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Conserved domains on  [gi|6680289|ref|NP_032319|]
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3 beta-hydroxysteroid dehydrogenase/Delta 5--

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
5-357 0e+00

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


The actual alignment was detected with superfamily member cd09811:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 354  Bit Score: 507.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVQEKE-LQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:cd09811   1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   84 AVIDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNHESTWSDPYPYSKKMAE 163
Cdd:cd09811  81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  164 KAVLAANGSMLKNGGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFSIANP-VYVENVAWAHILAARGLRD 242
Cdd:cd09811 161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  243 PKKstSIQGQFYYISDDTPHQSYDDLNYTLSKEWGLRPNASW-SLPLPLLYWLAFLLETVSFLLRPVYRYRPLFNRHLIT 321
Cdd:cd09811 241 PDK--AIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSWwYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6680289  322 LSNSTFTFSYKKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:cd09811 319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
 
Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 0e+00

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 507.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVQEKE-LQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:cd09811   1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   84 AVIDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNHESTWSDPYPYSKKMAE 163
Cdd:cd09811  81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  164 KAVLAANGSMLKNGGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFSIANP-VYVENVAWAHILAARGLRD 242
Cdd:cd09811 161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  243 PKKstSIQGQFYYISDDTPHQSYDDLNYTLSKEWGLRPNASW-SLPLPLLYWLAFLLETVSFLLRPVYRYRPLFNRHLIT 321
Cdd:cd09811 241 PDK--AIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSWwYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6680289  322 LSNSTFTFSYKKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:cd09811 319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 2.89e-158

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


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 445.27  E-value: 2.89e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKTkvtVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNVIK---YIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     87 DVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNHESTWSDPYPYSKKMAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    167 LAANGSMLKNGGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFS-IANPVYVENVAWAHILAARGLRDPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKFKTGDDNnLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 6680289    246 STSIQGQFYYISDDTPHQSYDDLNYTLSKEWGLRPNaSWSLPL 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLP-SISLPL 279
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-357 1.29e-50

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 171.32  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDkvfRPETKEEfsKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGH--EVVGLD---RSPPGAA--NLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 DVTGVIPRQTIlDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKivlngheeqnHESTWSDP---YPYSKKMAE 163
Cdd:COG0451  76 GVGEEDPDETL-EVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEGPI----------DEDTPLRPvspYGASKLAAE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  164 KAVLAANgsmlKNGGtLNTCALRPMYIYGER-SPFIFNAIIRALKNKGILCVTGKFSIANPVYVENVAWAHILAARGLRD 242
Cdd:COG0451 145 LLARAYA----RRYG-LPVTILRPGNVYGPGdRGVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEAPAA 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  243 PkkstsiqGQFYYISDDTPHqSYDDLNYTLSKEWGLRPnaswslplpllywlaflletvsfllRPVYRYRPLFNRHLItL 322
Cdd:COG0451 220 P-------GGVYNVGGGEPV-TLRELAEAIAEALGRPP-------------------------EIVYPARPGDVRPRR-A 265
                       330       340       350
                ....*....|....*....|....*....|....*
gi 6680289  323 SNStftfsykKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:COG0451 266 DNS-------KARRELGWRPRTSLEEGLRETVAWY 293
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
8-236 1.44e-10

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 61.57  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVID 87
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESSFEQAIEGCDAVFHTASPVF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    88 VTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIvlnGHEEQNHESTWSDP---------YPYS 158
Cdd:PLN02986  90 FTVKDPQTELIDPALKGTINVLNTCKETPSVKRVILTSSTAAVLFRQPPI---EANDVVDETFFSDPslcretknwYPLS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   159 KKMAEKAVLaangSMLKNGGtLNTCALRPMYIYGERSPFIFNAIIRALKNkgilCVTGKFSIANPVY----VENVAWAHI 234
Cdd:PLN02986 167 KILAENAAW----EFAKDNG-IDMVVLNPGFICGPLLQPTLNFSVELIVD----FINGKNLFNNRFYrfvdVRDVALAHI 237

                 ..
gi 6680289   235 LA 236
Cdd:PLN02986 238 KA 239
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-192 7.84e-09

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: 56.65  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLV----QEKELQEVRA---------LDKVFRPETKEEFSklQTKTKVTVLEGDI------LDAQ 67
Cdd:TIGR01746   3 LLTGATGFLGAYLLEELLrrstRAKVICLVRAdseehamerLREALRSYRLWHEN--LAMERIEVVAGDLskprlgLSDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     68 CLRRACQGISVVIHTAAVIDVtgVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNH 147
Cdd:TIGR01746  81 EWERLAENVDTIVHNGALVNH--VYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVTEDDATVTP 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6680289    148 ESTWSDPYPYSKKMAEKAVLAANgsmlkNGGtLNTCALRPMYIYG 192
Cdd:TIGR01746 159 YPGLAGGYTQSKWVAELLVREAS-----DRG-LPVTIVRPGRILG 197
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-126 1.82e-06

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 47.86  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289       7 LVTGAGGFVGQRIIKMLVQekelQEVRALdkVF---RPETKEEFSKLQTK-----TKVTVLEGDILDAQCLRRACQGISV 78
Cdd:smart00822   4 LITGGLGGLGRALARWLAE----RGARRL--VLlsrSGPDAPGAAALLAEleaagARVTVVACDVADRDALAAVLAAIPA 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680289      79 -------VIHTAAVIDvTGVIPRQTILDVN------LKGTQNLLEACVQASVPAFIFCSSV 126
Cdd:smart00822  78 vegpltgVIHAAGVLD-DGVLASLTPERFAavlapkAAGAWNLHELTADLPLDFFVLFSSI 137
 
Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 0e+00

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 507.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVQEKE-LQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:cd09811   1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   84 AVIDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNHESTWSDPYPYSKKMAE 163
Cdd:cd09811  81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  164 KAVLAANGSMLKNGGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFSIANP-VYVENVAWAHILAARGLRD 242
Cdd:cd09811 161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  243 PKKstSIQGQFYYISDDTPHQSYDDLNYTLSKEWGLRPNASW-SLPLPLLYWLAFLLETVSFLLRPVYRYRPLFNRHLIT 321
Cdd:cd09811 241 PDK--AIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSWwYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6680289  322 LSNSTFTFSYKKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:cd09811 319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 2.89e-158

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


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 445.27  E-value: 2.89e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKTkvtVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNVIK---YIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     87 DVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNHESTWSDPYPYSKKMAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    167 LAANGSMLKNGGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFS-IANPVYVENVAWAHILAARGLRDPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKFKTGDDNnLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 6680289    246 STSIQGQFYYISDDTPHQSYDDLNYTLSKEWGLRPNaSWSLPL 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLP-SISLPL 279
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
5-357 8.54e-110

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 324.38  E-value: 8.54e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVQEkELQEVRALDKVFRPETKEEFSKLQTKtkvtVLEGDILDAQCLRRACQGISVVIHTAA 84
Cdd:cd05241   1 SVLVTGGSGFFGERLVKQLLER-GGTYVRSFDIAPPGEALSAWQHPNIE----FLKGDITDRNDVEQALSGADCVFHTAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDVTGviPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPnsyKKIVLNGHEEQNHESTWSDPYPYSKKMAEK 164
Cdd:cd05241  76 IVPLAG--PRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFG---GQNIHNGDETLPYPPLDSDMYAETKAIAEI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  165 AVLAANGSmlkngGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTG-KFSIANPVYVENVAWAHILAARGLRDP 243
Cdd:cd05241 151 IVLEANGR-----DDLLTCALRPAGIFGPGDQGLVPILFEWAEKGLVKFVFGrGNNLVDFTYVHNLAHAHILAAAALVKG 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  244 KKstsIQGQFYYISDDTPHQSYDDLNYTLsKEWGLRPNASWSLPLPLLYWLAFLLETVSFLLRPVYRYRPLFNRHLITls 323
Cdd:cd05241 226 KT---ISGQTYFITDAEPHNMFELLRPVW-KALGFGSRPKIRLSGPLAYCAALLSELVSFMLGPYFVFSPFYVRALVT-- 299
                       330       340       350
                ....*....|....*....|....*....|....
gi 6680289  324 nsTFTFSYKKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:cd05241 300 --PMYFSIAKAQKDLGYAPRYSNEEGLIETLNWY 331
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
5-357 8.81e-64

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 206.44  E-value: 8.81e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVqEKELQEVRALDKVFRPETKEEFSKlqtktKVTVLEGDILDAQCLRRA--CQGISVVIHT 82
Cdd:cd09813   1 SCLVVGGSGFLGRHLVEQLL-RRGNPTVHVFDIRPTFELDPSSSG-----RVQFHTGDLTDPQDLEKAfnEKGPNVVFHT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   83 AAVIDVTGvipRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVagpnsykkiVLNGHEEQNHESTWS------DPYP 156
Cdd:cd09813  75 ASPDHGSN---DDLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASV---------VFNGQDIINGDESLPypdkhqDAYN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  157 YSKKMAEKAVLAANGSMLKnggtLNTCALRPMYIYGERSPFIFNAIIRALKNKgilcvTGKFSIANP------VYVENVA 230
Cdd:cd09813 143 ETKALAEKLVLKANDPESG----LLTCALRPAGIFGPGDRQLVPGLLKAAKNG-----KTKFQIGDGnnlfdfTYVENVA 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  231 WAHILAARGLRDPKKSTSIQGQFYYISDDTPHQSYdDLNYTLSKEWGLRPNASWSLPLPLLYWLAFLLETVSFLLRPVyr 310
Cdd:cd09813 214 HAHILAADALLSSSHAETVAGEAFFITNDEPIYFW-DFARAIWEGLGYERPPSIKLPRPVALYLASLLEWTCKVLGKE-- 290
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 6680289  311 yrPLFNRHLITLSNSTFTFSYKKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:cd09813 291 --PTFTPFRVALLCSTRYFNIEKAKKRLGYTPVVTLEEGIERTLQWF 335
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-357 1.29e-50

