAAA--------GVEVVQGDLDDPESLAAALAGVDAVFLLV- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 iidvfGVTHRESImNVNVKGTQLLLEACVQASVPVFIYTSSIevagpnsykeiiqnGHEEEPlentwPAPYPHSKKLAEK 164
Cdd:COG0702   72 -----PSGPGGDF-AVDVEGARNLADAAKAAGVKRIVYLSAL--------------GADRDS-----PSPYLRAKAAVEE 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 165 AVLAAngwnlkngGTLYTcALRPMYIYGegsrFLSASINEALNNNGILSSVGKfSTVNPVYVGNVAWAhilALRALQDPK 244
Cdd:COG0702  127 ALRAS--------GLPYT-ILRPGWFMG----NLLGFFERLRERGVLPLPAGD-GRVQPIAVRDVAEA---AAAALTDPG 189

                 ..
gi 158256544 245 KA 246
Cdd:COG0702  190 HA 191
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
7-213 4.20e-17

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 81.19  E-value: 4.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDK--AFGPELREEFSklqNKTKLTVLEGDILDEPFLKRACQDVSVIIHTAC 84
Cdd:cd05257    3 LVTGADGFIGSHLTERLLREGH--EVRALDIynSFNSWGLLDNA---VHDRFHFISGDVRDASEVEYLVKKCDVVFHLAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDV-FGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIiqngHEEEPL--ENTWPAPYPHSKKL 161
Cdd:cd05257   78 LIAIpYSYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPI----DEDHPLlyINKPRSPYSASKQG 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 162 AEKAVLAangWNLKNGgtLYTCALRPMYIYGEGSRFL--------SASINEALNNNGILS 213
Cdd:cd05257  154 ADRLAYS---YGRSFG--LPVTIIRPFNTYGPRQSARaviptiisQRAIGQRLINLGDGS 208
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-353 3.40e-16

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 78.16  E-value: 3.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVldkafgpelREEFSKLQNktkltVLEGDILDEPFLKRACQDVSVIIHTACII 86
Cdd:cd05232    3 LVTGANGFIGRALVDKLLSRGEEVRIAV---------RNAENAEPS-----VVLAELPDIDSFTDLFLGVDAVVHLAARV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  87 DVFGVTHRESI---MNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGpnsykeiiqNGHEEEPLENTWPA----PYPHSK 159
Cdd:cd05232   69 HVMNDQGADPLsdyRKVNTELTRRLARAAARQGVKRFVFLSSVKVNG---------EGTVGAPFDETDPPapqdAYGRSK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 160 KLAEKAVLAangwnLKNGGTLYTCALRPMYIYGEGSR--FLSAS--------INEALNNNgilssvgKFSTvnpVYVGNV 229
Cdd:cd05232  140 LEAERALLE-----LGASDGMEVVILRPPMVYGPGVRgnFARLMrlidrglpLPPGAVKN-------RRSL---VSLDNL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 230 AwahILALRALQDPKKApsirGQFYYISDDTPHQSYDnLNYTLSKEFGLRLdSRWSFPLSLMYWIGFLleivsFLLRPIY 309
Cdd:cd05232  205 V---DAIYLCISLPKAA----NGTFLVSDGPPVSTAE-LVDEIRRALGKPT-RLLPVPAGLLRFAAKL-----LGKRAVI 270
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 158256544 310 tyrppfNRHIVTLSnsvftFSYKKAQRDLAYKPLYSWEEAKQKT 353
Cdd:cd05232  271 ------QRLFGSLQ-----YDPEKTQNELGWRPPISLEEGLQET 303
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
7-168 1.54e-15

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 76.43  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDK-AFGPELrEEFSKLQNKTKLTVLEGDILDEPFLKRACQ--DVSVIIHTA 83
Cdd:cd05246    4 LVTGGAGFIGSNFVRYLLNKYPDYKIINLDKlTYAGNL-ENLEDVSSSPRYRFVKGDICDAELVDRLFEeeKIDAVIHFA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIidvfgvTH-RESI------MNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPnsyKEIIQNGHEEEPLENTwpAPYP 156
Cdd:cd05246   83 AE------SHvDRSIsdpepfIRTNVLGTYTLLEAARKYGVKRFVHISTDEVYGD---LLDDGEFTETSPLAPT--SPYS 151
                        170
                 ....*....|..
gi 158256544 157 HSKKLAEKAVLA 168
Cdd:cd05246  152 ASKAAADLLVRA 163
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
7-192 4.29e-15

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 75.00  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEI-----------------RVLDKAFGPELREEFSKlqnktKLTVLEGDI------ 63
Cdd:cd05235    3 LLTGATGFLGAYLLRELLKRKNVSKIyclvrakdeeaalerliDNLKEYGLNLWDELELS-----RIKVVVGDLskpnlg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  64 LDEPFLKRACQDVSVIIHTACIIDVFGvtHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQngHE 143
Cdd:cd05235   78 LSDDDYQELAEEVDVIIHNGANVNWVY--PYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDD--EE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158256544 144 EEPLE---NTWPAPYPHSKKLAEKAVLAANgwnlKNGgtLYTCALRPMYIYG 192
Cdd:cd05235  154 SDDMLesqNGLPNGYIQSKWVAEKLLREAA----NRG--LPVAIIRPGNIFG 199
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
7-192 1.15e-14

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 73.87  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRII-RLLVKEKELKEIRVL---DKAFGPE--LREE-----FSKLQN-----KTKLTVLEGDI------L 64
Cdd:cd05236    4 LITGATGFLGKVLLeKLLRSCPDIGKIYLLirgKSGQSAEerLRELlkdklFDRGRNlnplfESKIVPIEGDLsepnlgL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  65 DEPFLKRACQDVSVIIHTACIIDvFGVTHRESImNVNVKGTQLLLEACVQ-ASVPVFIYTSSIEVAGPNSYKE------- 136
Cdd:cd05236   84 SDEDLQTLIEEVNIIIHCAATVT-FDERLDEAL-SINVLGTLRLLELAKRcKKLKAFVHVSTAYVNGDRQLIEekvyppp 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 137 --IIQNGHEEEPLE------------NTWPAPYPHSKKLAEKAVlaangwnLKNGGTLYTCALRPMYIYG 192
Cdd:cd05236  162 adPEKLIDILELMDdleleratpkllGGHPNTYTFTKALAERLV-------LKERGNLPLVIVRPSIVGA 224
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
7-239 1.20e-14

