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Conserved domains on  [gi|162461808|ref|NP_001104806|]
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NADPH-dependent 3-keto-steroid reductase Hsd3b4 [Mus musculus]

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 7.29e-172

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: 451247 [Multi-domain]  Cd Length: 354  Bit Score: 482.78  E-value: 7.29e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   5 SCLVTGAGGFLGQRIVRMLVQEEE-LQEIRALFRTFGRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  84 AAIDPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEEHHESTWSNPYPYSKKMAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 164 KAVLAANGSILKNGGTLHTCALRLSFIYGEECQVTSTTVKTALKNNSIIKKNATFSIANP-VYVGNAAWAHILAARSLQD 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 243 PKKspSIQGQFYYITDDTPHQSYDDLKCTLSKEWGLRLDTSW-SLPLPLLYWLAFLLETVSFLLRPVYNYRPPFNRLLIT 321
Cdd:cd09811  241 PDK--AIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSWwYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 162461808 322 VLNSVFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 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 7.29e-172

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: 482.78  E-value: 7.29e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   5 SCLVTGAGGFLGQRIVRMLVQEEE-LQEIRALFRTFGRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  84 AAIDPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEEHHESTWSNPYPYSKKMAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 164 KAVLAANGSILKNGGTLHTCALRLSFIYGEECQVTSTTVKTALKNNSIIKKNATFSIANP-VYVGNAAWAHILAARSLQD 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 243 PKKspSIQGQFYYITDDTPHQSYDDLKCTLSKEWGLRLDTSW-SLPLPLLYWLAFLLETVSFLLRPVYNYRPPFNRLLIT 321
Cdd:cd09811  241 PDK--AIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSWwYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 162461808 322 VLNSVFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 3.12e-128

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerisation 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: 369.39  E-value: 3.12e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFRTFGRKQEEELSKLQTKTkvtVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNVIK---YIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   87 DPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEEHHESTWSNPYPYSKKMAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  167 LAANGSILKNGGTLHTCALRLSFIYGEECQVTSTTVKTALKNNSIIKKNATFS-IANPVYVGNAAWAHILAARSLQDPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKFKTGDDNnLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 162461808  246 SPSIQGQFYYITDDTPHQSYDDLKCTLSKEWGLRLDtSWSLPL 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLP-SISLPL 279
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-359 4.46e-33

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


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 125.44  E-value: 4.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFRTFGRKQEEElsklqtkTKVTVLKGDILDAQCLKRACQGMS-AVIHTAAA 85
Cdd:COG0451    4 LVTGGAGFIGSHLVERLLAAGH--DVRGLDRLRDGLDPLL-------SGVEFVVLDLTDRDLVDELAKGVPdAVIHLAAQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGAASRQ--TILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIIlnahEEEHHESTWSNPYPYSKKMAE 163
Cdd:COG0451   75 SSVPDSNASDpaEFLDVNVDGTLNLLEAARAAGVKRFVFASSVSVVYGDPPPLPI----DEDLGPPRPLNPYGVSKLAAE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 164 KAVLAANgsilkNGGTLHTCALRLSFIYGEECQ------VTSTTVKTALKNNSII----KKNATFSIanpVYVGNAAWAH 233
Cdd:COG0451  151 QLLRAYA-----RLYGLPVVILRPFNVYGPGDKpdlssgVVSAFIRQLLKGEPIIviggDGSQTRDF---VYVDDVADAL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 234 ILAARSLQDPkkspsiqgqFYYITDDTPHQSYDDLKCTLSKEWGlrldtswsLPLPLLYWLAflletvsflLRPVYNYRP 313
Cdd:COG0451  223 LLALENPDGG---------VFNIGSGTAEITVRELAEAVAEAVG--------SKAPLIVYIP---------LGRRGDLRE 276
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 162461808 314 PfnrllitvlnsvFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWIGT 359
Cdd:COG0451  277 G------------KLLDISKARAALGWEPKVSLEEGLADTLEWLLK 310
PLN02214 PLN02214
cinnamoyl-CoA reductase
3-165 2.32e-09

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 58.23  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   3 GWSCLVTGAGGFLGQRIVRMLVqeEELQEIRALFRTFGRKQEEELSKLQT-KTKVTVLKGDILDAQCLKRACQGMSAVIH 81
Cdd:PLN02214  10 GKTVCVTGAGGYIASWIVKILL--ERGYTVKGTVRNPDDPKNTHLRELEGgKERLILCKADLQDYEALKAAIDGCDGVFH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  82 TAAAI--DPlgaasrQTILDVNLKGTQLLLDACVEANVPTFIYSSSV--LVAGPNSYKEIILNaheeehhESTWS----- 152
Cdd:PLN02214  88 TASPVtdDP------EQMVEPAVNGAKFVINAAAEAKVKRVVITSSIgaVYMDPNRDPEAVVD-------ESCWSdldfc 154
                        170
                 ....*....|....*..
gi 162461808 153 ----NPYPYSKKMAEKA 165
Cdd:PLN02214 155 kntkNWYCYGKMVAEQA 171
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-170 2.78e-07