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 171.32  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDkvfRPETKEEfsKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGH--EVVGLD---RSPPGAA--NLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 DVTGVIPRQTIlDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKivlngheeqnHESTWSDP---YPYSKKMAE 163
Cdd:COG0451  76 GVGEEDPDETL-EVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEGPI----------DEDTPLRPvspYGASKLAAE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  164 KAVLAANgsmlKNGGtLNTCALRPMYIYGER-SPFIFNAIIRALKNKGILCVTGKFSIANPVYVENVAWAHILAARGLRD 242
Cdd:COG0451 145 LLARAYA----RRYG-LPVTILRPGNVYGPGdRGVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEAPAA 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  243 PkkstsiqGQFYYISDDTPHqSYDDLNYTLSKEWGLRPnaswslplpllywlaflletvsfllRPVYRYRPLFNRHLItL 322
Cdd:COG0451 220 P-------GGVYNVGGGEPV-TLRELAEAIAEALGRPP-------------------------EIVYPARPGDVRPRR-A 265
                       330       340       350
                ....*....|....*....|....*....|....*
gi 6680289  323 SNStftfsykKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:COG0451 266 DNS-------KARRELGWRPRTSLEEGLRETVAWY 293
3b-HSD_like_1_SDR_e cd09812
3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An ...
5-342 6.55e-50

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187672 [Multi-domain]  Cd Length: 339  Bit Score: 170.76  E-value: 6.55e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVQEKE---LQEVRALDKVFRPETKeefsklqtktkvtVLEGDILDAQCLRRACQGISVVIH 81
Cdd:cd09812   1 SVLITGGGGYFGFRLGCALAKSGVhviLFDIRRPQQELPEGIK-------------FIQADVRDLSQLEKAVAGVDCVFH 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   82 TAAViDVTGV--IPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVA--------GPNSYKKIVLNGHeeqnhestw 151
Cdd:cd09812  68 IASY-GMSGReqLNRELIEEINVRGTENIIQVCVRRRVPRLIYTSTFNVIfggqpirnGDESLPYLPLDLH--------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  152 SDPYPYSKKMAEKAVLAANGSMLKN-GGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKF-SIANPVYVENV 229
Cdd:cd09812 138 VDHYSRTKSIAEQLVLKANNMPLPNnGGVLRTCALRPAGIYGPGEQRHLPRIVSYIEKGLFMFVYGDPkSLVEFVHVDNL 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  230 AWAHILAARGLRDPKKSTSiQGQFYYISDDTPHQSYddlnytlskEWgLRP--------NASWSLPLPLLYWLAFLLETV 301
Cdd:cd09812 218 VQAHILAAEALTTAKGYIA-SGQAYFISDGRPVNNF---------EF-FRPlveglgysFPSLRLPLSLVYFFAFLTEMV 286
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 6680289  302 SFLLRPVYRYRPLFNRHLITLSNSTFTFSYKKAQRDLGYEP 342
Cdd:cd09812 287 HFALGPICNFQPLLTRTEVYKTGVTHYFSIEKARAELGYEP 327
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
7-357 4.53e-45

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: 157.45  E-value: 4.53e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALdkvFRPETKEEFSKlqtKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:cd05228   2 LVTGATGFLGSNLVRALLAQGY--RVRAL---VRSGSDAVLLD---GLPVEVVEGDLTDAASLAAAMKGCDRVFHLAAFT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 DVTGVIPRQtILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIvlngHEEQNHEStWSDPYPY--SKKMAEK 164
Cdd:cd05228  74 SLWAKDRKE-LYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRI----DETTPWNE-RPFPNDYyrSKLLAEL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  165 AVLAAngsmLKNGgtLNTCALRPMYIYG--ERSPFIFNAII-RALKNKGILCVTGKFSIanpVYVENVAWAHILAA-RGL 240
Cdd:cd05228 148 EVLEA----AAEG--LDVVIVNPSAVFGpgDEGPTSTGLDVlDYLNGKLPAYPPGGTSF---VDVRDVAEGHIAAMeKGR 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  241 RdpkkstsiqGQFYYISDdtPHQSYDDLNYTLSKEWGLRPnASWSLPLPLLYWLAFLLETVSFLlrpvYRYRPLFNRHLI 320
Cdd:cd05228 219 R---------GERYILGG--ENLSFKQLFETLAEITGVKP-PRRTIPPWLLKAVAALSELKARL----TGKPPLLTPRTA 282
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 6680289  321 TLSNSTFTFSYKKAQRDLGYEPlVNWEEAKQKTSEWI 357
Cdd:cd05228 283 RVLRRNYLYSSDKARRELGYSP-RPLEEALRDTLAWL 318
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
7-238 1.39e-28

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: 111.24  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDkvfRPETKEEFSKLQtktKVTVLEGDILDAQCLRRACQ--GISVVIHTAA 84
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKG--YEVIGLD---RLTSASNTARLA---DLRFVEGDLTDRDALEKLLAdvRPDAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     85 V--IDVTGVIPRQTIlDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPnsykkivlnGHEEQNHESTWSD------PYP 156
Cdd:pfam01370  74 VggVGASIEDPEDFI-EANVLGTLNLLEAARKAGVKRFLFASSSEVYGD---------GAEIPQEETTLTGplapnsPYA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    157 YSKKMAEKAVLAANGSmlkngGTLNTCALRPMYIYGERSP------FIFNAIIRALKNKGILcvtgKFSIANP----VYV 226
Cdd:pfam01370 144 AAKLAGEWLVLAYAAA-----YGLRAVILRLFNVYGPGDNegfvsrVIPALIRRILEGKPIL----LWGDGTQrrdfLYV 214
                         250
                  ....*....|..
gi 6680289    227 ENVAWAHILAAR 238
Cdd:pfam01370 215 DDVARAILLALE 226
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
6-236 1.64e-24

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


Pssm-ID: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 101.50  E-value: 1.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    6 CLVTGAGGFVGQRIIKMLvqekeLQE---VRAldKVFRPETKEEFSKLQ----TKTKVTVLEGDILDAQCLRRACQGISV 78
Cdd:cd08958   1 VCVTGASGFIGSWLVKRL-----LQRgytVRA--TVRDPGDEKKVAHLLelegAKERLKLFKADLLDYGSFDAAIDGCDG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   79 VIHTAAVIDVTGVIPRQTILDVNLKGTQNLLEACVQA-SVPAFIFCSSVD--VAGPNSYKKIVLNgheeqnhESTWSDP- 154
Cdd:cd08958  74 VFHVASPVDFDSEDPEEEMIEPAVKGTLNVLEACAKAkSVKRVVFTSSVAavVWNPNRGEGKVVD-------ESCWSDLd 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  155 --------YPYSKKMAEKAVLAANGsmlKNGgtLNTCALRPMYIYGersPFIF-------NAIIRALKNKGILCVTGKFS 219
Cdd:cd08958 147 fckktklwYALSKTLAEKAAWEFAE---ENG--LDLVTVNPSLVVG---PFLQpslnsssQLILSLLKGNAEMYQNGSLA 218
                       250
                ....*....|....*..
gi 6680289  220 IanpVYVENVAWAHILA 236
Cdd:cd08958 219 L---VHVDDVADAHILL 232
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
6-357 2.05e-24

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


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 101.53  E-value: 2.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    6 CLVTGAGGFVGQRIIKMLVqeKELQEVRALDK--VFRPETKEEFsklqtKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:cd05256   2 VLVTGGAGFIGSHLVERLL--ERGHEVIVLDNlsTGKKENLPEV-----KPNVKFIEGDIRDDELVEFAFEGVDYVFHQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   84 AVIDVTGVI--PRQTiLDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIvlngheEQNHESTWSDPYPYSKKM 161
Cdd:cd05256  75 AQASVPRSIedPIKD-HEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPK------DEDHPPNPLSPYAVSKYA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  162 AEKAVLAANGSMlknggTLNTCALRPMYIYGERS-PF--------IFnaIIRALKNKGILCV-TGK----FsianpVYVE 227
Cdd:cd05256 148 GELYCQVFARLY-----GLPTVSLRYFNVYGPRQdPNggyaavipIF--IERALKGEPPTIYgDGEqtrdF-----TYVE 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  228 NVAWAHILAAR-GLRdpkkstsiqGQFYYISDDTPHQsyddLNYtlskewglrpnaswslplpllywLAFLL-ETVSFLL 305
Cdd:cd05256 216 DVVEANLLAATaGAG---------GEVYNIGTGKRTS----VNE-----------------------LAELIrEILGKEL 259
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 6680289  306 RPVYR-YRPLFNRHliTLSNSTftfsykKAQRDLGYEPLVNWEEAKQKTSEWI 357
Cdd:cd05256 260 EPVYApPRPGDVRH--SLADIS------KAKKLLGWEPKVSFEEGLRLTVEWF 304
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-238 5.15e-23

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


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 95.06  E-value: 5.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    6 CLVTGAGGFVGQRIIKMLvqekelqevraldkvfrpetkeefskLQTKTKVTVLegDILDaqclrracqgisVVIHTAAV 85
Cdd:cd08946   1 ILVTGGAGFIGSHLVRRL--------------------------LERGHEVVVI--DRLD------------VVVHLAAL 40
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   86 IDVTGVIPRQT-ILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGpnsykkivlNGHEEQNHESTWSDPY-PY--SKKM 161
Cdd:cd08946  41 VGVPASWDNPDeDFETNVVGTLNLLEAARKAGVKRFVYASSASVYG---------SPEGLPEEEETPPRPLsPYgvSKLA 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  162 AEKAVLAANgsmlkNGGTLNTCALRPMYIYG----ERSPFIFNAIIRALKNKGILCVTGKF-SIANPVYVENVAWAHILA 236
Cdd:cd08946 112 AEHLLRSYG-----ESYGLPVVILRLANVYGpgqrPRLDGVVNDFIRRALEGKPLTVFGGGnQTRDFIHVDDVVRAILHA 186

                ..
gi 6680289  237 AR 238
Cdd:cd08946 187 LE 188
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-353 8.20e-23