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 73.94  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAfGPELREEfsklqnktKLTVLEGDILDE-PFLKRACQDVSVIIHTACI 85
Cdd:cd05240    2 LVTGAAGGLGRLLARRLAASPRVIGVDGLDRR-RPPGSPP--------KVEYVRLDIRDPaAADVFREREADAVVHLAFI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  86 IDvFGVTHRESiMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQngHEEEPLENTWPAPYPHSKKLAEkA 165
Cdd:cd05240   73 LD-PPRDGAER-HRINVDGTQNVLDACAAAGVPRVVVTSSVAVYGAHPDNPAPL--TEDAPLRGSPEFAYSRDKAEVE-Q 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158256544 166 VLAANGWNLKNGGTLytcALRPMYIYGEGSRflsaSINEALNNNGILSSVGKF-STVNPVYVGNVAWAHILALRA 239
Cdd:cd05240  148 LLAEFRRRHPELNVT---VLRPATILGPGTR----NTTRDFLSPRRLPVPGGFdPPFQFLHEDDVARALVLAVRA 215
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
7-207 2.19e-14

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 72.80  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKA--FGPelreefsklQNKTKLTVLEGDILDEPFLKRACQDVS-VIIHTA 83
Cdd:cd05238    4 LITGASGFVGQRLAERLLSDVPNERLILIDVVspKAP---------SGAPRVTQIAGDLAVPALIEALANGRPdVVFHLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIIDVFGVTHRESIMNVNVKGTQLLLEAC-VQASVPVFIYTSSIEVAGPNSYKEIIQNGHeeeplentwPAP---YPHSK 159
Cdd:cd05238   75 AIVSGGAEADFDLGYRVNVDGTRNLLEALrKNGPKPRFVFTSSLAVYGLPLPNPVTDHTA---------LDPassYGAQK 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158256544 160 KLAEkAVLAangwNLKNGGTLYTCALR-PMYIYGEG------SRFLSASINEALN 207
Cdd:cd05238  146 AMCE-LLLN----DYSRRGFVDGRTLRlPTVCVRPGrpnkaaSAFASTIIREPLV 195
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
6-174 5.03e-14

flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 71.84  E-value: 5.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   6 CLVTGAGGFLGQRIIRLLV--------------KEKELKEIRVLDKAfgpelreefsklqnKTKLTVLEGDILDEPFLKR 71
Cdd:cd08958    1 VCVTGASGFIGSWLVKRLLqrgytvratvrdpgDEKKVAHLLELEGA--------------KERLKLFKADLLDYGSFDA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  72 ACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQA-SVPVFIYTSSIEVAGPNsykeiiQNGHEEEPL-EN 149
Cdd:cd08958   67 AIDGCDGVFHVASPVDFDSEDPEEEMIEPAVKGTLNVLEACAKAkSVKRVVFTSSVAAVVWN------PNRGEGKVVdES 140
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 158256544 150 TWPAP---------YPHSKKLAEKAVLAA---NGWNL 174
Cdd:cd08958  141 CWSDLdfckktklwYALSKTLAEKAAWEFaeeNGLDL 177
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
8-217 6.73e-14

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 70.72  E-value: 6.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    8 VTGAGGFLGQRIIR-------------LLVKEKELKEI--RVLDKAFGPELREEFSKLQnKTKLTVLEGDI------LDE 66
Cdd:pfam07993   1 LTGATGFLGKVLLEkllrstpdvkkiyLLVRAKDGESAleRLRQELEKYPLFDALLKEA-LERIVPVAGDLsepnlgLSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   67 PFLKRACQDVSVIIHTACIIDVFGvtHRESIMNVNVKGTQLLLEACVQ-ASVPVFIYTSSIEVAGPNS-------YKEII 138
Cdd:pfam07993  80 EDFQELAEEVDVIIHSAATVNFVE--PYDDARAVNVLGTREVLRLAKQgKQLKPFHHVSTAYVNGERGglveekpYPEGE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  139 QNGHEEEPLENT---WPAPYPHSKKLAEKAVLAANGWNLKnggtlyTCALRPMYIYGEgsrflsaSINEALNNN-----G 210
Cdd:pfam07993 158 DDMLLDEDEPALlggLPNGYTQTKWLAEQLVREAARRGLP------VVIYRPSIITGE-------PKTGWINNFdfgprG 224

                  ....*..
gi 158256544  211 ILSSVGK 217
Cdd:pfam07993 225 LLGGIGK 231
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
7-184 3.77e-13

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 69.18  E-value: 3.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElKEIRVLD----KAFgpELREEFSKLQNKTKLTVLEGDILDEPFLKRAC--QDVSVII 80
Cdd:cd05237    6 LVTGGAGSIGSELVRQILKFGP-KKLIVFDrdenKLH--ELVRELRSRFPHDKLRFIIGDVRDKERLRRAFkeRGPDIVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  81 HTACIIDVFGVTHR-ESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYkeiiqngheeeplentwpapYPHSK 159
Cdd:cd05237   83 HAAALKHVPSMEDNpEEAIKTNVLGTKNVIDAAIENGVEKFVCISTDKAVNPVNV--------------------MGATK 142
                        170       180
                 ....*....|....*....|....*
gi 158256544 160 KLAEKAVLAANGwnlKNGGTLYTCA 184
Cdd:cd05237  143 RVAEKLLLAKNE---YSSSTKFSTV 164
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-215 6.48e-12

