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Conserved domains on  [gi|564330401|ref|XP_006230080|]
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fatty acyl-CoA reductase 1 isoform X1 [Rattus norvegicus]

Protein Classification

fatty acyl-CoA reductase( domain architecture ID 10859931)

fatty acyl-CoA reductase is an extended SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase that catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols; 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
11-330 0e+00

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: 515.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEILSGKLFDRLRDENPDFRQKIIAINSELTQPK 90
Cdd:cd05236    1 KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNPLFESKIVPIEGDLSEPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 LALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPP 170
Cdd:cd05236   81 LGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQLIEEKVYPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 171 PVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGP 250
Cdd:cd05236  161 PADPEKLIDILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 251 SGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNP 330
Cdd:cd05236  241 DGLFLAYGKGILRTMNADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHCGSSDVNPFTWGEAEELINQYLKKNP 320
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
357-447 3.47e-38

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: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 134.90  E-value: 3.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  357 HKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYIEN 436
Cdd:pfam03015   2 HLLPAYLLDLLLRLLGKKPRLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPEDRKLFNFDIRSIDWDDYFEN 81
                          90
                  ....*....|.
gi 564330401  437 YCMGTKKYVLN 447
Cdd:pfam03015  82 YILGIRKYLLK 92
 
Name Accession Description Interval E-value
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
11-330 0e+00

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: 515.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEILSGKLFDRLRDENPDFRQKIIAINSELTQPK 90
Cdd:cd05236    1 KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNPLFESKIVPIEGDLSEPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 LALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPP 170
Cdd:cd05236   81 LGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQLIEEKVYPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 171 PVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGP 250
Cdd:cd05236  161 PADPEKLIDILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 251 SGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNP 330
Cdd:cd05236  241 DGLFLAYGKGILRTMNADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHCGSSDVNPFTWGEAEELINQYLKKNP 320
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
15-284 1.80e-103

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: 310.70  E-value: 1.80e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   15 LTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERV-EEILSGKLFDRLRDEnpdFRQKIIAINSELTQPKLAL 93
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLrQELEKYPLFDALLKE---ALERIVPVAGDLSEPNLGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   94 SEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRK-HIDEVVYPPPv 172
Cdd:pfam07993  78 SEEDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVSTAYVNGERGgLVEEKPYPEG- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  173 dpkklidslewMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGA-KLNVAIVRPSIVGAswkEPFPGWIDNFN-GP 250
Cdd:pfam07993 157 -----------EDDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARrGLPVVIYRPSIITG---EPKTGWINNFDfGP 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 564330401  251 SGLFIAAGKGILRTMRASNNALADLVPVDVVVNT 284
Cdd:pfam07993 223 RGLLGGIGKGVLPSILGDPDAVLDLVPVDYVANA 256
PLN02503 PLN02503
fatty acyl-CoA reductase 2
2-446 1.76e-56

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 198.55  E-value: 1.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   2 VSIPEYYEGKNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVE-EILSGKLFDRLRDENPDFRQ--- 77
Cdd:PLN02503 111 IGIAEFLRGKNFLITGATGFLAKVLIEKILRTNPDVGKIYLLIKAKDKEAAIERLKnEVIDAELFKCLQETHGKSYQsfm 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  78 --KIIAINSELTQPKLALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAY 155
Cdd:PLN02503 191 lsKLVPVVGNVCESNLGLEPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKLFLQVSTAY 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 156 AYCNRK-------------------HIDEVVYPPPV-----DPKKLIDSLEWMDDGlvNDITPKL--IG-DRP------N 202
Cdd:PLN02503 271 VNGQRQgrimekpfrmgdciarelgISNSLPHNRPAldieaEIKLALDSKRHGFQS--NSFAQKMkdLGlERAklygwqD 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 203 TYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTMRASNNALADLVPVDVVV 282
Cdd:PLN02503 349 TYVFTKAMGEMVINSMRGDIPVVIIRPSVIESTWKDPFPGWMEGNRMMDPIVLYYGKGQLTGFLADPNGVLDVVPADMVV 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 283 NTSLAA-AWYSGVNRPrNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPnVNLTSNHLL-------YHYWia 354
Cdd:PLN02503 429 NATLAAmAKHGGAAKP-EINVYQIASSVVNPLVFQDLARLLYEHYKSSPYMDSKGRP-IHVPPMKLFssmedfsSHLW-- 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 355 vshkapaflYDIYLR-----MTGRSPRMMKTITRLHKAMV--------FLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTF 421
Cdd:PLN02503 505 ---------RDALLRsglagMSSSDRKLSQKLENICAKSVeqakylasIYEPYTFYGGRFDNSNTQRLMERMSEEEKAEF 575
                        490       500
                 ....*....|....*....|....*.
gi 564330401 422 NIDVRQLHWAEYIEN-YCMGTKKYVL 446
Cdd:PLN02503 576 GFDVGSIDWRDYITNvHIPGLRRHVM 601
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
11-282 1.87e-45