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


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 97.04  E-value: 8.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALdkVFRPETKEEfsklqtktkvTVLEGDILDAQCLRRACQGISVVIHTAA-- 84
Cdd:cd05232   3 LVTGANGFIGRALVDKLLSRGE--EVRIA--VRNAENAEP----------SVVLAELPDIDSFTDLFLGVDAVVHLAArv 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 -VIDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNsykkivlNGHEEQNHESTW--SDPYPYSKKM 161
Cdd:cd05232  69 hVMNDQGADPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEG-------TVGAPFDETDPPapQDAYGRSKLE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  162 AEKAV--LAANGSMlknggtlNTCALRPMYIYGERSPFIFNAIIRALKNKGIL---CVTGKFSIanpVYVENVAWAHILA 236
Cdd:cd05232 142 AERALleLGASDGM-------EVVILRPPMVYGPGVRGNFARLMRLIDRGLPLppgAVKNRRSL---VSLDNLVDAIYLC 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  237 argLRDPKKStsiqGQFYYISDDTPHqSYDDLNYTLSKEWGLRPnasWSLPLPllywlAFLLETVSFLLRPVYRYRPLFn 316
Cdd:cd05232 212 ---ISLPKAA----NGTFLVSDGPPV-STAELVDEIRRALGKPT---RLLPVP-----AGLLRFAAKLLGKRAVIQRLF- 274
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 6680289  317 rhlitlsnSTFTFSYKKAQRDLGYEPLVNWEEAKQKT 353
Cdd:cd05232 275 --------GSLQYDPEKTQNELGWRPPISLEEGLQET 303
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
7-289 3.56e-21

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


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 92.33  E-value: 3.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLvqekeLQE-------VRALDKvfRPETKEEFSKLQTKTKVTVLEGDILDA-QCLRRACQGISV 78
Cdd:cd05227   3 LVTGATGFIASHIVEQL-----LKAgykvrgtVRSLSK--SAKLKALLKAAGYNDRLEFVIVDDLTApNAWDEALKGVDY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   79 VIHTAAVIDVTGVIPRQTILDVNLKGTQNLLEACVQA-SVPAFIFCSSV-DVAGPNSY-KKIVLNgheeqnhESTWSD-- 153
Cdd:cd05227  76 VIHVASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKAAgSVKRVVLTSSVaAVGDPTAEdPGKVFT-------EEDWNDlt 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  154 --------PYPYSKKMAEKA---VLAANgsmlKNGGTLNTcaLRPMYIYGersPFIF-------NAIIRALknkgilcVT 215
Cdd:cd05227 149 isksngldAYIASKTLAEKAaweFVKEN----KPKFELIT--INPGYVLG---PSLLadelnssNELINKL-------LD 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  216 GKFS----IANPVYVEN--VAWAHILAargLRDPKKStsiqGQFYYISdDTPHQSYDDLNyTLSKEWglrPNASWSLPLP 289
Cdd:cd05227 213 GKLPaippNLPFGYVDVrdVADAHVRA---LESPEAA----GQRFIVS-AGPFSFQEIAD-LLREEF---PQLTAPFPAP 280
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
6-193 1.24e-20

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: 90.89  E-value: 1.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    6 CLVTGAGGFVGQRIIKMLVQEKElqEVRALDkvfRPETKEEFSKLQT-----KTKVTVLEGDI------LDAQCLRRACQ 74
Cdd:cd05263   1 VFVTGGTGFLGRHLVKRLLENGF--KVLVLV---RSESLGEAHERIEeagleADRVRVLEGDLtqpnlgLSAAASRELAG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   75 GISVVIHTAAVIDVTgvIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYkkivLNGHEEQNHESTWSDP 154
Cdd:cd05263  76 KVDHVIHCAASYDFQ--APNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNREG----NIRETELNPGQNFKNP 149
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6680289  155 YPYSKKMAEKAVLAAngsmlknGGTLNTCALRPMYIYGE 193
Cdd:cd05263 150 YEQSKAEAEQLVRAA-------ATQIPLTVYRPSIVVGD 181
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
7-243 1.93e-20

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: 88.36  E-value: 1.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALdkVFRPETKEEFSKLQtktkVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARG--HPVRAL--VRDPEKAAALAAAG----VEVVQGDLDDPESLAAALAGVDAVFLLVPSG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 DVTGViprqtilDVNLKGTQNLLEACVQASVPAFIFCSSVDVagpnsykkivlngheeqnHESTWSDPYPySKKMAEKAV 166
Cdd:COG0702  75 PGGDF-------AVDVEGARNLADAAKAAGVKRIVYLSALGA------------------DRDSPSPYLR-AKAAVEEAL 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  167 LAANgsmlknggtLNTCALRPMYIYGErspfiFNAIIRALKNKGIL---CVTGKFSianPVYVENVAWAhilAARGLRDP 243
Cdd:COG0702 129 RASG---------LPYTILRPGWFMGN-----LLGFFERLRERGVLplpAGDGRVQ---PIAVRDVAEA---AAAALTDP 188
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
7-169 1.44e-19

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: 87.19  E-value: 1.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQeVRALdkvFRPETKEE-FSKLQTKTK------------VTVLEGDI------LDAQ 67
Cdd:COG3320   4 LLTGATGFLGAHLLRELLRRTDAR-VYCL---VRASDEAAaRERLEALLEryglwleldasrVVVVAGDLtqprlgLSEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   68 CLRRACQGISVVIHTAAVIDVTGviPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLngHEEQNH 147
Cdd:COG3320  80 EFQELAEEVDAIVHLAALVNLVA--PYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFE--EDDLDE 155
                       170       180
                ....*....|....*....|..
gi 6680289  148 ESTWSDPYPYSKKMAEKAVLAA 169
Cdd:COG3320 156 GQGFANGYEQSKWVAEKLVREA 177
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
7-349 5.29e-17

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


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 80.49  E-value: 5.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEefsklqtktKVTVLEGDILDAQC---LRRAcqGISVVIHTA 83
Cdd:cd05240   2 LVTGAAGGLGRLLARRLAASPRVIGVDGLDRRRPPGSPP---------KVEYVRLDIRDPAAadvFRER--EADAVVHLA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   84 AVID--VTGVIPRQtildVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLngheEQNHESTWSDPYPYSKKM 161
Cdd:cd05240  71 FILDppRDGAERHR----INVDGTQNVLDACAAAGVPRVVVTSSVAVYGAHPDNPAPL----TEDAPLRGSPEFAYSRDK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  162 AEKAVLAAngSMLKNGGTLNTCALRPMYIYGersPFIFNaIIRALKNKGILCVTGKFSIA-NPVYVENVAWAhilAARGL 240
Cdd:cd05240 143 AEVEQLLA--EFRRRHPELNVTVLRPATILG---PGTRN-TTRDFLSPRRLPVPGGFDPPfQFLHEDDVARA---LVLAV 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  241 RDPKKSTsiqgqfYYISDDTPHQSYDDLnytlsKEWGLRPnasWSLPLPLLYWLAFLLetvSFLLRPVYRYRPLFNRHLI 320
Cdd:cd05240 214 RAGATGI------FNVAGDGPVPLSLVL-----ALLGRRP---VPLPSPLPAALAAAR---RLGLRPLPPEQLDFLQYPP 276
                       330       340
                ....*....|....*....|....*....
gi 6680289  321 TLSNStftfsykKAQRDLGYEPLVNWEEA 349
Cdd:cd05240 277 VMDTT-------RARVELGWQPKHTSAEV 298
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
7-208 5.76e-16

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


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 77.72  E-value: 5.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVqeKELQEVRALDK--VFRPETKEEFSklqTKTKVTVLEGDILDAQCLRRACQGISVVIHTAA 84
Cdd:cd05257   3 LVTGADGFIGSHLTERLL--REGHEVRALDIynSFNSWGLLDNA---VHDRFHFISGDVRDASEVEYLVKKCDVVFHLAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDV-TGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNHESTWsdPYPYSKKMAE 163
Cdd:cd05257  78 LIAIpYSYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPIDEDHPLLYINKPRS--PYSASKQGAD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6680289  164 KAVLAangSMLKNGgtLNTCALRPMYIYGERS---PFIFNAIIRALKN 208
Cdd:cd05257 156 RLAYS---YGRSFG--LPVTIIRPFNTYGPRQsarAVIPTIISQRAIG 198
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
7-135 1.07e-15

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 74.96  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALdkvFRPETKEEFSKLQtktKVTVLEGDILDAQCLRRACQGISVVIHTAAvi 86
Cdd:cd05243   3 LVVGATGKVGRHVVRELLDRGY--QVRAL---VRDPSQAEKLEAA---GAEVVVGDLTDAESLAAALEGIDAVISAAG-- 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6680289   87 dvTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYK 135
Cdd:cd05243  73 --SGGKGGPRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPL 119
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
6-317 7.04e-15

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 73.82  E-value: 7.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    6 CLVTGAGGFVGQRIIKMLVqeKELQEVRAldkVFRPETKEEFSKLQTK-TKVTVLEGDILDAQCLRRACQGISVVIHTAA 84
Cdd:cd05271   3 VTVFGATGFIGRYVVNRLA--KRGSQVIV---PYRCEAYARRLLVMGDlGQVLFVEFDLRDDESIRKALEGSDVVINLVG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDVTGvipRQTILDVNLKGTQNLLEACVQASVPAFIFCSS--VDVAGPNSYKKivlngheeqnhestwsdpypySKKMA 162
Cdd:cd05271  78 RLYETK---NFSFEDVHVEGPERLAKAAKEAGVERLIHISAlgADANSPSKYLR---------------------SKAEG 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  163 EKAVLAAngsmlknggTLNTCALRPMYIYGERSPFiFNAIIRALK----NKGILCVTGKFsiaNPVYVENVAWAhilAAR 238
Cdd:cd05271 134 EEAVREA---------FPEATIVRPSVVFGREDRF-LNRFAKLLAflpfPPLIGGGQTKF---QPVYVGDVAEA---IAR 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  239 GLRDPkkstSIQGQFYYISDdtPHQsyddlnYTLSK--EWGLRPNASWSLPLPLLYWLAFLLETVSFLLRPvyrYRPLFN 316
Cdd:cd05271 198 ALKDP----ETEGKTYELVG--PKV------YTLAElvELLRRLGGRKRRVLPLPLWLARLIARVKLLLLL---PEPPLT 262

                .
gi 6680289  317 R 317
Cdd:cd05271 263 R 263
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
7-202 1.21e-14

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: 71.28  E-value: 1.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDKVFRPETKEEfsklqtKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:cd05226   2 LILGATGFIGRALARELLEQG--HEVTLLVRNTKRLSKED------QEPVAVVEGDLRDLDSLSDAVQGVDVVIHLAGAP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 DVTgviprQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGpnsykkivlNGHEEQNHEStwSDPYPYSKKMAEKAV 166
Cdd:cd05226  74 RDT-----RDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYG---------DLHEETEPSP--SSPYLAVKAKTEAVL 137
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6680289  167 LAANgsmlknggtLNTCALRPMYIYGERSPFIFNAI 202
Cdd:cd05226 138 REAS---------LPYTIVRPGVIYGDLARAIANAV 164
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
7-163 1.60e-14