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: 51.65  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLV----------------QEEELQEIRALFRTFGRKQEEELSKlqtktKVTVLKGDI------L 64
Cdd:TIGR01746   3 LLTGATGFLGAYLLEELLrrstrakviclvradsEEHAMERLREALRSYRLWHENLAME-----RIEVVAGDLskprlgL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   65 DAQCLKRACQGMSAVIHTAAAIDPLGaaSRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEE 144
Cdd:TIGR01746  78 SDAEWERLAENVDTIVHNGALVNHVY--PYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVTEDDAT 155
                         170       180
                  ....*....|....*....|....*.
gi 162461808  145 EHHESTWSNPYPYSKKMAEKAVLAAN 170
Cdd:TIGR01746 156 VTPYPGLAGGYTQSKWVAELLVREAS 181
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-126 6.45e-05

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: 43.24  E-value: 6.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808     7 LVTGAGGFLGQRIVRMLVQ---------------EEELQEIRALFRTFGRkqeeelsklqtktKVTVLKGDILDAQCLKR 71
Cdd:smart00822   4 LITGGLGGLGRALARWLAErgarrlvllsrsgpdAPGAAALLAELEAAGA-------------RVTVVACDVADRDALAA 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162461808    72 ACQGMSA-------VIHTAAAID--PLGAASRQTILDVN---LKGTQLLLDACVEANVPTFIYSSSV 126
Cdd:smart00822  71 VLAAIPAvegpltgVIHAAGVLDdgVLASLTPERFAAVLapkAAGAWNLHELTADLPLDFFVLFSSI 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 7.29e-172

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: 482.78  E-value: 7.29e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   5 SCLVTGAGGFLGQRIVRMLVQEEE-LQEIRALFRTFGRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  84 AAIDPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEEHHESTWSNPYPYSKKMAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 164 KAVLAANGSILKNGGTLHTCALRLSFIYGEECQVTSTTVKTALKNNSIIKKNATFSIANP-VYVGNAAWAHILAARSLQD 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 243 PKKspSIQGQFYYITDDTPHQSYDDLKCTLSKEWGLRLDTSW-SLPLPLLYWLAFLLETVSFLLRPVYNYRPPFNRLLIT 321
Cdd:cd09811  241 PDK--AIRGQFYFISDDTPHNSYSDFNYELLKELGLRLKTSWwYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 162461808 322 VLNSVFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 3.12e-128

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerisation 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: 369.39  E-value: 3.12e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFRTFGRKQEEELSKLQTKTkvtVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNVIK---YIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   87 DPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEEHHESTWSNPYPYSKKMAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  167 LAANGSILKNGGTLHTCALRLSFIYGEECQVTSTTVKTALKNNSIIKKNATFS-IANPVYVGNAAWAHILAARSLQDPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKFKTGDDNnLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 162461808  246 SPSIQGQFYYITDDTPHQSYDDLKCTLSKEWGLRLDtSWSLPL 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 8.42e-99

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: 296.26  E-value: 8.42e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   5 SCLVTGAGGFLGQRIVRMLVqEEELQEIRALFRTFgrkQEEELSKlQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAA 84
Cdd:cd05241    1 SVLVTGGSGFFGERLVKQLL-ERGGTYVRSFDIAP---PGEALSA-WQHPNIEFLKGDITDRNDVEQALSGADCVFHTAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  85 AIDPLGaaSRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPnsyKEIILNAHEEEHHESTWSNPYPYSKKMAEK 164
Cdd:cd05241   76 IVPLAG--PRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFG---GQNIHNGDETLPYPPLDSDMYAETKAIAEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 165 AVLAANGSilkngGTLHTCALRLSFIYGEECQ-VTSTTVKTALKNNSII---KKNATFsiaNPVYVGNAAWAHILAARSL 240
Cdd:cd05241  151 IVLEANGR-----DDLLTCALRPAGIFGPGDQgLVPILFEWAEKGLVKFvfgRGNNLV---DFTYVHNLAHAHILAAAAL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 241 QDPKKspsIQGQFYYITDDTPHQSYDDLkCTLSKEWGLRLDTSWSLPLPLLYWLAFLLETVSFLLRPVYNYRPPFNRLLI 320
Cdd:cd05241  223 VKGKT---ISGQTYFITDAEPHNMFELL-RPVWKALGFGSRPKIRLSGPLAYCAALLSELVSFMLGPYFVFSPFYVRALV 298
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 162461808 321 TVlnsvFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd05241  299 TP----MYFSIAKAQKDLGYAPRYSNEEGLIETLNWY 331
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
5-357 8.32e-57