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 66.28  E-value: 6.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPE---------LREEFSKLQNKT--KLTVLEGDI------LDEPFL 69
Cdd:TIGR01746   3 LLTGATGFLGAYLLEELLRRSTRAKVICLVRADSEEhamerlreaLRSYRLWHENLAmeRIEVVAGDLskprlgLSDAEW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   70 KRACQDVSVIIHTACIIDVFGvtHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQngHEEEPLEN 149
Cdd:TIGR01746  83 ERLAENVDTIVHNGALVNHVY--PYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVT--EDDATVTP 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158256544  150 --TWPAPYPHSKKLAEKAVLAANgwNLKNGGTLYtcalRPMYIygegsrfLSASINEALNNNGILSSV 215
Cdd:TIGR01746 159 ypGLAGGYTQSKWVAELLVREAS--DRGLPVTIV----RPGRI-------LGDSYTGAWNSSDILWRM 213
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
7-170 1.81e-11

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 64.00  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLvkEKELKEIRVLDKAfgpelreefsklqnktkltvlEGDILDEPFLKRACQDVS--VIIHTAC 84
Cdd:COG1091    3 LVTGANGQLGRALVRLL--AERGYEVVALDRS---------------------ELDITDPEAVAALLEEVRpdVVINAAA 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVFGV-THRESIMNVNVKGTQLLLEACVQASVPvFIYTSSIEV---AGPNSYKeiiqnghEEEPlentwPAP---YPH 157
Cdd:COG1091   60 YTAVDKAeSEPELAYAVNATGPANLAEACAELGAR-LIHISTDYVfdgTKGTPYT-------EDDP-----PNPlnvYGR 126
                        170
                 ....*....|...
gi 158256544 158 SKKLAEKAVLAAN 170
Cdd:COG1091  127 SKLAGEQAVRAAG 139
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
7-196 1.85e-11

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein mannosyl-transferase and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 64.07  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEKeLKEIRVLD----KAFgpELREEFSKLQNKTKLTVLE----GDILDEPFLKRACQ--DV 76
Cdd:pfam02719   2 LVTGGGGSIGSELCRQILKFN-PKKIILFSrdelKLY--EIRQELREKFNDPKLRFFIvpviGDVRDRERLERAMEqyGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   77 SVIIHTACIIDVFGVTH--RESIMNvNVKGTQLLLEACVQASVPVFIYTSSIEVAGP-NSYkeiiqnGheeeplentwpa 153
Cdd:pfam02719  79 DVVFHAAAYKHVPLVEYnpMEAIKT-NVLGTENVADAAIEAGVKKFVLISTDKAVNPtNVM------G------------ 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 158256544  154 pypHSKKLAEKAVLAANGwNLKNGGTLYtCALRpmyiYGE--GSR 196
Cdd:pfam02719 140 ---ATKRLAEKLFQAANR-ESGSGGTRF-SVVR----FGNvlGSR 175
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-245 2.45e-10

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 61.01  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDkAFGPELREEFSKLQnKTKLTVLEGDILDEPFLKR--ACQDVSVIIHTAC 84
Cdd:cd05247    3 LVTGGAGYIGSHTVVELLEAGY--DVVVLD-NLSNGHREALPRIE-KIRIEFYEGDIRDRAALDKvfAEHKIDAVIHFAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVfGvthrESI------MNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIiqngHEEEPLENTwpAPYPHS 158
Cdd:cd05247   79 LKAV-G----ESVqkplkyYDNNVVGTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVPI----TEEAPLNPT--NPYGRT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 159 KKLAE---KAVLAANGWNlknggtlYTCaLRpmYIYGEGSRFlSASINEALN--NN----------GILSSVGKFSTVNP 223
Cdd:cd05247  148 KLMVEqilRDLAKAPGLN-------YVI-LR--YFNPAGAHP-SGLIGEDPQipNNlipyvlqvalGRREKLAIFGDDYP 216
                        250       260       270
                 ....*....|....*....|....*....|..
gi 158256544 224 ----------VYVGNVAWAHILALRALQDPKK 245
Cdd:cd05247  217 tpdgtcvrdyIHVVDLADAHVLALEKLENGGG 248
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
7-212 2.76e-10

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: 58.95  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDkafgpelREE--FSKLQNKTKLtVLEGDILDEPFLKRACQDVSVIIHTAc 84
Cdd:cd05226    2 LILGATGFIGRALARELLEQGH--EVTLLV-------RNTkrLSKEDQEPVA-VVEGDLRDLDSLSDAVQGVDVVIHLA- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 iidvfGVTH-RESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVagpnsykeiiqNGHEEEPLENTWPAPYPHSKKLAE 163
Cdd:cd05226   71 -----GAPRdTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGA-----------YGDLHEETEPSPSSPYLAVKAKTE 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 158256544 164 KAVLAAngwnlkngGTLYTcALRPMYIYGEGSRFLSASINEALNNNGIL 212
Cdd:cd05226  135 AVLREA--------SLPYT-IVRPGVIYGDLARAIANAVVTPGKKNETF 174
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
7-356 1.23e-09

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 58.89  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKE-KELKEIRVLDKAFGPELREE-FSKLQNKTKLTVLEGDILDEPFLKRACQDVS--VIIHT 82
Cdd:cd05253    4 LVTGAAGFIGFHVAKRLLERgDEVVGIDNLNDYYDVRLKEArLELLGKSGGFKFVKGDLEDREALRRLFKDHEfdAVIHL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  83 ACIIDVfgvthRESIMN------VNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIiqnghEEEPLENTWPAPYP 156
Cdd:cd05253   84 AAQAGV-----RYSLENphayvdSNIVGFLNLLELCRHFGVKHLVYASSSSVYGLNTKMPF-----SEDDRVDHPISLYA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 157 HSKKLAEkavLAANGWNLKNGgtLYTCALRPMYIYGEGSR-------FLSASIN-EALN--NNGILSSvgKFStvnpvYV 226
Cdd:cd05253  154 ATKKANE---LMAHTYSHLYG--IPTTGLRFFTVYGPWGRpdmalflFTKAILEgKPIDvfNDGNMSR--DFT-----YI 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 227 GNVAWAHILALralqDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKefglrldsrwsfPLSLMYWIGfLLEivSFLLR 306
Cdd:cd05253  222 DDIVEGVVRAL----DTPAKPNPNWDAEAPDPSTSSAPYRVYNIGNNS------------PVKLMDFIE-ALE--KALGK 282
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158256544 307 PIYTYRPPFNRHIVtlsnsVFTF-SYKKAQRDLAYKPLYSWEEAKQKTVEW 356
Cdd:cd05253  283 KAKKNYLPMQKGDV-----PETYaDISKLQRLLGYKPKTSLEEGVKRFVEW 328
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
7-246 1.97e-09