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: 159.99  E-value: 1.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRSCPkvNSVYVLVRQKAGQTPQERVEEilsgkLFDRLRDENPDFRQKIIAINSELTQPK 90
Cdd:COG3320    1 RTVLLTGATGFLGAHLLRELLRRTD--ARVYCLVRASDEAAARERLEA-----LLERYGLWLELDASRVVVVAGDLTQPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 LALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKnLEVFMHVSTAYAYcnrkhidevvypP 170
Cdd:COG3320   74 LGLSEAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGR-LKPFHYVSTIAVA------------G 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 171 PVDPKKLIDSLEW-MDDGLvnditpkligdrPNTYIYTKALAEYVVQQEGA-KLNVAIVRPS-IVGASWKepfpGWIDNF 247
Cdd:COG3320  141 PADRSGVFEEDDLdEGQGF------------ANGYEQSKWVAEKLVREARErGLPVTIYRPGiVVGDSRT----GETNKD 204
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564330401 248 NGPSGLFiaagKGILRTMRA--SNNALADLVPVDVVV 282
Cdd:COG3320  205 DGFYRLL----KGLLRLGAApgLGDARLNLVPVDYVA 237
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
357-447 3.47e-38

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: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 134.90  E-value: 3.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  357 HKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYIEN 436
Cdd:pfam03015   2 HLLPAYLLDLLLRLLGKKPRLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPEDRKLFNFDIRSIDWDDYFEN 81
                          90
                  ....*....|.
gi 564330401  437 YCMGTKKYVLN 447
Cdd:pfam03015  82 YILGIRKYLLK 92
FAR_C cd09071
C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, ...
355-446 1.04e-35

C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, a family of SDR-like proteins. SDRs or short-chain dehydrogenases/reductases are Rossmann-fold NAD(P)H-binding proteins. Many proteins in this FAR_C family may function as fatty acyl-CoA reductases (FARs), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as the 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. The function of this C-terminal domain is unclear.


Pssm-ID: 176924 [Multi-domain]  Cd Length: 92  Bit Score: 128.06  E-value: 1.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 355 VSHKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYI 434
Cdd:cd09071    1 FLHLLPAYLLDLLLRLLGRKPRLLKLYRKIHKLLDLLEYFTTNEWRFDNDNTRALWERLSEEDRELFNFDIRSIDWDDYF 80
                         90
                 ....*....|..
gi 564330401 435 ENYCMGTKKYVL 446
Cdd:cd09071   81 ENYIPGLRKYLL 92
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
12-229 4.57e-22

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: 97.87  E-value: 4.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   12 NILLTGATGFLGKVLLEKLLRSCPKVnSVYVLVRQKAGQTPQERVEEILSGKlfdRLRDENPDfRQKIIAINSELTQPKL 91
Cdd:TIGR01746   1 TVLLTGATGFLGAYLLEELLRRSTRA-KVICLVRADSEEHAMERLREALRSY---RLWHENLA-MERIEVVAGDLSKPRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   92 ALSEEDKEIIIDSTNVIFHCAATVRFN---ENLRDAvqlNVIATRQLILLAQQMKnLEVFMHVSTAYAYC-NRKHIDEVV 167
Cdd:TIGR01746  76 GLSDAEWERLAENVDTIVHNGALVNHVypySELRGA---NVLGTVEVLRLAASGR-AKPLHYVSTISVGAaIDLSTGVTE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330401  168 YPPPVDPKKLIdslewmddglvnditpkligdrPNTYIYTKALAEYVVQQEGAK-LNVAIVRP 229
Cdd:TIGR01746 152 DDATVTPYPGL----------------------AGGYTQSKWVAELLVREASDRgLPVTIVRP 192
 
Name Accession Description Interval E-value
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
11-330 0e+00

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: 515.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEILSGKLFDRLRDENPDFRQKIIAINSELTQPK 90
Cdd:cd05236    1 KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNPLFESKIVPIEGDLSEPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 LALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPP 170
Cdd:cd05236   81 LGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQLIEEKVYPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 171 PVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGP 250
Cdd:cd05236  161 PADPEKLIDILELMDDLELERATPKLLGGHPNTYTFTKALAERLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 251 SGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNP 330
Cdd:cd05236  241 DGLFLAYGKGILRTMNADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHCGSSDVNPFTWGEAEELINQYLKKNP 320
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
15-284 1.80e-103