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


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 73.19  E-value: 1.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVfrPETKEEFSklqtkTKVTVLEGDiLDAQCLRRA--CQGISVVIHTAA 84
Cdd:cd05238   4 LITGASGFVGQRLAERLLSDVPNERLILIDVV--SPKAPSGA-----PRVTQIAGD-LAVPALIEAlaNGRPDVVFHLAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDVTGVIPRQTILDVNLKGTQNLLEAC-VQASVPAFIFCSSVDVAGPNSYKKIVLNGHeeqnhestwSDP---YPYSKK 160
Cdd:cd05238  76 IVSGGAEADFDLGYRVNVDGTRNLLEALrKNGPKPRFVFTSSLAVYGLPLPNPVTDHTA---------LDPassYGAQKA 146

                ...
gi 6680289  161 MAE 163
Cdd:cd05238 147 MCE 149
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
8-196 1.79e-14

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


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 72.64  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      8 VTGAGGFVGQRII-KMLVQEKELQE----VRALDK---------------VFRPETKEEFSKlqtktkVTVLEGDI---- 63
Cdd:pfam07993   1 LTGATGFLGKVLLeKLLRSTPDVKKiyllVRAKDGesalerlrqelekypLFDALLKEALER------IVPVAGDLsepn 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     64 --LDAQCLRRACQGISVVIHTAAviDVTGVIPRQTILDVNLKGTQNLLEACVQ-ASVPAFIFCSS-----------VDVA 129
Cdd:pfam07993  75 lgLSEEDFQELAEEVDVIIHSAA--TVNFVEPYDDARAVNVLGTREVLRLAKQgKQLKPFHHVSTayvngergglvEEKP 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6680289    130 GPNSYKKIVLNGhEEQNHESTWSDPYPYSKKMAEKAVLAAngsmlkNGGTLNTCALRPMYIYGERSP 196
Cdd:pfam07993 153 YPEGEDDMLLDE-DEPALLGGLPNGYTQTKWLAEQLVREA------ARRGLPVVIYRPSIITGEPKT 212
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
7-201 2.48e-14

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: 72.68  E-value: 2.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQEVRALdkVFRPETKEEFSKLQTK--------------TKVTVLEGDI------LDA 66
Cdd:cd05235   3 LLTGATGFLGAYLLRELLKRKNVSKIYCL--VRAKDEEAALERLIDNlkeyglnlwdelelSRIKVVVGDLskpnlgLSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   67 QCLRRACQGISVVIHTAAviDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHE-EQ 145
Cdd:cd05235  81 DDYQELAEEVDVIIHNGA--NVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEESDdML 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680289  146 NHESTWSDPYPYSKKMAEKAVLAANGSMLknggtlntcalrPMYIYgeRSPFIFNA 201
Cdd:cd05235 159 ESQNGLPNGYIQSKWVAEKLLREAANRGL------------PVAII--RPGNIFGD 200
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-164 1.94e-13

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


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 70.26  E-value: 1.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDKVFRpeTKEEFSKLQTKTKVTVLEGDILDAQCLRR--ACQGISVVIHTAA 84
Cdd:cd05247   3 LVTGGAGYIGSHTVVELLEAGY--DVVVLDNLSN--GHREALPRIEKIRIEFYEGDIRDRAALDKvfAEHKIDAVIHFAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDVtGVIPRQTIL--DVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIvlngheEQNHESTWSDPYPYSKKMA 162
Cdd:cd05247  79 LKAV-GESVQKPLKyyDNNVVGTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVPI------TEEAPLNPTNPYGRTKLMV 151

                ..
gi 6680289  163 EK 164
Cdd:cd05247 152 EQ 153
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
7-237 3.13e-13

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: 69.63  E-value: 3.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRII-KMLVQEKELQEVRAL---------DKVFRPETKE-EFSKLQ-----TKTKVTVLEGDILDAQC-- 68
Cdd:cd05236   4 LITGATGFLGKVLLeKLLRSCPDIGKIYLLirgksgqsaEERLRELLKDkLFDRGRnlnplFESKIVPIEGDLSEPNLgl 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   69 ----LRRACQGISVVIHTAAVIDVTGVIPrqTILDVNLKGTQNLLEACVQ-ASVPAFIFCSSVDVAGPNSY--KKIV--- 138
Cdd:cd05236  84 sdedLQTLIEEVNIIIHCAATVTFDERLD--EALSINVLGTLRLLELAKRcKKLKAFVHVSTAYVNGDRQLieEKVYppp 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  139 LNGHEEQNHEST----------------WSDPYPYSKKMAEKAVlaangsmLKNGGTLNTCALRPMYIYGE-RSPF---- 197
Cdd:cd05236 162 ADPEKLIDILELmddleleratpkllggHPNTYTFTKALAERLV-------LKERGNLPLVIVRPSIVGATlKEPFpgwi 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6680289  198 -IFNAIIRALK--NKGILCVT--GKFSIANPVYVENVAWAHILAA 237
Cdd:cd05236 235 dNFNGPDGLFLayGKGILRTMnaDPNAVADIIPVDVVANALLAAA 279
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
7-356 6.21e-13

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


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 68.73  E-value: 6.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQ--GISVVIHTAA 84
Cdd:cd05246   4 LVTGGAGFIGSNFVRYLLNKYPDYKIINLDKLTYAGNLENLEDVSSSPRYRFVKGDICDAELVDRLFEeeKIDAVIHFAA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 --VIDVTGVIPRQTIlDVNLKGTQNLLEACVQASVPAFIFCSSVDVagpnsYkkivlnGHEEQNHESTWSDPY----PY- 157
Cdd:cd05246  84 esHVDRSISDPEPFI-RTNVLGTYTLLEAARKYGVKRFVHISTDEV-----Y------GDLLDDGEFTETSPLaptsPYs 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  158 -SKKMAEKAVLAANGSmlkngGTLNTCALRPMYIYGersPF------IFNAIIRALKNKGiLCVTGK-FSIANPVYVENV 229
Cdd:cd05246 152 aSKAAADLLVRAYHRT-----YGLPVVITRCSNNYG---PYqfpeklIPLFILNALDGKP-LPIYGDgLNVRDWLYVEDH 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  230 AWA-HILAARGlrdpkkstsIQGQFYYISDDTPhQSYDDLNYTLSKEWGlrpnASWSlplpllyWLAFLLEtvsfllRPV 308
Cdd:cd05246 223 ARAiELVLEKG---------RVGEIYNIGGGNE-LTNLELVKLILELLG----KDES-------LITYVKD------RPG 275
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6680289  309 Y--RYRplfnrhlitlsnstftFSYKKAQRDLGYEPLVNWEEAKQKTSEW 356
Cdd:cd05246 276 HdrRYA----------------IDSSKIRRELGWRPKVSFEEGLRKTVRW 309
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
7-167 1.68e-12

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: 67.26  E-value: 1.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALdkvFRPETKEEFSKLQ-----TKTKVTVLEGDILDAQCLRRACQGISVVIH 81
Cdd:cd05193   2 LVTGASGFVASHVVEQLLERG--YKVRAT---VRDPSKVKKVNHLldldaKPGRLELAVADLTDEQSFDEVIKGCAGVFH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   82 TAAVIDVTGVIPRQTILDvNLKGTQNLLEACVQA-SVPAFIFCSSVDVAGPNSYKKIVLnGHEEQ--NHESTWSDP---- 154
Cdd:cd05193  77 VATPVSFSSKDPNEVIKP-AIGGTLNALKAAAAAkSVKRFVLTSSAGSVLIPKPNVEGI-VLDEKswNLEEFDSDPkksa 154
                       170
                ....*....|....*
gi 6680289  155 --YPYSKKMAEKAVL 167
Cdd:cd05193 155 wvYAASKTLAEKAAW 169
NAD_binding_10 pfam13460
NAD(P)H-binding;
10-166 8.06e-12

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 63.39  E-value: 8.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     10 GAGGFVGQRIIKMLVQEKelQEVRALdkvFRpeTKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAvidvt 89
Cdd:pfam13460   1 GATGKIGRLLVKQLLARG--HEVTAL---VR--NPEKLADLEDHPGVEVVDGDVLDPDDLAEALAGQDAVISALG----- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     90 gviprqtILDVNLKGTQNLLEACVQASVPAFIFCSSVDVagpnsykkivlnGHEEQNHESTWSD----PYPYSKKMAEKA 165
Cdd:pfam13460  69 -------GGGTDETGAKNIIDAAKAAGVKRFVLVSSLGV------------GDEVPGPFGPWNKemlgPYLAAKRAAEEL 129

                  .
gi 6680289    166 V 166
Cdd:pfam13460 130 L 130
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
7-170 9.37e-12

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


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 64.84  E-value: 9.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKeLQEVRALDkvfRPETK---------EEFSKLQTKTKVTVLEGDILDAQCLRRACQ--G 75
Cdd:pfam02719   2 LVTGGGGSIGSELCRQILKFN-PKKIILFS---RDELKlyeirqelrEKFNDPKLRFFIVPVIGDVRDRERLERAMEqyG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     76 ISVVIHTAAVIDVTGV--IPRQTILdVNLKGTQNLLEACVQASVPAFIFCSSVDVAGP-NSYkkivlnGHeeqnhestws 152
Cdd:pfam02719  78 VDVVFHAAAYKHVPLVeyNPMEAIK-TNVLGTENVADAAIEAGVKKFVLISTDKAVNPtNVM------GA---------- 140
                         170
                  ....*....|....*...
gi 6680289    153 dpypySKKMAEKAVLAAN 170
Cdd:pfam02719 141 -----TKRLAEKLFQAAN 153
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
7-172 1.12e-11

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: 64.56  E-value: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElQEVRALDkvfRPETK-----EEFSKLQTKTKVTVLEGDILDAQCLRRAC--QGISVV 79
Cdd:cd05237   6 LVTGGAGSIGSELVRQILKFGP-KKLIVFD---RDENKlhelvRELRSRFPHDKLRFIIGDVRDKERLRRAFkeRGPDIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   80 IHTAAVIDVTGV--IPRQTIlDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGP-NSYkkivlnGHeeqnhestwsdpyp 156
Cdd:cd05237  82 FHAAALKHVPSMedNPEEAI-KTNVLGTKNVIDAAIENGVEKFVCISTDKAVNPvNVM------GA-------------- 140
                       170
                ....*....|....*.
gi 6680289  157 ySKKMAEKAVLAANGS 172
Cdd:cd05237 141 -TKRVAEKLLLAKNEY 155
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
7-356 5.86e-11