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: 188.34  E-value: 8.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   5 SCLVTGAGGFLGQRIVRMLVQEEELQeiralFRTFGRKQEEELSKlQTKTKVTVLKGDILDAQCLKRA--CQGMSAVIHT 82
Cdd:cd09813    1 SCLVVGGSGFLGRHLVEQLLRRGNPT-----VHVFDIRPTFELDP-SSSGRVQFHTGDLTDPQDLEKAfnEKGPNVVFHT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  83 AAaidPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSvlvAGPNSYKEIILNAHEEEHHESTWSNPYPYSKKMA 162
Cdd:cd09813   75 AS---PDHGSNDDLYYKVNVQGTRNVIEACRKCGVKKLVYTSS---ASVVFNGQDIINGDESLPYPDKHQDAYNETKALA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 163 EKAVLAANGSILKnggtLHTCALRLSFIYGE-ECQVTSTTVKTAL--KNNSIIKKNAtfSIANPVYVGNAAWAHILAARS 239
Cdd:cd09813  149 EKLVLKANDPESG----LLTCALRPAGIFGPgDRQLVPGLLKAAKngKTKFQIGDGN--NLFDFTYVENVAHAHILAADA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 240 LQDPKKSPSIQGQFYYITDDTPHQSYDDLKcTLSKEWGLRLDTSWSLPLPLLYWLAFLLETVSFLLRPVynyrPPFNRLL 319
Cdd:cd09813  223 LLSSSHAETVAGEAFFITNDEPIYFWDFAR-AIWEGLGYERPPSIKLPRPVALYLASLLEWTCKVLGKE----PTFTPFR 297
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 162461808 320 ITVLNSVFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09813  298 VALLCSTRYFNIEKAKKRLGYTPVVTLEEGIERTLQWF 335
3b-HSD_like_1_SDR_e cd09812
3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An ...
5-342 1.48e-43

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: 153.81  E-value: 1.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   5 SCLVTGAGGFLGQRIVRMLVQEEE---LQEIRalfrtfgrKQEEELSKlqtktKVTVLKGDILDAQCLKRACQGMSAVIH 81
Cdd:cd09812    1 SVLITGGGGYFGFRLGCALAKSGVhviLFDIR--------RPQQELPE-----GIKFIQADVRDLSQLEKAVAGVDCVFH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  82 TAA-AIDPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVA--------GPNSYKEIILNAHEEEhhestws 152
Cdd:cd09812   68 IASyGMSGREQLNRELIEEINVRGTENIIQVCVRRRVPRLIYTSTFNVIfggqpirnGDESLPYLPLDLHVDH------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 153 npYPYSKKMAEKAVLAANGSILKN-GGTLHTCALRLSFIYGEECQVTSTTVKTALKNNSII-KKNATFSIANPVYVGNAA 230
Cdd:cd09812  141 --YSRTKSIAEQLVLKANNMPLPNnGGVLRTCALRPAGIYGPGEQRHLPRIVSYIEKGLFMfVYGDPKSLVEFVHVDNLV 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 231 WAHILAARSLQDPKKSPSiQGQFYYITDDTPHQSYDDLKCTLSkewGLRLDTSW-SLPLPLLYWLAFLLETVSFLLRPVY 309
Cdd:cd09812  219 QAHILAAEALTTAKGYIA-SGQAYFISDGRPVNNFEFFRPLVE---GLGYSFPSlRLPLSLVYFFAFLTEMVHFALGPIC 294
                        330       340       350
                 ....*....|....*....|....*....|...
gi 162461808 310 NYRPPFNRLLITVLNSVFTFSYKKAQRDLGYEP 342
Cdd:cd09812  295 NFQPLLTRTEVYKTGVTHYFSIEKARAELGYEP 327
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
7-357 2.73e-37

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: 136.65  E-value: 2.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFRtfgrkQEEELSKLQtKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:cd05228    2 LVTGATGFLGSNLVRALLAQGY--RVRALVR-----SGSDAVLLD-GLPVEVVEGDLTDAASLAAAMKGCDRVFHLAAFT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 DPlGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIilnahEE--EHHESTWSNPYPYSKKMAEK 164
Cdd:cd05228   74 SL-WAKDRKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRI-----DEttPWNERPFPNDYYRSKLLAEL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 165 AVLAAngsiLKNGgtLHTCALRLSFIYG--EECQVTSTTVKTALKNNSIIkknatFSI---ANPVYVGNAAWAHILAArs 239
Cdd:cd05228  148 EVLEA----AAEG--LDVVIVNPSAVFGpgDEGPTSTGLDVLDYLNGKLP-----AYPpggTSFVDVRDVAEGHIAAM-- 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 240 lqdpKKSPSiqGQFYYITDdtPHQSYDDLKCTLSKEWGLRLdTSWSLPLPLLYWLAFLLETVSFLLRpvynyRPP-FNRL 318
Cdd:cd05228  215 ----EKGRR--GERYILGG--ENLSFKQLFETLAEITGVKP-PRRTIPPWLLKAVAALSELKARLTG-----KPPlLTPR 280
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 162461808 319 LITVLNSVFTFSYKKAQRDLGYEPlVSWEEAKQKTSEWI 357
Cdd:cd05228  281 TARVLRRNYLYSSDKARRELGYSP-RPLEEALRDTLAWL 318
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-359 4.46e-33