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: 310.70  E-value: 1.80e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   15 LTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERV-EEILSGKLFDRLRDEnpdFRQKIIAINSELTQPKLAL 93
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLrQELEKYPLFDALLKE---ALERIVPVAGDLSEPNLGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   94 SEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRK-HIDEVVYPPPv 172
Cdd:pfam07993  78 SEEDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVSTAYVNGERGgLVEEKPYPEG- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  173 dpkklidslewMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGA-KLNVAIVRPSIVGAswkEPFPGWIDNFN-GP 250
Cdd:pfam07993 157 -----------EDDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARrGLPVVIYRPSIITG---EPKTGWINNFDfGP 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 564330401  251 SGLFIAAGKGILRTMRASNNALADLVPVDVVVNT 284
Cdd:pfam07993 223 RGLLGGIGKGVLPSILGDPDAVLDLVPVDYVANA 256
PLN02503 PLN02503
fatty acyl-CoA reductase 2
2-446 1.76e-56

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 198.55  E-value: 1.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   2 VSIPEYYEGKNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVE-EILSGKLFDRLRDENPDFRQ--- 77
Cdd:PLN02503 111 IGIAEFLRGKNFLITGATGFLAKVLIEKILRTNPDVGKIYLLIKAKDKEAAIERLKnEVIDAELFKCLQETHGKSYQsfm 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  78 --KIIAINSELTQPKLALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAY 155
Cdd:PLN02503 191 lsKLVPVVGNVCESNLGLEPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKLFLQVSTAY 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 156 AYCNRK-------------------HIDEVVYPPPV-----DPKKLIDSLEWMDDGlvNDITPKL--IG-DRP------N 202
Cdd:PLN02503 271 VNGQRQgrimekpfrmgdciarelgISNSLPHNRPAldieaEIKLALDSKRHGFQS--NSFAQKMkdLGlERAklygwqD 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 203 TYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTMRASNNALADLVPVDVVV 282
Cdd:PLN02503 349 TYVFTKAMGEMVINSMRGDIPVVIIRPSVIESTWKDPFPGWMEGNRMMDPIVLYYGKGQLTGFLADPNGVLDVVPADMVV 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 283 NTSLAA-AWYSGVNRPrNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPnVNLTSNHLL-------YHYWia 354
Cdd:PLN02503 429 NATLAAmAKHGGAAKP-EINVYQIASSVVNPLVFQDLARLLYEHYKSSPYMDSKGRP-IHVPPMKLFssmedfsSHLW-- 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 355 vshkapaflYDIYLR-----MTGRSPRMMKTITRLHKAMV--------FLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTF 421
Cdd:PLN02503 505 ---------RDALLRsglagMSSSDRKLSQKLENICAKSVeqakylasIYEPYTFYGGRFDNSNTQRLMERMSEEEKAEF 575
                        490       500
                 ....*....|....*....|....*.
gi 564330401 422 NIDVRQLHWAEYIEN-YCMGTKKYVL 446
Cdd:PLN02503 576 GFDVGSIDWRDYITNvHIPGLRRHVM 601
PLN02996 PLN02996
fatty acyl-CoA reductase
2-446 7.58e-49

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 175.28  E-value: 7.58e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   2 VSIPEYYEGKNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERV-EEILSGKLFDRLRDE-----NPDF 75
Cdd:PLN02996   3 GSCVQFLENKTILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLhDEVIGKDLFKVLREKlgenlNSLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  76 RQKIIAINSELTQPKLALSEED-KEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTA 154
Cdd:PLN02996  83 SEKVTPVPGDISYDDLGVKDSNlREEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKKCVKVKMLLHVSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 155 YAyCNRKH--IDEVVYP--------PPVD---PKKLIDslEWMDDGLVNDITPKLI-------GDR-------PNTYIYT 207
Cdd:PLN02996 163 YV-CGEKSglILEKPFHmgetlngnRKLDineEKKLVK--EKLKELNEQDASEEEItqamkdlGMEraklhgwPNTYVFT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 208 KALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLA 287
Cdd:PLN02996 240 KAMGEMLLGNFKENLPLVIIRPTMITSTYKEPFPGWIEGLRTIDSVIVGYGKGKLTCFLADPNSVLDVIPADMVVNAMIV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 288 AAWYSGVNRPRNiMVYNCTTGSTNPFHWGEVEYHVISTFKRNPLE----QAFRRPNVNLTSNHLLYHYWIAVSHKAP--- 360
Cdd:PLN02996 320 AMAAHAGGQGSE-IIYHVGSSLKNPVKFSNLHDFAYRYFSKNPWInkegSPVKVGKGTILSTMASFSLYMTIRYLLPlka 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 361 -AFLYDIYLRMTG-------RSPRMMKTITRLHKAMVFLEYFTSNSwvwNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAE 432
Cdd:PLN02996 399 lQLVNIILPKRYGdkytdlnRKIKLVMRLVDLYKPYVFFKGIFDDT---NTEKLRIKRKETGKEEADMFDFDPKSIDWED 475
                        490
                 ....*....|....*
gi 564330401 433 YIEN-YCMGTKKYVL 446
Cdd:PLN02996 476 YMTNvHIPGLVKYVL 490
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
11-282 1.87e-45