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


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 63.12  E-value: 5.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDKV---FRPETKEE-FSKLQTKTKVTVLEGDILDAQCLRRACQ--GISVVI 80
Cdd:cd05253   4 LVTGAAGFIGFHVAKRLLERGD--EVVGIDNLndyYDVRLKEArLELLGKSGGFKFVKGDLEDREALRRLFKdhEFDAVI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   81 HTAAVIDVTGVI--PRqTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNsyKKIVLNGHEEQNHESTwsdPYPYS 158
Cdd:cd05253  82 HLAAQAGVRYSLenPH-AYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYGLN--TKMPFSEDDRVDHPIS---LYAAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  159 KKMAEkaVLAANGSMLKNggtLNTCALRPMYIYGE-----RSPFIFnaiIRALKNkgilcvtGKfsianPVYVENvawah 233
Cdd:cd05253 156 KKANE--LMAHTYSHLYG---IPTTGLRFFTVYGPwgrpdMALFLF---TKAILE-------GK-----PIDVFN----- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  234 ilAARGLRDpkkstsiqgqFYYISD---------DTPHQSydDLNYTLSKEWGLRPNASW-------SLPLPLLYWLAfL 297
Cdd:cd05253 211 --DGNMSRD----------FTYIDDivegvvralDTPAKP--NPNWDAEAPDPSTSSAPYrvynignNSPVKLMDFIE-A 275
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680289  298 LEtvSFLLRPVYR-YRPLF-NRHLITLSNSTftfsykKAQRDLGYEPLVNWEEAKQKTSEW 356
Cdd:cd05253 276 LE--KALGKKAKKnYLPMQkGDVPETYADIS------KLQRLLGYKPKTSLEEGVKRFVEW 328
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
7-135 1.09e-10

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


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 62.31  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDKVFRPETKEEFSKLQTKTK---VTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:cd05258   4 LITGGAGFIGSNLARFFLKQGW--EVIGFDNLMRRGSFGNLAWLKANREdggVRFVHGDIRNRNDLEDLFEDIDLIIHTA 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680289   84 AVIDVTGVI--PRQTIlDVNLKGTQNLLEACVQASVPA-FIFCSSVDVAG--PNSYK 135
Cdd:cd05258  82 AQPSVTTSAssPRLDF-ETNALGTLNVLEAARQHAPNApFIFTSTNKVYGdlPNYLP 137
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
8-236 1.44e-10

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 61.57  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVID 87
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESSFEQAIEGCDAVFHTASPVF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    88 VTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIvlnGHEEQNHESTWSDP---------YPYS 158
Cdd:PLN02986  90 FTVKDPQTELIDPALKGTINVLNTCKETPSVKRVILTSSTAAVLFRQPPI---EANDVVDETFFSDPslcretknwYPLS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   159 KKMAEKAVLaangSMLKNGGtLNTCALRPMYIYGERSPFIFNAIIRALKNkgilCVTGKFSIANPVY----VENVAWAHI 234
Cdd:PLN02986 167 KILAENAAW----EFAKDNG-IDMVVLNPGFICGPLLQPTLNFSVELIVD----FINGKNLFNNRFYrfvdVRDVALAHI 237

                 ..
gi 6680289   235 LA 236
Cdd:PLN02986 238 KA 239
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
7-238 2.52e-10

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


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 60.79  E-value: 2.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDkvfRPETKEEFSKlqtkTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:cd05264   3 LIVGGNGFIGSHLVDALLEEG--PQVRVFD---RSIPPYELPL----GGVDYIKGDYENRADLESALVGIDTVIHLASTT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 dVTGVIPRQTILDV--NLKGTQNLLEACVQASVPAFIFCSSvdvaGPNSYkkivlnGHEEQN--HESTWSDP---YPYSK 159
Cdd:cd05264  74 -NPATSNKNPILDIqtNVAPTVQLLEACAAAGIGKIIFASS----GGTVY------GVPEQLpiSESDPTLPissYGISK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  160 KMAEKAVlaangSMLKNGGTLNTCALRPMYIYGER-SP-----FIFNAIIRALKNKGILCVTGKFSIANPVYVENVAWAH 233
Cdd:cd05264 143 LAIEKYL-----RLYQYLYGLDYTVLRISNPYGPGqRPdgkqgVIPIALNKILRGEPIEIWGDGESIRDYIYIDDLVEAL 217

                ....*
gi 6680289  234 ILAAR 238
Cdd:cd05264 218 MALLR 222
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
7-125 2.60e-10

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 59.48  E-value: 2.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALdkVFRPEtkeefsKLQTK-TKVTVLEGDILDAQCLRRACQGISVVIHTAAV 85
Cdd:COG2910   3 AVIGATGRVGSLIVREALARGH--EVTAL--VRNPE------KLPDEhPGLTVVVGDVLDPAAVAEALAGADAVVSALGA 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6680289   86 idvtgviPRQTILDVNLKGTQNLLEACVQASVPAFIFCSS 125
Cdd:COG2910  73 -------GGGNPTTVLSDGARALIDAMKAAGVKRLIVVGG 105
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
7-238 8.47e-10

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 58.99  E-value: 8.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLvqEKELQEVRALDkvfRPetkeefsklqtktkvtvlEGDILDAQCLRRACQGIS--VVIHTAA 84
Cdd:COG1091   3 LVTGANGQLGRALVRLL--AERGYEVVALD---RS------------------ELDITDPEAVAALLEEVRpdVVINAAA 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDVTGV-IPRQTILDVNLKGTQNLLEACVQASVPaFIFCSSvDvagpnsYkkiVLNGHEEQNHESTwsDP------YPY 157
Cdd:COG1091  60 YTAVDKAeSEPELAYAVNATGPANLAEACAELGAR-LIHIST-D------Y---VFDGTKGTPYTED--DPpnplnvYGR 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  158 SKKMAEKAVLAANGsmlknggtlNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFsIANPVYVENVAWA--HIL 235
Cdd:COG1091 127 SKLAGEQAVRAAGP---------RHLILRTSWVYGPHGKNFVKTMLRLLKEGEELRVVDDQ-IGSPTYAADLARAilALL 196

                ...
gi 6680289  236 AAR 238
Cdd:COG1091 197 EKD 199
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
7-112 6.37e-09

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 56.79  E-value: 6.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDKV---FRPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGIS--VVIH 81
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGY--EVHGIVRRsssFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQpdEIYN 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 6680289     82 TAAVIDVTGVI--PRQTIlDVNLKGTQNLLEAC 112
Cdd:pfam16363  79 LAAQSHVDVSFeqPEYTA-DTNVLGTLRLLEAI 110
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-192 7.84e-09

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: 56.65  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLV----QEKELQEVRA---------LDKVFRPETKEEFSklQTKTKVTVLEGDI------LDAQ 67
Cdd:TIGR01746   3 LLTGATGFLGAYLLEELLrrstRAKVICLVRAdseehamerLREALRSYRLWHEN--LAMERIEVVAGDLskprlgLSDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     68 CLRRACQGISVVIHTAAVIDVtgVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSYKKIVLNGHEEQNH 147
Cdd:TIGR01746  81 EWERLAENVDTIVHNGALVNH--VYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVTEDDATVTP 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6680289    148 ESTWSDPYPYSKKMAEKAVLAANgsmlkNGGtLNTCALRPMYIYG 192
Cdd:TIGR01746 159 YPGLAGGYTQSKWVAELLVREAS-----DRG-LPVTIVRPGRILG 197
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
7-194 1.16e-08

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


Pssm-ID: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 55.95  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDkVFRPETKEEFSKlqtktKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:cd05273   4 LVTGAGGFIGSHLAERLKAEG--HYVRGAD-WKSPEHMTQPTD-----DDEFHLVDLREMENCLKATEGVDHVFHLAADM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 DVTGVIPRQ--TILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAgPNSYKKIVLNG--HEEQNHESTWSDPYPYSKKMA 162
Cdd:cd05273  76 GGMGYIQSNhaVIMYNNTLINFNMLEAARINGVERFLFASSACVY-PEFKQLETTVVrlREEDAWPAEPQDAYGWEKLAT 154
                       170       180       190
                ....*....|....*....|....*....|..
gi 6680289  163 EKAVLAANGSMlknggTLNTCALRPMYIYGER 194
Cdd:cd05273 155 ERLCQHYNEDY-----GIETRIVRFHNIYGPR 181
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-130 2.85e-08

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


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 54.61  E-value: 2.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDKvFRPETKEEFSKLQTKTKVTVLEGDILDAQCLRrACQGISVVIHTAAVI 86
Cdd:cd05234   3 LVTGGAGFIGSHLVDRLLEEG--NEVVVVDN-LSSGRRENIEPEFENKAFRFVKRDLLDTADKV-AKKDGDTVFHLAANP 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6680289   87 DVT-GVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAG 130
Cdd:cd05234  79 DVRlGATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSSTVYG 123
PRK07201 PRK07201
SDR family oxidoreductase;
7-130 4.01e-08

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 54.96  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     7 LVTGAGGFVGQRIIKMLVQEKELQEVRALdkvFRPETKEEFSKLQTK---TKVTVLEGDILDAQC-----LRRACQGISV 78
Cdd:PRK07201   4 FVTGGTGFIGRRLVSRLLDRRREATVHVL---VRRQSLSRLEALAAYwgaDRVVPLVGDLTEPGLglseaDIAELGDIDH 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6680289    79 VIHTAAVIDVTGVIPRQTIldVNLKGTQNLLEACVQASVPAFIFCSSVDVAG 130
Cdd:PRK07201  81 VVHLAAIYDLTADEEAQRA--ANVDGTRNVVELAERLQAATFHHVSSIAVAG 130
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
7-126 1.48e-07

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 52.75  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLvqekeLQEVRAldKVF----RPETKEEFSKLQTKTK-------VTVLEGDILDAQCLRRA--- 72
Cdd:cd08953 209 LVTGGAGGIGRALARAL-----ARRYGA--RLVllgrSPLPPEEEWKAQTLAAlealgarVLYISADVTDAAAVRRLlek 281
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680289   73 ----CQGISVVIHTAAVIDvTGVIPRQT------ILDVNLKGTQNLLEACVQASVPAFIFCSSV 126
Cdd:cd08953 282 vrerYGAIDGVIHAAGVLR-DALLAQKTaedfeaVLAPKVDGLLNLAQALADEPLDFFVLFSSV 344
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
5-274 1.69e-07