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


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 125.44  E-value: 4.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFRTFGRKQEEElsklqtkTKVTVLKGDILDAQCLKRACQGMS-AVIHTAAA 85
Cdd:COG0451    4 LVTGGAGFIGSHLVERLLAAGH--DVRGLDRLRDGLDPLL-------SGVEFVVLDLTDRDLVDELAKGVPdAVIHLAAQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGAASRQ--TILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIIlnahEEEHHESTWSNPYPYSKKMAE 163
Cdd:COG0451   75 SSVPDSNASDpaEFLDVNVDGTLNLLEAARAAGVKRFVFASSVSVVYGDPPPLPI----DEDLGPPRPLNPYGVSKLAAE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 164 KAVLAANgsilkNGGTLHTCALRLSFIYGEECQ------VTSTTVKTALKNNSII----KKNATFSIanpVYVGNAAWAH 233
Cdd:COG0451  151 QLLRAYA-----RLYGLPVVILRPFNVYGPGDKpdlssgVVSAFIRQLLKGEPIIviggDGSQTRDF---VYVDDVADAL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 234 ILAARSLQDPkkspsiqgqFYYITDDTPHQSYDDLKCTLSKEWGlrldtswsLPLPLLYWLAflletvsflLRPVYNYRP 313
Cdd:COG0451  223 LLALENPDGG---------VFNIGSGTAEITVRELAEAVAEAVG--------SKAPLIVYIP---------LGRRGDLRE 276
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 162461808 314 PfnrllitvlnsvFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWIGT 359
Cdd:COG0451  277 G------------KLLDISKARAALGWEPKVSLEEGLADTLEWLLK 310
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-202 8.48e-22

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: 91.98  E-value: 8.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLvqeeelqeiralfrtfgrkqeeelskLQTKTKVTVLkgDILDAqclkracqgmsaVIHTAAA 85
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRL--------------------------LERGHEVVVI--DRLDV------------VVHLAAL 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 I-DPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEiilnahEEEHHESTWSNPYPYSKKMAEK 164
Cdd:cd08946   41 VgVPASWDNPDEDFETNVVGTLNLLEAARKAGVKRFVYASSASVYGSPEGLP------EEEETPPRPLSPYGVSKLAAEH 114
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 162461808 165 AVLAANgsilkNGGTLHTCALRLSFIYGEECQVTSTTV 202
Cdd:cd08946  115 LLRSYG-----ESYGLPVVILRLANVYGPGQRPRLDGV 147
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
7-193 5.05e-21

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: 90.82  E-value: 5.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQEEelQEIRALFRtfgrkqEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMS--AVIHTAA 84
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKG--YEVIGLDR------LTSASNTARLADLRFVEGDLTDRDALEKLLADVRpdAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   85 AID-PLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEEHHEstwSNPYPYSKKMAE 163
Cdd:pfam01370  74 VGGvGASIEDPEDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEETTLTGPLAP---NSPYAAAKLAGE 150
                         170       180       190
                  ....*....|....*....|....*....|
gi 162461808  164 KAVLAANGSilkngGTLHTCALRLSFIYGE 193
Cdd:pfam01370 151 WLVLAYAAA-----YGLRAVILRLFNVYGP 175
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
6-194 1.41e-19

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: 87.81  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLVQEEElqEIRALFR--TFGRKQEEELSKLQTKTKVTVLKGDI------LDAQCLKRACQGMS 77
Cdd:cd05263    1 VFVTGGTGFLGRHLVKRLLENGF--KVLVLVRseSLGEAHERIEEAGLEADRVRVLEGDLtqpnlgLSAAASRELAGKVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  78 AVIHTAAAIDPlgAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSykEIIlnaHEEEH-HESTWSNPYP 156
Cdd:cd05263   79 HVIHCAASYDF--QAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNRE--GNI---RETELnPGQNFKNPYE 151
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 162461808 157 YSKKMAEKAVLAAngsilknGGTLHTCALRLSFIYGEE 194
Cdd:cd05263  152 QSKAEAEQLVRAA-------ATQIPLTVYRPSIVVGDS 182
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
6-168 1.82e-19

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: 87.24  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLvqeeeLQE---IRALFRTFG-RKQEEELSKLQ-TKTKVTVLKGDILDAQCLKRACQGMSAVI 80
Cdd:cd08958    1 VCVTGASGFIGSWLVKRL-----LQRgytVRATVRDPGdEKKVAHLLELEgAKERLKLFKADLLDYGSFDAAIDGCDGVF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  81 HTAAAIDPLGAASRQTILDVNLKGTQLLLDACVEAN-VPTFIYSSSV--LVAGPNSYKEIILNaheeehhESTWSNP--- 154
Cdd:cd08958   76 HVASPVDFDSEDPEEEMIEPAVKGTLNVLEACAKAKsVKRVVFTSSVaaVVWNPNRGEGKVVD-------ESCWSDLdfc 148
                        170       180
                 ....*....|....*....|
gi 162461808 155 ------YPYSKKMAEKAVLA 168
Cdd:cd08958  149 kktklwYALSKTLAEKAAWE 168
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
6-357 9.87e-19