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: 159.99  E-value: 1.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRSCPkvNSVYVLVRQKAGQTPQERVEEilsgkLFDRLRDENPDFRQKIIAINSELTQPK 90
Cdd:COG3320    1 RTVLLTGATGFLGAHLLRELLRRTD--ARVYCLVRASDEAAARERLEA-----LLERYGLWLELDASRVVVVAGDLTQPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 LALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKnLEVFMHVSTAYAYcnrkhidevvypP 170
Cdd:COG3320   74 LGLSEAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGR-LKPFHYVSTIAVA------------G 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 171 PVDPKKLIDSLEW-MDDGLvnditpkligdrPNTYIYTKALAEYVVQQEGA-KLNVAIVRPS-IVGASWKepfpGWIDNF 247
Cdd:COG3320  141 PADRSGVFEEDDLdEGQGF------------ANGYEQSKWVAEKLVREARErGLPVTIYRPGiVVGDSRT----GETNKD 204
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564330401 248 NGPSGLFiaagKGILRTMRA--SNNALADLVPVDVVV 282
Cdd:COG3320  205 DGFYRLL----KGLLRLGAApgLGDARLNLVPVDYVA 237
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
357-447 3.47e-38

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: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 134.90  E-value: 3.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  357 HKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYIEN 436
Cdd:pfam03015   2 HLLPAYLLDLLLRLLGKKPRLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPEDRKLFNFDIRSIDWDDYFEN 81
                          90
                  ....*....|.
gi 564330401  437 YCMGTKKYVLN 447
Cdd:pfam03015  82 YILGIRKYLLK 92
FAR_C cd09071
C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, ...
355-446 1.04e-35

C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, a family of SDR-like proteins. SDRs or short-chain dehydrogenases/reductases are Rossmann-fold NAD(P)H-binding proteins. Many proteins in this FAR_C family may function as fatty acyl-CoA reductases (FARs), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as the 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. The function of this C-terminal domain is unclear.


Pssm-ID: 176924 [Multi-domain]  Cd Length: 92  Bit Score: 128.06  E-value: 1.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 355 VSHKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYI 434
Cdd:cd09071    1 FLHLLPAYLLDLLLRLLGRKPRLLKLYRKIHKLLDLLEYFTTNEWRFDNDNTRALWERLSEEDRELFNFDIRSIDWDDYF 80
                         90
                 ....*....|..
gi 564330401 435 ENYCMGTKKYVL 446
Cdd:cd09071   81 ENYIPGLRKYLL 92
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
12-329 5.67e-34

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: 129.69  E-value: 5.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  12 NILLTGATGFLGKVLLEKLLRsCPKVNSVYVLVRQKAGQTPQERVEEILSGKlFDRLRDEnpDFRQKIIAINSELTQPKL 91
Cdd:cd05235    1 TVLLTGATGFLGAYLLRELLK-RKNVSKIYCLVRAKDEEAALERLIDNLKEY-GLNLWDE--LELSRIKVVVGDLSKPNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  92 ALSEEDKEIIIDSTNVIFHCAATVRFN---ENLRDAvqlNVIATRQLILLAQQMKnLEVFMHVSTAYaycnrkhidevVY 168
Cdd:cd05235   77 GLSDDDYQELAEEVDVIIHNGANVNWVypyEELKPA---NVLGTKELLKLAATGK-LKPLHFVSTLS-----------VF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 169 PPPVDPKKLIDSLEwmddglvNDITPKLigDRPNTYIYTKALAEYVVQQEGAK-LNVAIVRP-SIVGASWKepfpGWIDN 246
Cdd:cd05235  142 SAEEYNALDDEESD-------DMLESQN--GLPNGYIQSKWVAEKLLREAANRgLPVAIIRPgNIFGDSET----GIGNT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 247 FNgpsgLFIAAGKGILRTMRASN-NALADLVPVDVVVNTSLAAAwysgVNRPRNIMVYNCTTGstNPFHWGEVeYHVIST 325
Cdd:cd05235  209 DD----FFWRLLKGCLQLGIYPIsGAPLDLSPVDWVARAIVKLA----LNESNEFSIYHLLNP--PLISLNDL-LDALEE 277

                 ....
gi 564330401 326 FKRN 329
Cdd:cd05235  278 KGYS 281
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
13-283 2.46e-31

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: 122.48  E-value: 2.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  13 ILLTGATGFLGKVLLEKLLRScpkVNSVYVLVRQKAGQTPQERVEEilSGKLFDRLRDENPDfrqkiiainseLTQPKLA 92
Cdd:cd05263    1 VFVTGGTGFLGRHLVKRLLEN---GFKVLVLVRSESLGEAHERIEE--AGLEADRVRVLEGD-----------LTQPNLG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  93 LSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQmKNLEVFMHVSTAYAYCNRKhidEVVYPPPV 172
Cdd:cd05263   65 LSAAASRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAAR-LDIQRFHYVSTAYVAGNRE---GNIRETEL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 173 DPKKlidslewmddglvnditpkligDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVgasWKEPFPGWIDNFNGPSG 252
Cdd:cd05263  141 NPGQ----------------------NFKNPYEQSKAEAEQLVRAAATQIPLTVYRPSIV---VGDSKTGRIEKIDGLYE 195
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564330401 253 LF-IAAGKGILRTMRASNNALADLVPVDVVVN 283
Cdd:cd05263  196 LLnLLAKLGRWLPMPGNKGARLNLVPVDYVAD 227
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
12-229 4.57e-22