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: 51.91  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    5 SCLVTGAGGFVGQRIIKMLVQEKelQEV----RALDKVFRPEtkeefsklqtktKVTVLEGDILDAQCLRRACQGISVvi 80
Cdd:cd05265   2 KILIIGGTRFIGKALVEELLAAG--HDVtvfnRGRTKPDLPE------------GVEHIVGDRNDRDALEELLGGEDF-- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   81 htAAVIDVTGVIPRQTildvnlkgtQNLLEACvQASVPAFIFCSSVDVagpnsYKKIVLN-------GHEEQNHESTWSD 153
Cdd:cd05265  66 --DVVVDTIAYTPRQV---------ERALDAF-KGRVKQYIFISSASV-----YLKPGRVitestplREPDAVGLSDPWD 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  154 pYPYSKKMAEKAVLAANGsmlknggtLNTCALRPMYIYGERSPFI--FNAIIRALKNKGILCVTGKFSIANPVYVENVAW 231
Cdd:cd05265 129 -YGRGKRAAEDVLIEAAA--------FPYTIVRPPYIYGPGDYTGrlAYFFDRLARGRPILVPGDGHSLVQFIHVKDLAR 199
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 6680289  232 AhILAARGlrDPKKStsiqGQFYYISDDTPHqSYDDLNYTLSK 274
Cdd:cd05265 200 A-LLGAAG--NPKAI----GGIFNITGDEAV-TWDELLEACAK 234
PLN00198 PLN00198
anthocyanidin reductase; Provisional
8-237 1.86e-07

anthocyanidin reductase; Provisional


Pssm-ID: 215100 [Multi-domain]  Cd Length: 338  Bit Score: 52.20  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLvqekeLQEVRALDKVFR-PETKEEFS---KLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:PLN00198  14 VIGGTGFLASLLIKLL-----LQKGYAVNTTVRdPENQKKIAhlrALQELGDLKIFGADLTDEESFEAPIAGCDLVFHVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    84 AVIDVTGVIPRQTILDVNLKGTQNLLEACVQA-SVPAFIFCSSVDVAGPNSykkivLNGHEEQNHESTWSD--------- 153
Cdd:PLN00198  89 TPVNFASEDPENDMIKPAIQGVHNVLKACAKAkSVKRVILTSSAAAVSINK-----LSGTGLVMNEKNWTDvefltsekp 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   154 ---PYPYSKKMAEKAV-----------------LAANGSMLKNggTLNTCALRPMYIYGERspFIFNAIiralknKGILC 213
Cdd:PLN00198 164 ptwGYPASKTLAEKAAwkfaeennidlitviptLMAGPSLTSD--IPSSLSLAMSLITGNE--FLINGL------KGMQM 233
                        250       260
                 ....*....|....*....|....
gi 6680289   214 VTGKFSIanpVYVENVAWAHILAA 237
Cdd:PLN00198 234 LSGSISI---THVEDVCRAHIFLA 254
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
6-81 2.23e-07

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 51.96  E-value: 2.23e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680289    6 CLVTGAGGFVGQRIIKMLVQEKElqEVRALdkvFRPETKeeFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIH 81
Cdd:cd05245   1 VLVTGATGYVGGRLVPRLLQEGH--QVRAL---VRSPEK--LADRPWSERVTVVRGDLEDPESLRAALEGIDTAYY 69
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
7-161 2.35e-07

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


Pssm-ID: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 51.92  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLvQEKELQEVRALDKVfrpeTKEEFSKLQTKTKVTvlegDILDAQCLRRACQG------ISVVI 80
Cdd:cd05248   3 IVTGGAGFIGSNLVKAL-NERGITDILVVDNL----SNGEKFKNLVGLKIA----DYIDKDDFKDWVRKgdenfkIEAIF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   81 HTAAVIDVT---GVIprqtILDVNLKGTQNLLEACVQASVPaFIFCSSVDVAGpnsykkivlNGHEEQNHESTWS----- 152
Cdd:cd05248  74 HQGACSDTTetdGKY----MMDNNYQYTKELLHYCLEKKIR-FIYASSAAVYG---------NGSLGFAEDIETPnlrpl 139

                ....*....
gi 6680289  153 DPYPYSKKM 161
Cdd:cd05248 140 NVYGYSKLL 148
PLN02650 PLN02650
dihydroflavonol-4-reductase
8-168 3.65e-07

dihydroflavonol-4-reductase


Pssm-ID: 178256 [Multi-domain]  Cd Length: 351  Bit Score: 51.37  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQEKELqeVRAldKVFRPETKEEFSKL----QTKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:PLN02650  10 VTGASGFIGSWLVMRLLERGYT--VRA--TVRDPANVKKVKHLldlpGATTRLTLWKADLAVEGSFDDAIRGCTGVFHVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    84 AVIDVTGVIPRQTILDVNLKGTQNLLEACVQA-SVPAFIFCSSVDVAGPNSYKKIVLNgheeqnhESTWSD--------- 153
Cdd:PLN02650  86 TPMDFESKDPENEVIKPTVNGMLSIMKACAKAkTVRRIVFTSSAGTVNVEEHQKPVYD-------EDCWSDldfcrrkkm 158
                        170
                 ....*....|....*...
gi 6680289   154 ---PYPYSKKMAEKAVLA 168
Cdd:PLN02650 159 tgwMYFVSKTLAEKAAWK 176
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
8-126 5.17e-07

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 50.98  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQEKEL--QEVRALDKVFRpetkeEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAV 85
Cdd:PLN02896  15 VTGATGYIGSWLVKLLLQRGYTvhATLRDPAKSLH-----LLSKWKEGDRLRLFRADLQEEGSFDEAVKGCDGVFHVAAS 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 6680289    86 --IDVTGV------IPRQTILDVNLKGTQNLLEACVQA-SVPAFIFCSSV 126
Cdd:PLN02896  90 meFDVSSDhnnieeYVQSKVIDPAIKGTLNVLKSCLKSkTVKRVVFTSSI 139
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-126 1.82e-06

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 47.86  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289       7 LVTGAGGFVGQRIIKMLVQekelQEVRALdkVF---RPETKEEFSKLQTK-----TKVTVLEGDILDAQCLRRACQGISV 78
Cdd:smart00822   4 LITGGLGGLGRALARWLAE----RGARRL--VLlsrSGPDAPGAAALLAEleaagARVTVVACDVADRDALAAVLAAIPA 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680289      79 -------VIHTAAVIDvTGVIPRQTILDVN------LKGTQNLLEACVQASVPAFIFCSSV 126
Cdd:smart00822  78 vegpltgVIHAAGVLD-DGVLASLTPERFAavlapkAAGAWNLHELTADLPLDFFVLFSSI 137
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
7-175 2.10e-06

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: 48.85  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLvqeKELQ-EVR--ALDKVFRPETKEefSKLQTKTKVTVlEGDILDAQCLRRACQGI--SVVIH 81
Cdd:cd05252   8 LVTGHTGFKGSWLSLWL---QELGaKVIgySLDPPTNPNLFE--LANLDNKISST-RGDIRDLNALREAIREYepEIVFH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   82 TAA--VIDVTGVIPRQTIlDVNLKGTQNLLEACVQA-SVPAFIFCSSVDVagpnsYKkivlngheeqNHESTW------- 151
Cdd:cd05252  82 LAAqpLVRLSYKDPVETF-ETNVMGTVNLLEAIRETgSVKAVVNVTSDKC-----YE----------NKEWGWgyrendp 145
                       170       180
                ....*....|....*....|....*..
gi 6680289  152 ---SDPYPYSKKMAEKAVLAANGSMLK 175
Cdd:cd05252 146 lggHDPYSSSKGCAELIISSYRNSFFN 172
PLN02686 PLN02686
cinnamoyl-CoA reductase
8-242 3.43e-06

cinnamoyl-CoA reductase


Pssm-ID: 215370  Cd Length: 367  Bit Score: 48.62  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQEKelQEVR-ALDKvfrPETKEEFSKLQT-------KTKVTVLEGDILDAQCLRRACQGISVV 79
Cdd:PLN02686  58 VTGGVSFLGLAIVDRLLRHG--YSVRiAVDT---QEDKEKLREMEMfgemgrsNDGIWTVMANLTEPESLHEAFDGCAGV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    80 IHTAAVID---VTGVIPRQTILDVnlKGTQNLLEACVQ-ASVPAFIFCSSVDVAG-----PNSYKKIVlngheeqNHESt 150
Cdd:PLN02686 133 FHTSAFVDpagLSGYTKSMAELEA--KASENVIEACVRtESVRKCVFTSSLLACVwrqnyPHDLPPVI-------DEES- 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   151 WSDP---------YPYSKKMAEKAVL-AANGSMLKnggtLNT-CalrPMYIYG----ERSPfifNAIIRALKNKGILCVT 215
Cdd:PLN02686 203 WSDEsfcrdnklwYALGKLKAEKAAWrAARGKGLK----LATiC---PALVTGpgffRRNS---TATIAYLKGAQEMLAD 272
                        250       260
                 ....*....|....*....|....*..
gi 6680289   216 GKFSIANpvyVENVAWAHILAARGLRD 242
Cdd:PLN02686 273 GLLATAD---VERLAEAHVCVYEAMGN 296
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
7-132 3.81e-06

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. 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: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 47.98  E-value: 3.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEV-----RALDkvFRPETKEEFskLQTKTKVTVLEGDILDAQCLRRACQGIS--VV 79
Cdd:cd05260   3 LITGITGQDGSYLAEFLLEKG--YEVhgivrRSSS--FNTDRIDHL--YINKDRITLHYGDLTDSSSLRRAIEKVRpdEI 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680289   80 IHTAAV--IDVTGVIPRQTiLDVNLKGTQNLLEACVQASVPA-FIFCSSVDVAGPN 132
Cdd:cd05260  77 YHLAAQshVKVSFDDPEYT-AEVNAVGTLNLLEAIRILGLDArFYQASSSEEYGKV 131
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
7-164 4.29e-06