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: 85.35  E-value: 9.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLVqeEELQEIRAL--FRTFGRKQEEELsklqtKTKVTVLKGDILDAQCLKRACQGMSAVIHTA 83
Cdd:cd05256    2 VLVTGGAGFIGSHLVERLL--ERGHEVIVLdnLSTGKKENLPEV-----KPNVKFIEGDIRDDELVEFAFEGVDYVFHQA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  84 AAI-------DPLGAAsrqtilDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIilnaheEEHHESTWSNPYP 156
Cdd:cd05256   75 AQAsvprsieDPIKDH------EVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPK------DEDHPPNPLSPYA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 157 YSKKMAEKAVLAANGSIlknggTLHTCALRLSFIYG-------EECQVTSTTVKTALKNNSII-----KKNATFsianpV 224
Cdd:cd05256  143 VSKYAGELYCQVFARLY-----GLPTVSLRYFNVYGprqdpngGYAAVIPIFIERALKGEPPTiygdgEQTRDF-----T 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 225 YVGNAAWAHILAARSLQDpkkspsiqGQFYYITDDTPHQsyddlkctlskewglrldtswslplpLLYWLAFLLETVSFL 304
Cdd:cd05256  213 YVEDVVEANLLAATAGAG--------GEVYNIGTGKRTS--------------------------VNELAELIREILGKE 258
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 162461808 305 LRPVynYRPPF---NRLliTVLNSvftfsyKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd05256  259 LEPV--YAPPRpgdVRH--SLADI------SKAKKLLGWEPKVSFEEGLRLTVEWF 304
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-353 8.31e-17

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: 80.09  E-value: 8.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFRTFGRKQEeelsklqtktkvTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:cd05232    3 LVTGANGFIGRALVDKLLSRGE--EVRIAVRNAENAEP------------SVVLAELPDIDSFTDLFLGVDAVVHLAARV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 DPLGAASRQTILD---VNLKGTQLLLDACVEANVPTFIYSSSVLVAGpnsykEIILNAHEEEHHESTWSNPYPYSKKMAE 163
Cdd:cd05232   69 HVMNDQGADPLSDyrkVNTELTRRLARAAARQGVKRFVFLSSVKVNG-----EGTVGAPFDETDPPAPQDAYGRSKLEAE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 164 KAVLAAngsILKNGgtLHTCALRLSFIYGEECQVTSTTVKTALKNNSIIKKNATFSIANPVYVGNAAwahILAARSLQDP 243
Cdd:cd05232  144 RALLEL---GASDG--MEVVILRPPMVYGPGVRGNFARLMRLIDRGLPLPPGAVKNRRSLVSLDNLV---DAIYLCISLP 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 244 KKSpsiqGQFYYITDDTP---HQSYDDLKCTLSKEwglrldtSWSLPLPllywlAFLLETVSFLLrpvyNYRPPFNRLLi 320
Cdd:cd05232  216 KAA----NGTFLVSDGPPvstAELVDEIRRALGKP-------TRLLPVP-----AGLLRFAAKLL----GKRAVIQRLF- 274
                        330       340       350
                 ....*....|....*....|....*....|...
gi 162461808 321 tvlnSVFTFSYKKAQRDLGYEPLVSWEEAKQKT 353
Cdd:cd05232  275 ----GSLQYDPEKTQNELGWRPPISLEEGLQET 303
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
7-165 1.82e-15

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: 76.15  E-value: 1.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQE-----------EELQEIRALFRTFGRKQEEELSKLqtktkvtvlkGDILDAQCLKRACQG 75
Cdd:cd05227    3 LVTGATGFIASHIVEQLLKAgykvrgtvrslSKSAKLKALLKAAGYNDRLEFVIV----------DDLTAPNAWDEALKG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  76 MSAVIHTAAAIDPLGAASRQTILDVNLKGTQLLLDACVEA-NVPTFIYSSSVL-VAGPNSYKeiilnaHEEEHHESTWSN 153
Cdd:cd05227   73 VDYVIHVASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKAAgSVKRVVLTSSVAaVGDPTAED------PGKVFTEEDWND 146
                        170       180
                 ....*....|....*....|..
gi 162461808 154 ----------PYPYSKKMAEKA 165
Cdd:cd05227  147 ltisksngldAYIASKTLAEKA 168
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
7-223 4.29e-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: 73.04  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFRTfgRKQEEELSKLqtktKVTVLKGDILDAQCLKRACQGMSAVIHTAAAi 86
Cdd:cd05243    3 LVVGATGKVGRHVVRELLDRGY--QVRALVRD--PSQAEKLEAA----GAEVVVGDLTDAESLAAALEGIDAVISAAGS- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 dplGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEEehhestwsnpypysKKMAEKaV 166
Cdd:cd05243   74 ---GGKGGPRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLEALGPYLDA--------------KRKAED-Y 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162461808 167 LAANG---SILKNGG-TLHTCALRLSFIYGE-ECQVTS-------TTVKTALKNNSIIKKnaTFSIANP 223
Cdd:cd05243  136 LRASGldyTIVRPGGlTDDPAGTGRVVLGGDgTRLDGPisradvaEVLAEALDTPAAIGK--TFELGGG 202
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
7-131 6.60e-15