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: 97.87  E-value: 4.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   12 NILLTGATGFLGKVLLEKLLRSCPKVnSVYVLVRQKAGQTPQERVEEILSGKlfdRLRDENPDfRQKIIAINSELTQPKL 91
Cdd:TIGR01746   1 TVLLTGATGFLGAYLLEELLRRSTRA-KVICLVRADSEEHAMERLREALRSY---RLWHENLA-MERIEVVAGDLSKPRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   92 ALSEEDKEIIIDSTNVIFHCAATVRFN---ENLRDAvqlNVIATRQLILLAQQMKnLEVFMHVSTAYAYC-NRKHIDEVV 167
Cdd:TIGR01746  76 GLSDAEWERLAENVDTIVHNGALVNHVypySELRGA---NVLGTVEVLRLAASGR-AKPLHYVSTISVGAaIDLSTGVTE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330401  168 YPPPVDPKKLIdslewmddglvnditpkligdrPNTYIYTKALAEYVVQQEGAK-LNVAIVRP 229
Cdd:TIGR01746 152 DDATVTPYPGL----------------------AGGYTQSKWVAELLVREASDRgLPVTIVRP 192
PRK07201 PRK07201
SDR family oxidoreductase;
12-283 1.41e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 79.61  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  12 NILLTGATGFLGKVLLEKLLrSCPKVNSVYVLVRQKAgqtpQERVEEILSGKLFDRlrdenpdfrqkIIAINSELTQPKL 91
Cdd:PRK07201   2 RYFVTGGTGFIGRRLVSRLL-DRRREATVHVLVRRQS----LSRLEALAAYWGADR-----------VVPLVGDLTEPGL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  92 ALSEEDKEIIIDSTNViFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNlEVFMHVST-AYAYCNRKHIDEvvypp 170
Cdd:PRK07201  66 GLSEADIAELGDIDHV-VHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQA-ATFHHVSSiAVAGDYEGVFRE----- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 171 pvdpkklidslewmDDglvNDITPKLigdrPNTYIYTKALAEYVVQQEgAKLNVAIVRPSIV-GASWKepfpGWIDNFNG 249
Cdd:PRK07201 139 --------------DD---FDEGQGL----PTPYHRTKFEAEKLVREE-CGLPWRVYRPAVVvGDSRT----GEMDKIDG 192
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564330401 250 PSGLF--IAAGKGILRTMRAsnnALAD-----LVPVDVVVN 283
Cdd:PRK07201 193 PYYFFkvLAKLAKLPSWLPM---VGPDggrtnIVPVDYVAD 230
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
13-289 2.25e-14

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: 73.86  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  13 ILLTGATGFLGKVLLEKLLRSCpkvNSVYVLVR--QKAGQTPQERVEeILSGKLFDRlrdenPDFRQkiiainseltqpk 90
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQG---YRVRALVRsgSDAVLLDGLPVE-VVEGDLTDA-----ASLAA------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 lALSEEDkeiiidstnVIFHCAATVRFNENLRDAV-QLNVIATRQLILLAQQmKNLEVFMHVSTayaycnrkhIDEVVYP 169
Cdd:cd05228   59 -AMKGCD---------RVFHLAAFTSLWAKDRKELyRTNVEGTRNVLDAALE-AGVRRVVHTSS---------IAALGGP 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 170 PpvdpkklidslewmdDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAK-LNVAIVRPS-IVGaswkepfPGwiDNF 247
Cdd:cd05228  119 P---------------DGRIDETTPWNERPFPNDYYRSKLLAELEVLEAAAEgLDVVIVNPSaVFG-------PG--DEG 174
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564330401 248 NGPSGLFI---AAGKgilrtMRASNNALADLVPVDVVVNTSLAAA 289
Cdd:cd05228  175 PTSTGLDVldyLNGK-----LPAYPPGGTSFVDVRDVAEGHIAAM 214
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
12-308 2.58e-13