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 48.27  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDKVfrpeTKEEFSKLQTKTKV-----TVLEGDILDAQCLRR--ACQGISVV 79
Cdd:PRK10675   4 LVTGGSGYIGSHTCVQLLQNG--HDVVILDNL----CNSKRSVLPVIERLggkhpTFVEGDIRNEALLTEilHDHAIDTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    80 IHTAAVIDVtGVIPRQTI--LDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSykKIvlnGHEEQNHESTWSDPYPY 157
Cdd:PRK10675  78 IHFAGLKAV-GESVQKPLeyYDNNVNGTLRLISAMRAANVKNLIFSSSATVYGDQP--KI---PYVESFPTGTPQSPYGK 151

                 ....*..
gi 6680289   158 SKKMAEK 164
Cdd:PRK10675 152 SKLMVEQ 158
PRK05865 PRK05865
sugar epimerase family protein;
8-130 4.32e-06

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 48.89  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQEKelQEVRALDKvFRPETkeefsklqTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVid 87
Cdd:PRK05865   5 VTGASGVLGRGLTARLLSQG--HEVVGIAR-HRPDS--------WPSSADFIAADIRDATAVESAMTGADVVAHCAWV-- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6680289    88 vtgvipRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAG 130
Cdd:PRK05865  72 ------RGRNDHINIDGTANVLKAMAETGTGRIVFTSSGHQPR 108
PLN02989 PLN02989
cinnamyl-alcohol dehydrogenase family protein
8-165 6.29e-06

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178569 [Multi-domain]  Cd Length: 325  Bit Score: 47.72  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVqekeLQEVRALDKVFRPETKEEFSKL----QTKTKVTVLEGDILDAQCLRRACQGISVVIHTA 83
Cdd:PLN02989  10 VTGASGYIASWIVKLLL----FRGYTINATVRDPKDRKKTDHLlaldGAKERLKLFKADLLDEGSFELAIDGCETVFHTA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    84 AVIDVT-GVIPRQTILDVNLKGTQNLLEACVQ-ASVPAFIFCSSV-DVAGPNSYKkivlnGHEEQNHESTWSDP------ 154
Cdd:PLN02989  86 SPVAITvKTDPQVELINPAVNGTINVLRTCTKvSSVKRVILTSSMaAVLAPETKL-----GPNDVVDETFFTNPsfaeer 160
                        170
                 ....*....|....
gi 6680289   155 ---YPYSKKMAEKA 165
Cdd:PLN02989 161 kqwYVLSKTLAEDA 174
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
7-237 7.21e-06

Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 47.40  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDKvFRPETKEEFSKLQTK------TKVTVLEGDILDAQCLRRACQGISVVI 80
Cdd:PRK15181  19 LITGVAGFIGSGLLEELLFLN--QTVIGLDN-FSTGYQHNLDDVRTSvseeqwSRFIFIQGDIRKFTDCQKACKNVDYVL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    81 HTAAVidvtGVIPRQ-----TILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPN-SYKKIvlnghEEQNHESTwsDP 154
Cdd:PRK15181  96 HQAAL----GSVPRSlkdpiATNSANIDGFLNMLTAARDAHVSSFTYAASSSTYGDHpDLPKI-----EERIGRPL--SP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   155 YPYSKKMAEkavLAANgsMLKNGGTLNTCALRPMYIYGER-------SPFIFNAIIRALKNKGILcVTGKFSIANP-VYV 226
Cdd:PRK15181 165 YAVTKYVNE---LYAD--VFARSYEFNAIGLRYFNVFGRRqnpngaySAVIPRWILSLLKDEPIY-INGDGSTSRDfCYI 238
                        250
                 ....*....|.
gi 6680289   227 ENVAWAHILAA 237
Cdd:PRK15181 239 ENVIQANLLSA 249
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
7-125 8.05e-06

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. 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: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 46.08  E-value: 8.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKmlvqeKELQ---EVRALdkVFRPETKEEFSKlqtktKVTVLEGDILDAQCLRRACQGISvvihta 83
Cdd:cd05244   3 AIIGATGRTGSAIVR-----EALArghEVTAL--VRDPAKLPAEHE-----KLKVVQGDVLDLEDVKEALEGQD------ 64
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680289   84 AVIDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSS 125
Cdd:cd05244  65 AVISALGTRNDLSPTTLHSEGTRNIVSAMKAAGVKRLIVVGG 106
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
8-165 1.39e-05

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 46.63  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     8 VTGAGGFVGQRIIKMLVQE--------------KELQEVRALDKvfrpetkeefsklqTKTKVTVLEGDILDAQCLRRAC 73
Cdd:PLN02662   9 VTGASGYIASWLVKLLLQRgytvkatvrdpndpKKTEHLLALDG--------------AKERLHLFKANLLEEGSFDSVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    74 QGISVVIHTAA--VIDVTGviPRQTILDVNLKGTQNLLEACVQA-SVPAFIFCSSVdvagpnsyKKIVLNG----HEEQN 146
Cdd:PLN02662  75 DGCEGVFHTASpfYHDVTD--PQAELIDPAVKGTLNVLRSCAKVpSVKRVVVTSSM--------AAVAYNGkpltPDVVV 144
                        170       180
                 ....*....|....*....|....*...
gi 6680289   147 HESTWSDP---------YPYSKKMAEKA 165
Cdd:PLN02662 145 DETWFSDPafceesklwYVLSKTLAEEA 172
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
8-237 1.72e-05

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 46.19  E-value: 1.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    8 VTGAGGFVGQRIIKMLVQEKelQEVRALDKvfrpetKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVID 87
Cdd:cd05262   5 VTGATGFIGSAVVRELVAAG--HEVVGLAR------SDAGAAKLEAAGAQVHRGDLEDLDILRKAAAEADAVIHLAFTHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   88 VTgviPRQTILDVNLKGTQNLLEACVQASVPaFIFCSSVDVAGPnsykkivlNGHEEQNHESTWSDPYPYSKKMAEKAVL 167
Cdd:cd05262  77 FD---NFAQACEVDRRAIEALGEALRGTGKP-LIYTSGIWLLGP--------TGGQEEDEEAPDDPPTPAARAVSEAAAL 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680289  168 AANGSmlkngGTLNTCALRPMYIYGERSPFIFNAIIRALKNKGILCVTGKFSIANP-VYVENVAWAHILAA 237
Cdd:cd05262 145 ELAER-----GVRASVVRLPPVVHGRGDHGFVPMLIAIAREKGVSAYVGDGKNRWPaVHRDDAARLYRLAL 210
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
6-261 1.76e-05

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site 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. 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: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 45.77  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    6 CLVTGAGgFVGQRIIKMLVQEKelQEVRALdkVFRPETKEEFSKLQtktkVTVLEGDILDAQCLRRACqgiSVVIHTAAv 85
Cdd:cd05266   1 VLILGCG-YLGQRLARQLLAQG--WQVTGT--TRSPEKLAADRPAG----VTPLAADLTQPGLLADVD---HLVISLPP- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   86 idvtgviPRQTILDVNLKGTQNLLEACVQASVPA-FIFCSSVDVAGpnsykkivlngheeqNHESTW----SDPYPYSKK 160
Cdd:cd05266  68 -------PAGSYRGGYDPGLRALLDALAQLPAVQrVIYLSSTGVYG---------------DQQGEWvdetSPPNPSTES 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289  161 maEKAVLAANgSMLKNGGTLNTCALRPMYIYG-ERSPfifnaIIRALKNKGILCVTGKFSiaNPVYVENVAWAhILAARG 239
Cdd:cd05266 126 --GRALLEAE-QALLALGSKPTTILRLAGIYGpGRHP-----LRRLAQGTGRPPAGNAPT--NRIHVDDLVGA-LAFALQ 194
                       250       260
                ....*....|....*....|..
gi 6680289  240 LRDPkkstsiqGQFYYISDDTP 261
Cdd:cd05266 195 RPAP-------GPVYNVVDDLP 209
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
7-135 2.46e-05

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


Pssm-ID: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 45.77  E-value: 2.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKtkvtvlegDILDAQCLRRACQ--GISVVIHTAA 84
Cdd:cd05272   3 LITGGLGQIGSELAKLLRKRYGKDNVIASDIRKPPAHVVLSGPFEYL--------DVLDFKSLEEIVVnhKITWIIHLAA 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6680289   85 VIDVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIfCSSVDVAGPNSYK 135
Cdd:cd05272  75 LLSAVGEKNPPLAWDVNMNGLHNVLELAREHNLRIFV-PSTIGAFGPTTPR 124
PLN02214 PLN02214
cinnamoyl-CoA reductase
2-165 2.50e-05

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 45.90  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     2 AGWSCLVTGAGGFVGQRIIKMLVQEKELQE--VRALDKvfrPETKEEFSKLQTKTKVTVLEGDILDAQCLRRACQGISVV 79
Cdd:PLN02214   9 AGKTVCVTGAGGYIASWIVKILLERGYTVKgtVRNPDD---PKNTHLRELEGGKERLILCKADLQDYEALKAAIDGCDGV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    80 IHTAAVIDVTgviPRQtILDVNLKGTQNLLEACVQASVPAFIFCSSVDVA--GPNSYKKIVLNgheeqnhESTWSDP--- 154
Cdd:PLN02214  86 FHTASPVTDD---PEQ-MVEPAVNGAKFVINAAAEAKVKRVVITSSIGAVymDPNRDPEAVVD-------ESCWSDLdfc 154
                        170
                 ....*....|....*..
gi 6680289   155 ------YPYSKKMAEKA 165
Cdd:PLN02214 155 kntknwYCYGKMVAEQA 171
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
7-168 6.08e-05

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 45.12  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     7 LVTGAGGFVGQRIIKMLVQEKELQEVRALDKVFRPETKEEFSKLQTKTKVTVLEGDILDAQC---LRRAcQGISVVIHTA 83
Cdd:PLN02260  10 LITGAAGFIASHVANRLIRNYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASADLvnyLLIT-EGIDTIMHFA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    84 AvidvtgviprQTILD-----------VNLKGTQNLLEAC-VQASVPAFIFCSSVDVAGPNSYKKIVlngheeQNHESTW 151
Cdd:PLN02260  89 A----------QTHVDnsfgnsfeftkNNIYGTHVLLEACkVTGQIRRFIHVSTDEVYGETDEDADV------GNHEASQ 152
                        170       180
                 ....*....|....*....|
gi 6680289   152 ---SDPYPYSKKMAEKAVLA 168
Cdd:PLN02260 153 llpTNPYSATKAGAEMLVMA 172
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
7-133 7.06e-05