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: 74.33  E-value: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFRTFGRKQEEelsklqtktKVTVLKGDILDAQC-LKRACQGMSAVIHTAAA 85
Cdd:cd05240    2 LVTGAAGGLGRLLARRLAASPRVIGVDGLDRRRPPGSPP---------KVEYVRLDIRDPAAaDVFREREADAVVHLAFI 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 162461808  86 IDP--LGAASRQtildVNLKGTQLLLDACVEANVPTFIYSSSVLVAGP 131
Cdd:cd05240   73 LDPprDGAERHR----INVDGTQNVLDACAAAGVPRVVVTSSVAVYGA 116
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
6-317 4.41e-13

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: 68.81  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLVQEEelQEIRALFRtfGRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHtAAA 85
Cdd:cd05271    3 VTVFGATGFIGRYVVNRLAKRG--SQVIVPYR--CEAYARRLLVMGDLGQVLFVEFDLRDDESIRKALEGSDVVIN-LVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGaaSRQTILDVNLKGTQLLLDACVEANVPTFIYSSSvlvagpnsykeiiLNAheEEHHEStwsnPYPYSKKMAEKA 165
Cdd:cd05271   78 RLYET--KNFSFEDVHVEGPERLAKAAKEAGVERLIHISA-------------LGA--DANSPS----KYLRSKAEGEEA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 166 VLAA--NGSIlknggtlhtcaLRLSFIYGEE----CQVTSTTVKTALkNNSIIKKNATFsiaNPVYVGNAAWAhilAARS 239
Cdd:cd05271  137 VREAfpEATI-----------VRPSVVFGREdrflNRFAKLLAFLPF-PPLIGGGQTKF---QPVYVGDVAEA---IARA 198
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162461808 240 LQDpkksPSIQGQFYYITDdtPHQ-SYDDLkctlsKEWGLRLDTSWSLPLPLLYWLAFLLETVSFLLRPvynYRPPFNR 317
Cdd:cd05271  199 LKD----PETEGKTYELVG--PKVyTLAEL-----VELLRRLGGRKRRVLPLPLWLARLIARVKLLLLL---PEPPLTR 263
NAD_binding_10 pfam13460
NAD(P)H-binding;
10-166 1.79e-12

NAD(P)H-binding;


Pssm-ID: 433226 [Multi-domain]  Cd Length: 183  Bit Score: 65.32  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   10 GAGGFLGQRIVRMLVQEEelQEIRALFRtfgrkQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAaidpl 89
Cdd:pfam13460   1 GATGKIGRLLVKQLLARG--HEVTALVR-----NPEKLADLEDHPGVEVVDGDVLDPDDLAEALKGQDAVISALG----- 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162461808   90 GAASRQTildvnlkGTQLLLDACVEANVPTFIYSSSvlvAGpnsykeiILNAHEEEHHESTWSNPYPY--SKKMAEKAV 166
Cdd:pfam13460  69 GGGTDEE-------GAKNIIDAAKAAGVKRFILVSS---LG-------VGDEVPGPFGPWNKEMLGPYlaAKRAAEELL 130
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
7-196 5.51e-12

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: 65.87  E-value: 5.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIRALfrtfgRKQEEELSKlqTKTKVTVLKGDILDAQCLKRACQGMS-AVIHTAAA 85
Cdd:cd05238    4 LITGASGFVGQRLAERLLSDVPNERLILI-----DVVSPKAPS--GAPRVTQIAGDLAVPALIEALANGRPdVVFHLAAI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGAASRQTILDVNLKGTQLLLDACVEAN-VPTFIYSSSVLVAGPNSYKEIILNaheeEHHESTWSnpYPYSKKMAEk 164
Cdd:cd05238   77 VSGGAEADFDLGYRVNVDGTRNLLEALRKNGpKPRFVFTSSLAVYGLPLPNPVTDH----TALDPASS--YGAQKAMCE- 149
                        170       180       190
                 ....*....|....*....|....*....|..
gi 162461808 165 aVLAANGSilkNGGTLHTCALRLSFIYGEECQ 196
Cdd:cd05238  150 -LLLNDYS---RRGFVDGRTLRLPTVCVRPGR 177
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
8-193 5.79e-12

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: 400380 [Multi-domain]  Cd Length: 257  Bit Score: 64.94  E-value: 5.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    8 VTGAGGFLGQRIVR-MLVQEEELQEI----RA---------LFRTFGRKQEEELSKLQTKTKVTVLKGDI------LDAQ 67
Cdd:pfam07993   1 LTGATGFLGKVLLEkLLRSTPDVKKIyllvRAkdgesalerLRQELEKYPLFDALLKEALERIVPVAGDLsepnlgLSEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   68 CLKRACQGMSAVIHTAAAID---PLGAAsrqtiLDVNLKGTQLLLD-ACVEANVPTFIYSSSVLVAGPNSYK--EIILNA 141
Cdd:pfam07993  81 DFQRLAEEVDVIIHSAATVNfdePYDDA-----RAINVLGTREVLRlAKQGKQLKAFHHVSTAYVNGEREGLveEKPYPE 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  142 HEEEHHEST--------WSNPYPYSKKMAEKAVLAAngsilkNGGTLHTCALRLSFIYGE 193
Cdd:pfam07993 156 GEDDMKLDEdepallggLPNTYTQTKWLAEQLVREA------ARRGLPVVIYRPSIITGE 209
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
7-192 5.95e-12