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 56.86  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVL--DKAFGPELREEfsklqnktKLTVLEGDILDEPFLKRACQDVSVIIHTAC 84
Cdd:cd05243    3 LVVGATGKVGRHVVRELLDRGY--QVRALvrDPSQAEKLEAA--------GAEVVVGDLTDAESLAAALEGIDAVISAAG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IidvfGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIqngheeeplentwpAPYPHSKKLAEK 164
Cdd:cd05243   73 S----GGKGGPRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLEAL--------------GPYLDAKRKAED 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 165 avlaangwNLKNGGTLYTCaLRPmyiygegSRFLSasiNEALNNNGILSSVGKfSTVNPVYVGNVAWahiLALRALQDPK 244
Cdd:cd05243  135 --------YLRASGLDYTI-VRP-------GGLTD---DPAGTGRVVLGGDGT-RLDGPISRADVAE---VLAEALDTPA 191

                 ..
gi 158256544 245 KA 246
Cdd:cd05243  192 AI 193
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-170 5.70e-09

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 56.92  E-value: 5.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKelKEIRVLDKAFGPELREEFSKLQNKtKLTVLEGDILDePFLKRACQDVSVIIHTACII 86
Cdd:cd05234    3 LVTGGAGFIGSHLVDRLLEEG--NEVVVVDNLSSGRRENIEPEFENK-AFRFVKRDLLD-TADKVAKKDGDTVFHLAANP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  87 DV-FGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSykeiIQNGHEEEPLEntwPAPYPHSKKLAEKA 165
Cdd:cd05234   79 DVrLGATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSSTVYGEAK----VIPTPEDYPPL---PISVYGASKLAAEA 151

                 ....*
gi 158256544 166 VLAAN 170
Cdd:cd05234  152 LISAY 156
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
7-158 1.65e-08

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 55.63  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEK-ELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVS--VIIHTA 83
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGyEVHGIVRRSSSFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQpdEIYNLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   84 CIIDVfgvthRESI------MNVNVKGTQLLLEACVQA---SVPVFIYTSSIEVAGpnSYKEIIQNghEEEPLentwpap 154
Cdd:pfam16363  81 AQSHV-----DVSFeqpeytADTNVLGTLRLLEAIRSLgleKKVRFYQASTSEVYG--KVQEVPQT--ETTPF------- 144

                  ....
gi 158256544  155 YPHS 158
Cdd:pfam16363 145 YPRS 148
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
7-170 1.73e-08

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 54.97  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVKEkelkeirvldkafGPELreefsklqnkTKLTVLEGDILDEPFLKRACQDV--SVIIHTAC 84
Cdd:pfam04321   2 LITGANGQLGTELRRLLAER-------------GIEV----------VALTRAELDLTDPEAVARLLREIkpDVVVNAAA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   85 IIDVFGV-THRESIMNVNVKGTQLLLEACVQASVPvFIYTSSIEV---AGPNSYkeiiqngHEEEPlentwPAP---YPH 157
Cdd:pfam04321  59 YTAVDKAeSEPDLAYAINALAPANLAEACAAVGAP-LIHISTDYVfdgTKPRPY-------EEDDE-----TNPlnvYGR 125
                         170
                  ....*....|...
gi 158256544  158 SKKLAEKAVLAAN 170
Cdd:pfam04321 126 TKLAGEQAVRAAG 138
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
7-167 5.38e-08

aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 53.78  E-value: 5.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVkEKELK---EIRVLDKAFGPELREEFSKLQnkTKLTVLEGDILDEPFLKRACQDVSVIIHTA 83
Cdd:cd05193    2 LVTGASGFVASHVVEQLL-ERGYKvraTVRDPSKVKKVNHLLDLDAKP--GRLELAVADLTDEQSFDEVIKGCAGVFHVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIIDvFGVTHRESIMNVNVKGTQLLLEACVQA-SVPVFIYTSSIEVAG-PNSYKEIIqnGHEEEP--LENTWPAP----- 154
Cdd:cd05193   79 TPVS-FSSKDPNEVIKPAIGGTLNALKAAAAAkSVKRFVLTSSAGSVLiPKPNVEGI--VLDEKSwnLEEFDSDPkksaw 155
                        170
                 ....*....|....
gi 158256544 155 -YPHSKKLAEKAVL 167
Cdd:cd05193  156 vYAASKTLAEKAAW 169
NAD_binding_10 pfam13460
NAD(P)H-binding;
10-187 6.66e-08

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   10 GAGGFLGQRIIRLLVKEKelkeIRVldKAFgpeLR--EEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTAciid 87
Cdd:pfam13460   1 GATGKIGRLLVKQLLARG----HEV--TAL---VRnpEKLADLEDHPGVEVVDGDVLDPDDLAEALAGQDAVISAL---- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   88 vfGVTHRESimnvnvKGTQLLLEACVQASVPVFIYTSSIEVagpnsYKEIiqnGHEEEPLENTWPAPYPHSKKLAEKAvl 167
Cdd:pfam13460  68 --GGGGTDE------TGAKNIIDAAKAAGVKRFVLVSSLGV-----GDEV---PGPFGPWNKEMLGPYLAAKRAAEEL-- 129
                         170       180
                  ....*....|....*....|
gi 158256544  168 aangwnLKNGGTLYTcALRP 187
Cdd:pfam13460 130 ------LRASGLDYT-IVRP 142
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
7-208 1.51e-07