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 44.18  E-value: 7.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALdkVFRPETKEEFSKLqtktKVTVLEGDILDAQCLRRACQGISVV--IHTAA 84
Cdd:cd05269   2 LVTGATGKLGTAVVELLLAKVA--SVVAL--VRNPEKAKAFAAD----GVEVRQGDYDDPETLERAFEGVDRLllISPSD 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6680289   85 VIDVtgviprqtildvnLKGTQNLLEACVQASVpAFIFCSSVDVAGPNS 133
Cdd:cd05269  74 LEDR-------------IQQHKNFIDAAKQAGV-KHIVYLSASGADEDS 108
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
7-133 1.29e-04

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. 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: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 43.06  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELqEVRALdkvFRPETKEefSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAvi 86
Cdd:cd05259   3 AIAGATGTLGGPIVSALLASPGF-TVTVL---TRPSSTS--SNEFQPSGVKVVPVDYASHESLVAALKGVDAVISALG-- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6680289   87 dvTGVIPRQTildvnlkgtqNLLEACVQASVPAFI---FCSSVDVAGPNS 133
Cdd:cd05259  75 --GAAIGDQL----------KLIDAAIAAGVKRFIpseFGVDYDRIGALP 112
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
7-197 2.57e-04

GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, 5-epimerase-4-reductase) acts in the NADP-dependent synthesis of GDP-fucose from GDP-mannose. Two activities have been proposed for the same active site: epimerization and reduction. Proteins in this subgroup are extended SDRs, which have a characteristic active site tetrad and an NADP-binding motif, [AT]GXXGXXG, that is a close match to the archetypical form. 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: 187550 [Multi-domain]  Cd Length: 300  Bit Score: 42.57  E-value: 2.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLvqekelqEVRALDKVFRPETKEEfsklqtktkvtvlegDILDAQCLRRAC--QGISVVIHTAA 84
Cdd:cd05239   3 LVTGHRGLVGSAIVRVL-------ARRGYENVVFRTSKEL---------------DLTDQEAVRAFFekEKPDYVIHLAA 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VidVTGVI-----PRQTILDvNLKGTQNLLEACVQASVPAFIFCSSV-----DVAGP--NSYkkiVLNGHEEQNHEstws 152
Cdd:cd05239  61 K--VGGIVanmtyPADFLRD-NLLINDNVIHAAHRFGVKKLVFLGSSciypdLAPQPidESD---LLTGPPEPTNE---- 130
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6680289  153 dPYPYSKKMAEKAVLAANgsmlKNGGTLNTCALrPMYIYGERSPF 197
Cdd:cd05239 131 -GYAIAKRAGLKLCEAYR----KQYGCDYISVM-PTNLYGPHDNF 169
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
7-137 2.60e-04

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. 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: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 42.32  E-value: 2.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVqeKELQEVRALDKvfRPetkeefSKLQTKTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:cd05229   3 HVLGASGPIGREVARELR--RRGWDVRLVSR--SG------SKLAWLPGVEIVAADAMDASSVIAAARGADVIYHCANPA 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6680289   87 D---VTGVIPRQtildvnlkgtQNLLEACvQASVPAFIFCSSVDVAGPNSYKKI 137
Cdd:cd05229  73 YtrwEELFPPLM----------ENVVAAA-EANGAKLVLPGNVYMYGPQAGSPI 115
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
7-127 6.50e-04

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. 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. Atypical SDRs are distinct from classical SDRs. 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: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 40.72  E-value: 6.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKELQeVRALDkvfRPETKEEFSKLQTKtKVTVLEGDILDAQCLRRACQGISVVIH-TAAV 85
Cdd:cd05251   2 LVFGATGKQGGSVVRALLKDPGFK-VRALT---RDPSSPAAKALAAP-GVEVVQGDLDDPESLEAALKGVYGVFLvTDFW 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680289   86 IDVTGVIPRQTIldvnlkgtqNLLEACVQASVPAFIFcSSVD 127
Cdd:cd05251  77 EAGGEDEIAQGK---------NVVDAAKRAGVQHFVF-SSVP 108
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
7-118 1.03e-03

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


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 40.43  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKElqEVRALdkVFRPETKEEfsklqtktKVTVLEGDILDAQCLRRACQGISVVIH----- 81
Cdd:COG1090   3 LITGGTGFIGSALVAALLARGH--EVVVL--TRRPPKAPD--------EVTYVAWDPETGGIDAAALEGADAVINlagas 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6680289   82 ------TAAVidvtgvipRQTILDVNLKGTQNLLEACVQASVP 118
Cdd:COG1090  71 iadkrwTEAR--------KQEILDSRVDSTRLLVEAIAAAANP 105
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
7-126 1.12e-03

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 40.02  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKelQEVRALdkvFRPETKEEFSKLQTKtKVTVLEGDILDAQCLRRACQGISVvihtaaVI 86
Cdd:pfam05368   2 LVFGATGQQGGSVVRASLKAG--HKVRAL---VRDPKSELAKSLKEA-GVELVKGDLDDKESLVEALKGVDV------VF 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 6680289     87 DVTGVIPRQTILDvnlkGTqNLLEACVQASVPAFIFcSSV 126
Cdd:pfam05368  70 SVTGFWAGKEIED----GK-KLADAAKEAGVKHFIP-SSF 103
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
7-170 1.46e-03

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: 39.92  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEKelQEVRALDKvfrpeTKEEFSKLqtktkvtvlegDILDAQCLRRACQGIS--VVIHTAA 84
Cdd:cd05254   3 LITGATGMLGRALVRLLKERG--YEVIGTGR-----SRASLFKL-----------DLTDPDAVEEAIRDYKpdVIINCAA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289   85 VIDVTGV--IPRQTILdVNLKGTQNLLEACVQASVPaFIFCSSvdvagpnSYkkiVLNGHEEQNHESTWSDP---YPYSK 159
Cdd:cd05254  65 YTRVDKCesDPELAYR-VNVLAPENLARAAKEVGAR-LIHIST-------DY---VFDGKKGPYKEEDAPNPlnvYGKSK 132
                       170
                ....*....|.
gi 6680289  160 KMAEKAVLAAN 170
Cdd:cd05254 133 LLGEVAVLNAN 143
PLN02583 PLN02583
cinnamoyl-CoA reductase
5-168 1.71e-03

cinnamoyl-CoA reductase


Pssm-ID: 178195 [Multi-domain]  Cd Length: 297  Bit Score: 39.70  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     5 SCLVTGAGGFVGQRIIKMLVQekelqevR------ALDKVFRPETKEEFSKLQTKT-KVTVLEGDILDAQCLRRACQGIS 77
Cdd:PLN02583   8 SVCVMDASGYVGFWLVKRLLS-------RgytvhaAVQKNGETEIEKEIRGLSCEEeRLKVFDVDPLDYHSILDALKGCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    78 VVIHTAAVIDVTGVIPRQTIlDVNLKGTQNLLEACVQA-SVPAFIFCSSVDVA---GPNsykkivlNGHEEQNHESTWSD 153
Cdd:PLN02583  81 GLFCCFDPPSDYPSYDEKMV-DVEVRAAHNVLEACAQTdTIEKVVFTSSLTAViwrDDN-------ISTQKDVDERSWSD 152
                        170       180
                 ....*....|....*....|....
gi 6680289   154 P---------YPYSKKMAEKAVLA 168
Cdd:PLN02583 153 QnfcrkfklwHALAKTLSEKTAWA 176
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
7-170 1.94e-03

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


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 39.56  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      7 LVTGAGGFVGQRIIKMLVQEKElqEVRALDKVfrpetkeefsklqtktkvtvlEGDILDAQCLRRACQGI--SVVIHTAA 84
Cdd:pfam04321   2 LITGANGQLGTELRRLLAERGI--EVVALTRA---------------------ELDLTDPEAVARLLREIkpDVVVNAAA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     85 VIDVTGV-IPRQTILDVNLKGTQNLLEACVQASVPaFIFCSS---VDVAGPNSYkkivlngheeqnHESTWSDP---YPY 157
Cdd:pfam04321  59 YTAVDKAeSEPDLAYAINALAPANLAEACAAVGAP-LIHISTdyvFDGTKPRPY------------EEDDETNPlnvYGR 125
                         170
                  ....*....|...
gi 6680289    158 SKKMAEKAVLAAN 170
Cdd:pfam04321 126 TKLAGEQAVRAAG 138
SDR_a6 cd05267
atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only ...
7-131 2.17e-03

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. 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: 187577 [Multi-domain]  Cd Length: 203  Bit Score: 38.88  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289    7 LVTGAGGFVGQRIIKMLVQEkelQEVRaLDKVFRPETKeeFSKLQTkTKVTVLEGDILDAQCLRRACQGISVVIHTAAVI 86
Cdd:cd05267   4 LILGANGEIAREATTMLLEN---SNVE-LTLFLRNAHR--LLHLKS-ARVTVVEGDALNSDDLKAAMRGQDVVYANLGGT 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6680289   87 DVTgviprqtildvnlKGTQNLLEACVQASVPAFIFCSSV----DVAGP 131
Cdd:cd05267  77 DLD-------------QQAENVVQAMKAVGVKRLIWTTSLgiydEVPGK 112
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
7-192 2.49e-03

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: 40.05  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289       7 LVTGAGGFVGQRIIKMLVQEKELQE------VRA------LDKVFRPET-----KEEFSKlqtktKVTVLEGDI------ 63
Cdd:TIGR03443  975 FLTGATGFLGSFILRDLLTRRSNSNfkvfahVRAkseeagLERLRKTGTtygiwDEEWAS-----RIEVVLGDLskekfg 1049
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289      64 LDAQCLRRACQGISVVIHTAAVidVTGVIPRQTILDVNLKGTQNLLEACVQASVPAFIFCSSVDVAGPNSY----KKIV- 138
Cdd:TIGR03443 1050 LSDEKWSDLTNEVDVIIHNGAL--VHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYYvnlsDELVq 1127
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680289     139 --LNGHEE----QNHESTWSDPYPYSKKMAEKAVLAANgsmlKNGgtLNTCALRPMYIYG 192
Cdd:TIGR03443 1128 agGAGIPEsddlMGSSKGLGTGYGQSKWVAEYIIREAG----KRG--LRGCIVRPGYVTG 1181
 
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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