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: 65.37  E-value: 5.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQ----------------EEELQEIRALFRTFGRKQ--EEELSKLQtktkvtVLKGDI----- 63
Cdd:cd05235    3 LLTGATGFLGAYLLRELLKrknvskiyclvrakdeEAALERLIDNLKEYGLNLwdELELSRIK------VVVGDLskpnl 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  64 -LDAQCLKRACQGMSAVIHTAAAIDPLGAASrqTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAH 142
Cdd:cd05235   77 gLSDDDYQELAEEVDVIIHNGANVNWVYPYE--ELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEES 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162461808 143 E-EEHHESTWSNPYPYSKKMAEKAVLAANgsilKNGgtLHTCALRLSFIYG 192
Cdd:cd05235  155 DdMLESQNGLPNGYIQSKWVAEKLLREAA----NRG--LPVAIIRPGNIFG 199
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
7-168 9.45e-12

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: 65.01  E-value: 9.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVqeEELQEIRAL-----FRTFGRKQEEELSKLQtktkvtVLKGDILDAQCLKRACQGMSAVIH 81
Cdd:cd05257    3 LVTGADGFIGSHLTERLL--REGHEVRALdiynsFNSWGLLDNAVHDRFH------FISGDVRDASEVEYLVKKCDVVFH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  82 TAAAID-PLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIilnahEEEHHESTWSNP-YPY-- 157
Cdd:cd05257   75 LAALIAiPYSYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPI-----DEDHPLLYINKPrSPYsa 149
                        170
                 ....*....|.
gi 162461808 158 SKKMAEKAVLA 168
Cdd:cd05257  150 SKQGADRLAYS 160
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
7-178 4.40e-11

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: 60.88  E-value: 4.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEelQEIRALFRtfgrkQEEELSKLQtKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAi 86
Cdd:cd05226    2 LILGATGFIGRALARELLEQG--HEVTLLVR-----NTKRLSKED-QEPVAVVEGDLRDLDSLSDAVQGVDVVIHLAGA- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 DPLGAASRQtildVNLKGTQLLLDACVEANVPTFIYSSSvlvagpnsykeiiLNAHEEEHHESTWSNPYPYSKKMA--EK 164
Cdd:cd05226   73 PRDTRDFCE----VDVEGTRNVLEAAKEAGVKHFIFISS-------------LGAYGDLHEETEPSPSSPYLAVKAktEA 135
                        170
                 ....*....|....*.
gi 162461808 165 AVLAANG--SILKNGG 178
Cdd:cd05226  136 VLREASLpyTIVRPGV 151
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
7-193 2.88e-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: 60.41  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEelQEIRAlfrtFGRKQEEElskLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:cd05264    3 LIVGGNGFIGSHLVDALLEEG--PQVRV----FDRSIPPY---ELPLGGVDYIKGDYENRADLESALVGIDTVIHLASTT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 DPlGAASRQTILDV--NLKGTQLLLDACVEANVPTFIYSSSvlvaGPNSYKEIILNAHEEEHHESTWSnPYPYSKKMAEK 164
Cdd:cd05264   74 NP-ATSNKNPILDIqtNVAPTVQLLEACAAAGIGKIIFASS----GGTVYGVPEQLPISESDPTLPIS-SYGISKLAIEK 147
                        170       180
                 ....*....|....*....|....*....
gi 162461808 165 AVLAANgsiLKNGgtLHTCALRLSFIYGE 193
Cdd:cd05264  148 YLRLYQ---YLYG--LDYTVLRISNPYGP 171
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
7-165 2.94e-10

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224012 [Multi-domain]  Cd Length: 329  Bit Score: 60.65  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLvqeeelqeiralfrtfgrkqeeelskLQTKTKVTVL-------------------KGDILDAQ 67
Cdd:COG1087    4 LVTGGAGYIGSHTVRQL--------------------------LKTGHEVVVLdnlsnghkiallklqfkfyEGDLLDRA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  68 CLKR--ACQGMSAVIHTAAAI-------DPLgaasrqTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEII 138
Cdd:COG1087   58 LLTAvfEENKIDAVVHFAASIsvgesvqNPL------KYYDNNVVGTLNLIEAMLQTGVKKFIFSSTAAVYGEPTTSPIS 131
                        170       180
                 ....*....|....*....|....*..
gi 162461808 139 lnaheEEHHESTwSNPYPYSKKMAEKA 165
Cdd:COG1087  132 -----ETSPLAP-INPYGRSKLMSEEI 152
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-164 3.00e-10