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 70.39  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  12 NILLTGATGFLGKVLLEKLLRSCpkvNSVYVLVRQKAGQTPQERVE--EILSGKLFDRlrdenPDFRQkiiainseltqp 89
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARG---HEVVGLDRSPPGAANLAALPgvEFVRGDLRDP-----EALAA------------ 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  90 klALSEEDkeiiidstnVIFHCAATVRFNE-NLRDAVQLNVIATRQLILLAQQmKNLEVFMHVSTAYAYCNRKH-IDEvv 167
Cdd:COG0451   61 --ALAGVD---------AVVHLAAPAGVGEeDPDETLEVNVEGTLNLLEAARA-AGVKRFVYASSSSVYGDGEGpIDE-- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 168 yPPPVDPKklidslewmddglvnditpkligdrpNTYIYTKALAEYVVQQEGAK--LNVAIVRPS-IVGASWKEPFPGWI 244
Cdd:COG0451  127 -DTPLRPV--------------------------SPYGASKLAAELLARAYARRygLPVTILRPGnVYGPGDRGVLPRLI 179
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564330401 245 DNfngpsglfIAAGKGIlrTMRASNNALADLVPVDVVVNTSLAAAwysgvNRPRNIM-VYNCTTG 308
Cdd:COG0451  180 RR--------ALAGEPV--PVFGDGDQRRDFIHVDDVARAIVLAL-----EAPAAPGgVYNVGGG 229
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
3-235 2.72e-12

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: 69.71  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401     3 SIPEYYEGK---------NILLTGATGFLGKVLLEKLL-RSCPKVNSVYVLVRQKAGQTPQERVEEilSGKLFDRLRDEn 72
Cdd:TIGR03443  955 SLPKSYPSRkeldastpiTVFLTGATGFLGSFILRDLLtRRSNSNFKVFAHVRAKSEEAGLERLRK--TGTTYGIWDEE- 1031
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401    73 pdFRQKIIAINSELTQPKLALSEEDKEIIIDSTNVIFHCAATVRF---NENLRDAvqlNVIATRQLILLAQQMKNlEVFM 149
Cdd:TIGR03443 1032 --WASRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGALVHWvypYSKLRDA---NVIGTINVLNLCAEGKA-KQFS 1105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   150 HVSTAYA----YCNRKHiDEVVypppVDPKKLI---DSLEWMDDGLVNDitpkligdrpntYIYTKALAEYVVQQEGAK- 221
Cdd:TIGR03443 1106 FVSSTSAldteYYVNLS-DELV----QAGGAGIpesDDLMGSSKGLGTG------------YGQSKWVAEYIIREAGKRg 1168
                          250
                   ....*....|....*
gi 564330401   222 LNVAIVRPS-IVGAS 235
Cdd:TIGR03443 1169 LRGCIVRPGyVTGDS 1183
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
13-282 1.06e-08

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: 55.38  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  13 ILLTGATGFLGKVLLEKLLRSCPKVnsvyvlvrqkagqtpqerveeilsgklfdrlrdenpdfrqkiiainseltqpkla 92
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERGHEV------------------------------------------------------- 25
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  93 lseedkeIIIDSTNVIFHCAATV---RFNENLRDAVQLNVIATRQLILLAQQMkNLEVFMHVSTAYAYCNRKHIDEVVYP 169
Cdd:cd08946   26 -------VVIDRLDVVVHLAALVgvpASWDNPDEDFETNVVGTLNLLEAARKA-GVKRFVYASSASVYGSPEGLPEEEET 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 170 PPvdpkklidslewmddglvnditpkligdRPNT-YIYTKALAEYVVQQEGAK--LNVAIVRPSIV-----GASWKEPFP 241
Cdd:cd08946   98 PP----------------------------RPLSpYGVSKLAAEHLLRSYGESygLPVVILRLANVygpgqRPRLDGVVN 149
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564330401 242 GWIDNFNGPSGLFIAAGKGILRtmrasnnalaDLVPVDVVV 282
Cdd:cd08946  150 DFIRRALEGKPLTVFGGGNQTR----------DFIHVDDVV 180
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
9-153 9.49e-08

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: 53.39  E-value: 9.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   9 EGKNILLTGATGFLGKVLLEKLLRSCPKVnsVYVLVRQKAGQtpQERVEEILSGKLFDRLRDENPDFRQKIIainseltq 88
Cdd:cd05237    1 KGKTILVTGGAGSIGSELVRQILKFGPKK--LIVFDRDENKL--HELVRELRSRFPHDKLRFIIGDVRDKER-------- 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330401  89 pkLALSEEDKEIiidstNVIFHCAAT--VRFNE-NLRDAVQLNVIATRQLILLAQQmKNLEVFMHVST 153
Cdd:cd05237   69 --LRRAFKERGP-----DIVFHAAALkhVPSMEdNPEEAIKTNVLGTKNVIDAAIE-NGVEKFVCIST 128
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
13-242 1.85e-07