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 52.32  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKaFGPELReefsklQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTAC-- 84
Cdd:cd05264    3 LIVGGNGFIGSHLVDALLEEGP--QVRVFDR-SIPPYE------LPLGGVDYIKGDYENRADLESALVGIDTVIHLAStt 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVFGVTHRESImNVNVKGTQLLLEACVQASVPVFIYTSSievaGPNSYKEiiqngHEEEPL-ENTWPAP---YPHSKK 160
Cdd:cd05264   74 NPATSNKNPILDI-QTNVAPTVQLLEACAAAGIGKIIFASS----GGTVYGV-----PEQLPIsESDPTLPissYGISKL 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158256544 161 LAEKAVLAANgwnlKNGGTLYTcALRPMYIYGEGSR------FLSASINEALNN 208
Cdd:cd05264  144 AIEKYLRLYQ----YLYGLDYT-VLRISNPYGPGQRpdgkqgVIPIALNKILRG 192
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
7-237 1.63e-07

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 52.24  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLvKEKELKEIRVLDKafgpelREEFSKLqnktkltvlegDILDEPFLKRACQDVS--VIIHTAC 84
Cdd:cd05254    3 LITGATGMLGRALVRLL-KERGYEVIGTGRS------RASLFKL-----------DLTDPDAVEEAIRDYKpdVIINCAA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVFGV-THRESIMNVNVKGTQLLLEACVQASVpVFIYTSSIEV----AGPnsYKeiiqnghEEEPlentwPAP---YP 156
Cdd:cd05254   65 YTRVDKCeSDPELAYRVNVLAPENLARAAKEVGA-RLIHISTDYVfdgkKGP--YK-------EEDA-----PNPlnvYG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 157 HSKKLAEKAVLAANGwnlknggtlYTCALRPMYIYGE---GSRFLSASINEALNNNgilsSVGKFSTV--NPVYVGNVAw 231
Cdd:cd05254  130 KSKLLGEVAVLNANP---------RYLILRTSWLYGElknGENFVEWMLRLAAERK----EVNVVHDQigSPTYAADLA- 195

                 ....*.
gi 158256544 232 AHILAL 237
Cdd:cd05254  196 DAILEL 201
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
7-168 2.72e-07

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 52.44  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDK----AFGPELREEFSKLQNK-TKLTVLEGDILDepFLKRAcQDVSVIIH 81
Cdd:PLN02260  10 LITGAAGFIASHVANRLIRNYPDYKIVVLDKldycSNLKNLNPSKSSPNFKfVKGDIASADLVN--YLLIT-EGIDTIMH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  82 TACIIDV---FGVTHrESIMNvNVKGTQLLLEAC-VQASVPVFIYTSSIEVAGPNSYKEIIQNgHEEEPLENTwpAPYPH 157
Cdd:PLN02260  87 FAAQTHVdnsFGNSF-EFTKN-NIYGTHVLLEACkVTGQIRRFIHVSTDEVYGETDEDADVGN-HEASQLLPT--NPYSA 161
                        170
                 ....*....|.
gi 158256544 158 SKKLAEKAVLA 168
Cdd:PLN02260 162 TKAGAEMLVMA 172
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
8-237 2.73e-07

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 51.58  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   8 VTGAGGFLGQRIIRLLVkekelkeirvldkAFGPEL-----REEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHT 82
Cdd:cd05262    5 VTGATGFIGSAVVRELV-------------AAGHEVvglarSDAGAAKLEAAGAQVHRGDLEDLDILRKAAAEADAVIHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  83 ACIidvFGVTHRESIMNVNVKGTQLLLEACVQASVPvFIYTSSIEVAGPnsykeiiqNGHEEEPLENTWPAPYPHSKKLA 162
Cdd:cd05262   72 AFT---HDFDNFAQACEVDRRAIEALGEALRGTGKP-LIYTSGIWLLGP--------TGGQEEDEEAPDDPPTPAARAVS 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158256544 163 EKAVLAANGWNLKNGGTlytcaLRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNP-VYVGNVAWAHILAL 237
Cdd:cd05262  140 EAAALELAERGVRASVV-----RLPPVVHGRGDHGFVPMLIAIAREKGVSAYVGDGKNRWPaVHRDDAARLYRLAL 210
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
7-161 1.15e-06

ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 49.61  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLvKEKELKEIRVLDKaFGpelREEFSKLQNKTKLTvlegDILDEPFLKRAC------QDVSVII 80
Cdd:cd05248    3 IVTGGAGFIGSNLVKAL-NERGITDILVVDN-LS---NGEKFKNLVGLKIA----DYIDKDDFKDWVrkgdenFKIEAIF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  81 HTACIIDVFgVTHRESIMNVNVKGTQLLLEACVQASVPvFIYTSSIEVAG--PNSYKEIIQNgHEEEPLEntwpaPYPHS 158
Cdd:cd05248   74 HQGACSDTT-ETDGKYMMDNNYQYTKELLHYCLEKKIR-FIYASSAAVYGngSLGFAEDIET-PNLRPLN-----VYGYS 145

                 ...
gi 158256544 159 KKL 161
Cdd:cd05248  146 KLL 148
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
7-246 3.52e-06

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 49.29  E-value: 3.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544     7 LVTGAGGFLGQRIIRLLVKEKELKEIRVL------DKAFGPE-LR----------EEFSKlqnktKLTVLEGDILDEPF- 68
Cdd:TIGR03443  975 FLTGATGFLGSFILRDLLTRRSNSNFKVFahvrakSEEAGLErLRktgttygiwdEEWAS-----RIEVVLGDLSKEKFg 1049
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    69 -----LKRACQDVSVIIHTACIidVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSY----KEIIQ 139
Cdd:TIGR03443 1050 lsdekWSDLTNEVDVIIHNGAL--VHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYYvnlsDELVQ 1127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   140 NGH----EEEPLENT---WPAPYPHSKKLAEKAVLAANGWNLKNggtlytCALRPMYIYGegsrflsASINEALNNNGIL 212
Cdd:TIGR03443 1128 AGGagipESDDLMGSskgLGTGYGQSKWVAEYIIREAGKRGLRG------CIVRPGYVTG-------DSKTGATNTDDFL 1194
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 158256544   213 SSVGK-----------FSTVNPVYVGNVawAHILALRALQDPKKA 246
Cdd:TIGR03443 1195 LRMLKgciqlglipniNNTVNMVPVDHV--ARVVVAAALNPPKES 1237
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
7-158 1.16e-05

Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 46.70  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKaFGPELREEFSKlqnktKLTVLEGDILDEPFLKRACQDVSVIIHTACii 86
Cdd:cd05273    4 LVTGAGGFIGSHLAERLKAEGH--YVRGADW-KSPEHMTQPTD-----DDEFHLVDLREMENCLKATEGVDHVFHLAA-- 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158256544  87 DVFGV----THRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVagpnsYKEIIQNGHEEEPL--ENTWPAPyPHS 158
Cdd:cd05273   74 DMGGMgyiqSNHAVIMYNNTLINFNMLEAARINGVERFLFASSACV-----YPEFKQLETTVVRLreEDAWPAE-PQD 145
PLN02214 PLN02214
cinnamoyl-CoA reductase
3-263 1.29e-05

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 46.67  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   3 GWSCLVTGAGGFLGQRIIRLLVKEKELKE--IRVLDKAFGPELREefskLQ-NKTKLTVLEGDILDEPFLKRACQDVSVI 79
Cdd:PLN02214  10 GKTVCVTGAGGYIASWIVKILLERGYTVKgtVRNPDDPKNTHLRE----LEgGKERLILCKADLQDYEALKAAIDGCDGV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  80 IHTACIIdvfgVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVA--GPNSYKEIIQNGHEEEPLE---NT--Wp 152
Cdd:PLN02214  86 FHTASPV----TDDPEQMVEPAVNGAKFVINAAAEAKVKRVVITSSIGAVymDPNRDPEAVVDESCWSDLDfckNTknW- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 153 apYPHSKKLAEKAvlaanGWNLKNGGTLYTCALRPMYIYGEGsrfLSASINEALNN--NGILSSVGKFSTVNPVYVG--N 228
Cdd:PLN02214 161 --YCYGKMVAEQA-----AWETAKEKGVDLVVLNPVLVLGPP---LQPTINASLYHvlKYLTGSAKTYANLTQAYVDvrD 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 158256544 229 VAWAHILALralqdpkKAPSIRGQfYYISDDTPHQ 263
Cdd:PLN02214 231 VALAHVLVY-------EAPSASGR-YLLAESARHR 257
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
7-135 1.93e-05

CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 46.13  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKAFGPELREEFSKLQNKTK---LTVLEGDILDEPFLKRACQDVSVIIHTA 83
Cdd:cd05258    4 LITGGAGFIGSNLARFFLKQGW--EVIGFDNLMRRGSFGNLAWLKANREdggVRFVHGDIRNRNDLEDLFEDIDLIIHTA 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 158256544  84 CIIDV-FGVTHRESIMNVNVKGTQLLLEACVQASV-PVFIYTSSIEVAG--PNSYK 135
Cdd:cd05258   82 AQPSVtTSASSPRLDFETNALGTLNVLEAARQHAPnAPFIFTSTNKVYGdlPNYLP 137
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
7-164 2.38e-05

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 45.96  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKAFGPE--LREEFSKLQNKTKlTVLEGDILDEPFLKR--ACQDVSVIIHT 82
Cdd:PRK10675   4 LVTGGSGYIGSHTCVQLLQNGH--DVVILDNLCNSKrsVLPVIERLGGKHP-TFVEGDIRNEALLTEilHDHAIDTVIHF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  83 ACIIDVfGVTHRESI--MNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPN---SYKEIIQNGHeeeplentwPA-PYP 156
Cdd:PRK10675  81 AGLKAV-GESVQKPLeyYDNNVNGTLRLISAMRAANVKNLIFSSSATVYGDQpkiPYVESFPTGT---------PQsPYG 150

                 ....*...
gi 158256544 157 HSKKLAEK 164
Cdd:PRK10675 151 KSKLMVEQ 158
PRK07201 PRK07201
SDR family oxidoreductase;
7-166 2.49e-05

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 46.10  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDI------LDEPFLKrACQDVSVII 80
Cdd:PRK07201   4 FVTGGTGFIGRRLVSRLLDRRREATVHVLVRRQSLSRLEALAAYWGADRVVPLVGDLtepglgLSEADIA-ELGDIDHVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  81 HTACIIDVfgVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAG--PNSYKEIIQNGHEEeplentWPAPYPHS 158
Cdd:PRK07201  83 HLAAIYDL--TADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAVAGdyEGVFREDDFDEGQG------LPTPYHRT 154

                 ....*...
gi 158256544 159 KKLAEKAV 166
Cdd:PRK07201 155 KFEAEKLV 162
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
8-253 7.86e-05