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: 52.30  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   13 ILLTGATGFLGKVLLEKLLRSCPKVNSVYvlVRQKAGQTPQERVEEILSGKLFDRlrdenpDFRQKIIAINSeltqpkla 92
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLD--RLTSASNTARLADLRFVEGDLTDR------DALEKLLADVR-------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   93 lseedkeiiIDstnVIFHCAAT---VRFNENLRDAVQLNVIATRQLILLAQQMkNLEVFMHVSTAYAYcnrkhidevvyp 169
Cdd:pfam01370  65 ---------PD---AVIHLAAVggvGASIEDPEDFIEANVLGTLNLLEAARKA-GVKRFLFASSSEVY------------ 119
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330401  170 PPVDPkklIDSLEWMDDGLVNDITPkligdrpntYIYTKALAEYVVQ--QEGAKLNVAIVRPS-IVGASWKEPFPG 242
Cdd:pfam01370 120 GDGAE---IPQEETTLTGPLAPNSP---------YAAAKLAGEWLVLayAAAYGLRAVILRLFnVYGPGDNEGFVS 183
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
13-232 1.88e-06

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: 48.17  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  13 ILLTGATGFLGKVLLEKLLRscpKVNSVYVLVR--QKAGQTPQERVEEILSgklfdrlrdenpDFRQkiiainseltqpk 90
Cdd:cd05226    1 ILILGATGFIGRALARELLE---QGHEVTLLVRntKRLSKEDQEPVAVVEG------------DLRD------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 lalsEEDKEIIIDSTNVIFHCAATVRFnenLRDAVQLNVIATRQLIllaQQMKNLEV--FMHVSTAYAYcnrKHIDEVVY 168
Cdd:cd05226   53 ----LDSLSDAVQGVDVVIHLAGAPRD---TRDFCEVDVEGTRNVL---EAAKEAGVkhFIFISSLGAY---GDLHEETE 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330401 169 PPPVDPkklidslewmddglvnditpkligdrpntYIYTKALAEYVVqqEGAKLNVAIVRPSIV 232
Cdd:cd05226  120 PSPSSP-----------------------------YLAVKAKTEAVL--REASLPYTIVRPGVI 152
CC3_like_SDR_a cd05250
CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as ...
11-104 3.83e-05

CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as TIP30) which is implicated in tumor suppression. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine rich NAD(P)-binding motif that resembles the extended SDRs, and have an active site triad of the SDRs (YXXXK and upstream Ser), although the upstream Asn of the usual SDR active site is substituted with Asp. For CC3, the Tyr of the triad is displaced compared to the usual SDRs and the protein is monomeric, both these observations suggest that the usual SDR catalytic activity is not present. NADP appears to serve an important role as a ligand, and may be important in the interaction with other macromolecules. 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: 187560 [Multi-domain]  Cd Length: 214  Bit Score: 44.98  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRScPKVNSVYVLVRQKAGQTPQ-ERVEEILSGklFDRLRDENPDFRQKIIAINSELTQP 89
Cdd:cd05250    1 KTALVLGATGLVGKHLLRELLKS-PYYSKVTAIVRRKLTFPEAkEKLVQIVVD--FERLDEYLEAFQNPDVGFCCLGTTR 77
                         90       100
                 ....*....|....*....|
gi 564330401  90 KLALSEE-----DKEIIIDS 104
Cdd:cd05250   78 KKAGSQEnfrkvDHDYVLKL 97
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
12-318 7.21e-05

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: 44.54  E-value: 7.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  12 NILLTGATGFLGKVLLeKLLRSCPKvnSVYVLVRQKAGQTP-----QERVEEIlsgklfdrLRDENPDfrqkiiainsel 86
Cdd:cd05254    1 KILITGATGMLGRALV-RLLKERGY--EVIGTGRSRASLFKldltdPDAVEEA--------IRDYKPD------------ 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  87 tqpklalseedkeiiidstnVIFHCAATVRFNENLRD---AVQLNVIATRQLILLAQQMKNLevFMHVSTAYaycnrkhi 163
Cdd:cd05254   58 --------------------VIINCAAYTRVDKCESDpelAYRVNVLAPENLARAAKEVGAR--LIHISTDY-------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 164 devVYpppvdpkklidslewmdDGlvnDITPKLIGDRP---NTYIYTKALAEYVVQQEGAklNVAIVRPSIVGASWK--E 238
Cdd:cd05254  108 ---VF-----------------DG---KKGPYKEEDAPnplNVYGKSKLLGEVAVLNANP--RYLILRTSWLYGELKngE 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401 239 PFPGWI--------------DNFNGP-------------------SGLFIAAGKGI-------LRTMRASNNALADLVPV 278
Cdd:cd05254  163 NFVEWMlrlaaerkevnvvhDQIGSPtyaadladaileliernslTGIYHLSNSGPiskyefaKLIADALGLPDVEIKPI 242
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 564330401 279 DVVVNTSLAAawysgvnRPRNiMVYNCT----TGSTNPFHWGEV 318
Cdd:cd05254  243 TSSEYPLPAR-------RPAN-SSLDCSkleeLGGIKPPDWKEA 278
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
12-57 7.18e-04