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 44.24  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   8 VTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIId 87
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESSFEQAIEGCDAVFHTASPV- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  88 VFGVTHRES-IMNVNVKGTQLLLEACVQ-ASVPVFIYTSSIEVA----GPNSYKEIIQNGHEEEPL----ENTWpapYPH 157
Cdd:PLN02986  89 FFTVKDPQTeLIDPALKGTINVLNTCKEtPSVKRVILTSSTAAVlfrqPPIEANDVVDETFFSDPSlcreTKNW---YPL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 158 SKKLAEKAvlaanGWNLKNGGTLYTCALRPMYIYGEgsrFLSASINEALNNngILSSVGKFSTVNPVY-----VGNVAWA 232
Cdd:PLN02986 166 SKILAENA-----AWEFAKDNGIDMVVLNPGFICGP---LLQPTLNFSVEL--IVDFINGKNLFNNRFyrfvdVRDVALA 235
                        250       260
                 ....*....|....*....|.
gi 158256544 233 HILALralqdpkKAPSIRGQF 253
Cdd:PLN02986 236 HIKAL-------ETPSANGRY 249
PLN00198 PLN00198
anthocyanidin reductase; Provisional
8-234 9.91e-05

anthocyanidin reductase; Provisional


Pssm-ID: 215100 [Multi-domain]  Cd Length: 338  Bit Score: 43.72  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   8 VTGAGGFLGQRIIRLLVKEKELKEIRVLDkafgPELREEFS---KLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTAC 84
Cdd:PLN00198  14 VIGGTGFLASLLIKLLLQKGYAVNTTVRD----PENQKKIAhlrALQELGDLKIFGADLTDEESFEAPIAGCDLVFHVAT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVFGVTHRESIMNVNVKGTQLLLEACVQA-SVPVFIYTSSIEVAGPNSYKE--IIQNGH---------EEEPLenTWP 152
Cdd:PLN00198  90 PVNFASEDPENDMIKPAIQGVHNVLKACAKAkSVKRVILTSSAAAVSINKLSGtgLVMNEKnwtdvefltSEKPP--TWG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 153 apYPHSKKLAEKAvlaanGWNLKNGGTLYTCALRPMYIYGEG-------SRFLSASI---NEALNNNgiLSSVGKFS-TV 221
Cdd:PLN00198 168 --YPASKTLAEKA-----AWKFAEENNIDLITVIPTLMAGPSltsdipsSLSLAMSLitgNEFLING--LKGMQMLSgSI 238
                        250
                 ....*....|...
gi 158256544 222 NPVYVGNVAWAHI 234
Cdd:PLN00198 239 SITHVEDVCRAHI 251
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
8-126 1.12e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 43.66  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   8 VTGAGGFLGQRIIRLLVKEKEL--KEIRVLDKAFgpelrEEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACI 85
Cdd:PLN02896  15 VTGATGYIGSWLVKLLLQRGYTvhATLRDPAKSL-----HLLSKWKEGDRLRLFRADLQEEGSFDEAVKGCDGVFHVAAS 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158256544  86 IDvFGVTH---------RESIMNVNVKGTQLLLEACVQA-SVPVFIYTSSI 126
Cdd:PLN02896  90 ME-FDVSSdhnnieeyvQSKVIDPAIKGTLNVLKSCLKSkTVKRVVFTSSI 139
PLN02989 PLN02989
cinnamyl-alcohol dehydrogenase family protein
8-253 2.08e-04

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178569 [Multi-domain]  Cd Length: 325  Bit Score: 42.71  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   8 VTGAGGFLGQRIIRLLVkekeLKEIRVLDKAFGPELREEFSKL----QNKTKLTVLEGDILDEPFLKRACQDVSVIIHTA 83
Cdd:PLN02989  10 VTGASGYIASWIVKLLL----FRGYTINATVRDPKDRKKTDHLlaldGAKERLKLFKADLLDEGSFELAIDGCETVFHTA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  84 CIIDVFGVTHRE-SIMNVNVKGTQLLLEACVQ-ASVPVFIYTSSIEVA-------GPNsykEIIQNGHEEEPL----ENT 150
Cdd:PLN02989  86 SPVAITVKTDPQvELINPAVNGTINVLRTCTKvSSVKRVILTSSMAAVlapetklGPN---DVVDETFFTNPSfaeeRKQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 151 WpapYPHSKKLAEKAvlaanGWNLKNGGTLYTCALRPMYIYG----EGSRFLSASINEalnnngILSSVGKFSTVNPVYV 226
Cdd:PLN02989 163 W---YVLSKTLAEDA-----AWRFAKDNEIDLIVLNPGLVTGpilqPTLNFSVAVIVE------LMKGKNPFNTTHHRFV 228
                        250       260
                 ....*....|....*....|....*....
gi 158256544 227 G--NVAWAHILALralqdpkKAPSIRGQF 253
Cdd:PLN02989 229 DvrDVALAHVKAL-------ETPSANGRY 250
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
5-262 2.14e-04

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 42.28  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   5 SCLVTGAGGFLGQRIIRLLVKEKElkEIRVL-----DKAFGPELREefsklqnktkltvLEGDILDEPFLKRACQDVSVI 79
Cdd:cd05265    2 KILIIGGTRFIGKALVEELLAAGH--DVTVFnrgrtKPDLPEGVEH-------------IVGDRNDRDALEELLGGEDFD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  80 IhtacIIDVFGVTHREsimnvnvkgTQLLLEACvQASVPVFIYTSSIEVagpnsYKEIIQNGHEEEPLENT------WPA 153
Cdd:cd05265   67 V----VVDTIAYTPRQ---------VERALDAF-KGRVKQYIFISSASV-----YLKPGRVITESTPLREPdavglsDPW 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 154 PYPHSKKLAEKAVLAAngWNLKnggtlYTcALRPMYIYGEGSRF--LSASINEALNNNGILSSVGKFSTVNPVYVGNVAW 231
Cdd:cd05265  128 DYGRGKRAAEDVLIEA--AAFP-----YT-IVRPPYIYGPGDYTgrLAYFFDRLARGRPILVPGDGHSLVQFIHVKDLAR 199
                        250       260       270
                 ....*....|....*....|....*....|.
gi 158256544 232 AhilALRALQDPKKApsirGQFYYISDDTPH 262
Cdd:cd05265  200 A---LLGAAGNPKAI----GGIFNITGDEAV 223
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
7-83 2.41e-04

Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 42.49  E-value: 2.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKaFGPELREEfskLQNKTKLTVLEGDILDEPFLKRACQDVS--VIIHTA 83
Cdd:cd08957    4 LITGGAGQIGSHLIEHLLERGH--QVVVIDN-FATGRREH---LPDHPNLTVVEGSIADKALVDKLFGDFKpdAVVHTA 76
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
7-196 3.01e-04

capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 41.96  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREefsklqnktkltvlegdildepflkrACQDVSVIIHTAcii 86
Cdd:cd05261    4 LITGAKGFIGKNLIARLKEQKDDDIFFYDRESDESELDD--------------------------FLQGADFIFHLA--- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  87 dvfGVT---HRESIMNVNVKGTQLLLEACVQA--SVPVfIYTSSIEVAGPNsykeiiqngheeeplentwpaPYPHSKKL 161
Cdd:cd05261   55 ---GVNrpkDEAEFESGNVGLTERLLDALTRNgkKPPI-LLSSSIQAALDN---------------------PYGKSKLA 109
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 158256544 162 AEKAVLAangWNLKNGGTLYTcaLRPMYIYGEGSR 196
Cdd:cd05261  110 AEELLQE---YARETGAPVYI--YRLPNVFGKWCR 139
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
8-237 3.67e-04

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 42.01  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   8 VTGAGGFLGQRIIRLL------VKE--------KELKEIRVLDKAfgpelreefsklqnKTKLTVLEGDILDEPFLKRAC 73
Cdd:PLN02662   9 VTGASGYIASWLVKLLlqrgytVKAtvrdpndpKKTEHLLALDGA--------------KERLHLFKANLLEEGSFDSVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544  74 QDVSVIIHTACIIdVFGVTH-RESIMNVNVKGTQLLLEACVQA-SVPVFIYTSSIEVagpnsykeIIQNGHEEEP---LE 148
Cdd:PLN02662  75 DGCEGVFHTASPF-YHDVTDpQAELIDPAVKGTLNVLRSCAKVpSVKRVVVTSSMAA--------VAYNGKPLTPdvvVD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544 149 NTW---PAP-------YPHSKKLAEKAvlaanGWNL--KNGGTLYTcaLRPMYIYGEgsrFLSASINeaLNNNGILSSVG 216
Cdd:PLN02662 146 ETWfsdPAFceesklwYVLSKTLAEEA-----AWKFakENGIDMVT--INPAMVIGP---LLQPTLN--TSAEAILNLIN 213
                        250       260
                 ....*....|....*....|....*.
gi 158256544 217 KFSTV-NPVY----VGNVAWAHILAL 237
Cdd:PLN02662 214 GAQTFpNASYrwvdVRDVANAHIQAF 239
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
7-126 4.78e-04

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: 40.62  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544    7 LVTGAGGFLGQRIIRLLVkEKELKEIRVL--DKAFGPELREEFSKLQNK-TKLTVLEGDILDEPFLKRACQDVSV----- 78
Cdd:pfam08659   4 LITGGLGGLGRELARWLA-ERGARHLVLLsrSAAPRPDAQALIAELEARgVEVVVVACDVSDPDAVAALLAEIKAegppi 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158256544   79 --IIHTAciidvfGVTHRESIMNVN-----------VKGTQLLLEACVQASVPVFIYTSSI 126
Cdd:pfam08659  83 rgVIHAA------GVLRDALLENMTdedwrrvlapkVTGTWNLHEATPDEPLDFFVLFSSI 137
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
7-134 1.25e-03

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 40.31  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKElkEIRVLDKaFGPELREEFSKLQNKTKLTVLEGDILDePFLKRacqdVSVIIHTACII 86
Cdd:cd05230    4 LITGGAGFLGSHLCDRLLEDGH--EVICVDN-FFTGRKRNIEHLIGHPNFEFIRHDVTE-PLYLE----VDQIYHLACPA 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158256544  87 D-VFGVTHRESIMNVNVKGTQ--LLLEACVQASvpvFIYTSSIEVAG-------PNSY 134
Cdd:cd05230   76 SpVHYQYNPIKTLKTNVLGTLnmLGLAKRVGAR---VLLASTSEVYGdpevhpqPESY 130
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
7-136 2.10e-03

L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 39.60  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKE--KE---LKEIRVLDKafGPELREEFSKLqnktkltvlegDILDEPFLKRACQDVSV--I 79
Cdd:cd05272    3 LITGGLGQIGSELAKLLRKRygKDnviASDIRKPPA--HVVLSGPFEYL-----------DVLDFKSLEEIVVNHKItwI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158256544  80 IHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIyTSSIEVAGPNSYKE 136
Cdd:cd05272   70 IHLAALLSAVGEKNPPLAWDVNMNGLHNVLELAREHNLRIFV-PSTIGAFGPTTPRN 125
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
6-81 2.57e-03

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 39.25  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158256544   6 CLVTGAGGFLGQRIIRLLVKEKElkEIRVLDKAfgpelREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIH 81
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGH--QVRALVRS-----PEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAYY 69
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
7-124 4.58e-03

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical 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: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 38.41  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEfsklqnktKLTVLEGDILDEPFLKRACQDVSV--IIHTAC 84
Cdd:cd05269    2 LVTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAAD--------GVEVRQGDYDDPETLERAFEGVDRllLISPSD 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 158256544  85 IIDVfGVTHResimNVnvkgtqllLEACVQASVPVFIYTS 124
Cdd:cd05269   74 LEDR-IQQHK----NF--------IDAAKQAGVKHIVYLS 100
PRK09186 PRK09186
flagellin modification protein A; Provisional
7-72 5.12e-03

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 38.05  E-value: 5.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRA 72
Cdd:PRK09186   8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVELDITDQESLEEF 73
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
7-126 8.22e-03

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: 38.12  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256544   7 LVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQ----NKTKLTVLEGDILDEPFLKRACQDVS----- 77
Cdd:cd08953  209 LVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKAQTLAaleaLGARVLYISADVTDAAAVRRLLEKVReryga 288
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158256544  78 --VIIHTAciidvfGVTHRESIMN-----------VNVKGTQLLLEACVQASVPVFIYTSSI 126
Cdd:cd08953  289 idGVIHAA------GVLRDALLAQktaedfeavlaPKVDGLLNLAQALADEPLDFFVLFSSV 344
 
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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