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: 40.98  E-value: 7.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564330401  12 NILLTGATGFLGKVLLEKLLRscpKVNSVYVLVR--QKAGQTPQERVE 57
Cdd:COG0702    1 KILVTGATGFIGRRVVRALLA---RGHPVRALVRdpEKAAALAAAGVE 45
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
11-232 9.01e-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: 41.12  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  11 KNILLTGATGFLGKVLLEKLLRscpKVNSVYVLVRQKAGQTPQERVEEILSgklfDRlrdENPDfrqkiiainsELTQpk 90
Cdd:cd05265    1 MKILIIGGTRFIGKALVEELLA---AGHDVTVFNRGRTKPDLPEGVEHIVG----DR---NDRD----------ALEE-- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  91 lALSEEDKEIIIDStnvifhCAATVRFNENLRDAVQLNViatRQLILlaqqmknlevfmhVSTAYAYCNRkhidevvypp 170
Cdd:cd05265   59 -LLGGEDFDVVVDT------IAYTPRQVERALDAFKGRV---KQYIF-------------ISSASVYLKP---------- 105
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564330401 171 pvdpkklidslewmdDGLVNDITPKLIGDRPNT-----YIYTKALAEYVVQQEGAkLNVAIVRPSIV 232
Cdd:cd05265  106 ---------------GRVITESTPLREPDAVGLsdpwdYGRGKRAAEDVLIEAAA-FPYTIVRPPYI 156
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
12-56 1.25e-03

NAD dependent epimerase/dehydratase family enzyme [General function prediction only];


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 40.82  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564330401  12 NILLTGATGFLGKVLLEKLLRscpKVNSVYVLVRQKAGQTPQERV 56
Cdd:COG1090    1 KILITGGTGFIGSALVAALLA---RGHEVVVLTRRPPKAPDEVTY 42
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
13-154 1.54e-03

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: 40.68  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  13 ILLTGATGFLGKVLLEKLLRSCPKVNSvyvLVRqkagqtPQERVEEIlsgKLFDRLRDENPDFrqkiiainsELTQPKLA 92
Cdd:cd05193    1 VLVTGASGFVASHVVEQLLERGYKVRA---TVR------DPSKVKKV---NHLLDLDAKPGRL---------ELAVADLT 59
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330401  93 LSEEDKEIIIDSTNViFHCAATVRF-NENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTA 154
Cdd:cd05193   60 DEQSFDEVIKGCAGV-FHVATPVSFsSKDPNEVIKPAIGGTLNALKAAAAAKSVKRFVLTSSA 121
PRK09072 PRK09072
SDR family oxidoreductase;
9-136 1.70e-03

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 40.31  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   9 EGKNILLTGATGFLGKVLLEKLLRSCPKVnsvyVLVrqkaGQTPQErveeilsgklFDRLRDE--NPDfRQKIIAinSEL 86
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARL----LLV----GRNAEK----------LEALAARlpYPG-RHRWVV--ADL 62
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330401  87 TQPK-----LALSEEDKEIiidstNVIFHCAATVRF-------NENLRDAVQLNVIATRQLI 136
Cdd:PRK09072  63 TSEAgreavLARAREMGGI-----NVLINNAGVNHFalledqdPEAIERLLALNLTAPMQLT 119
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
12-135 3.09e-03

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: 39.67  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401  12 NILLTGATGFLGKVLLEKLLRscpkvnsvyvlvrqkagQTPQERVeeilsgKLFDRLRDENPDFRQKIIAINSELTQPKL 91
Cdd:cd05238    2 KVLITGASGFVGQRLAERLLS-----------------DVPNERL------ILIDVVSPKAPSGAPRVTQIAGDLAVPAL 58
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564330401  92 AlseedKEIIIDSTNVIFHCAATV-RFNE-NLRDAVQLNVIATRQL 135
Cdd:cd05238   59 I-----EALANGRPDVVFHLAAIVsGGAEaDFDLGYRVNVDGTRNL 99
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
7-160 5.14e-03

CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4,6-dehydratase, an extended SDR, which catalyzes the conversion of CDP-D-glucose to CDP-4-keto-6-deoxy-D-glucose. 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: 187562 [Multi-domain]  Cd Length: 336  Bit Score: 39.22  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330401   7 YYEGKNILLTGATGFLGKVLLEKLLRSCPKVnSVYVLvrqkagqTPQERVEEILSGKLFDRLRDENPDFRQKIiainsel 86
Cdd:cd05252    1 FWQGKRVLVTGHTGFKGSWLSLWLQELGAKV-IGYSL-------DPPTNPNLFELANLDNKISSTRGDIRDLN------- 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330401  87 tqpKLalseedKEIIIDS-TNVIFHCAAT--VRF-NENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNR 160
Cdd:cd05252   66 ---AL------REAIREYePEIVFHLAAQplVRLsYKDPVETFETNVMGTVNLLEAIRETGSVKAVVNVTSDKCYENK 134
 
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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