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


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 60.63  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIralFRTFGRKQEEELSKLQtKTKVTVLKGDILDAQCLKR--ACQGMSAVIHTAA 84
Cdd:cd05247    3 LVTGGAGYIGSHTVVELLEAGYDVVV---LDNLSNGHREALPRIE-KIRIEFYEGDIRDRAALDKvfAEHKIDAVIHFAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  85 AIDpLGAASRQTIL--DVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIilnahEEEHHESTwSNPYPYSKKMA 162
Cdd:cd05247   79 LKA-VGESVQKPLKyyDNNVVGTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVPI-----TEEAPLNP-TNPYGRTKLMV 151

                 ..
gi 162461808 163 EK 164
Cdd:cd05247  152 EQ 153
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
7-168 5.18e-10

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: 59.87  E-value: 5.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFR-TF-GRKqeEELSKLQTKTKVTVLKGDILDAQCLKRACQGMS--AVIHT 82
Cdd:cd05246    4 LVTGGAGFIGSNFVRYLLNKYPDYKIINLDKlTYaGNL--ENLEDVSSSPRYRFVKGDICDAELVDRLFEEEKidAVIHF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  83 AA------AIDplgaaSRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPnsykeiilNAHEEEHHESTW---SN 153
Cdd:cd05246   82 AAeshvdrSIS-----DPEPFIRTNVLGTYTLLEAARKYGVKRFVHISTDEVYGD--------LLDDGEFTETSPlapTS 148
                        170
                 ....*....|....*
gi 162461808 154 PYPYSKKMAEKAVLA 168
Cdd:cd05246  149 PYSASKAAADLLVRA 163
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
7-171 7.13e-10

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 225857 [Multi-domain]  Cd Length: 382  Bit Score: 59.71  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQ---------------EEELQEIRALFRTFGRKQEEELSklqtktKVTVLKGDI------LD 65
Cdd:COG3320    4 LLTGATGFLGAYLLLELLDrsdakviclvraqsdEAALARLEKTFDLYRHWDELSAD------RVEVVAGDLaepdlgLS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  66 AQCLKRACQGMSAVIHTAAAIDPLGAASRqtILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSY---KEIILNAH 142
Cdd:COG3320   78 ERTWQELAENVDLIIHNAALVNHVFPYSE--LRGANVLGTAEVLRLAATGKPKPLHYVSSISVGETEYYsnfTVDFDEIS 155
                        170       180
                 ....*....|....*....|....*....
gi 162461808 143 EEEHHESTWSNPYPYSKKMAEKAVLAANG 171
Cdd:COG3320  156 PTRNVGQGLAGGYGRSKWVAEKLVREAGD 184
PLN02214 PLN02214
cinnamoyl-CoA reductase
3-165 2.32e-09

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 58.23  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   3 GWSCLVTGAGGFLGQRIVRMLVqeEELQEIRALFRTFGRKQEEELSKLQT-KTKVTVLKGDILDAQCLKRACQGMSAVIH 81
Cdd:PLN02214  10 GKTVCVTGAGGYIASWIVKILL--ERGYTVKGTVRNPDDPKNTHLRELEGgKERLILCKADLQDYEALKAAIDGCDGVFH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  82 TAAAI--DPlgaasrQTILDVNLKGTQLLLDACVEANVPTFIYSSSV--LVAGPNSYKEIILNaheeehhESTWS----- 152
Cdd:PLN02214  88 TASPVtdDP------EQMVEPAVNGAKFVINAAAEAKVKRVVITSSIgaVYMDPNRDPEAVVD-------ESCWSdldfc 154
                        170
                 ....*....|....*..
gi 162461808 153 ----NPYPYSKKMAEKA 165
Cdd:PLN02214 155 kntkNWYCYGKMVAEQA 171
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
7-192 2.51e-09

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: 57.69  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIV-RMLVQEEELQEIRALFRtfGRKQEEELSKLQ-----------------TKTKVTVLKGDILDAQC 68
Cdd:cd05236    4 LITGATGFLGKVLLeKLLRSCPDIGKIYLLIR--GKSGQSAEERLRellkdklfdrgrnlnplFESKIVPIEGDLSEPNL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  69 ------LKRACQGMSAVIHTAAAID---PLGAAsrqtiLDVNLKGTQLLLDACVE-ANVPTFIYSSSVLVAGPNSYKE-- 136
Cdd:cd05236   82 glsdedLQTLIEEVNIIIHCAATVTfdeRLDEA-----LSINVLGTLRLLELAKRcKKLKAFVHVSTAYVNGDRQLIEek 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162461808 137 ---IILNAHEEEHHEST----------------WSNPYPYSKKMAEKAVlaangsiLKNGGTLHTCALRLSFIYG 192
Cdd:cd05236  157 vypPPADPEKLIDILELmddleleratpkllggHPNTYTFTKALAERLV-------LKERGNLPLVIVRPSIVGA 224
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
7-170 3.49e-09

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: 57.14  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQ------------EEELQEIRALFRtfgrkqeEELSKLQTKTKVTVLKGDILDAQCLKRACQ 74
Cdd:pfam02719   2 LVTGGGGSIGSELCRQILKfnpkkiilfsrdELKLYEIRQELR-------EKFNDPKLRFFIVPVIGDVRDRERLERAME 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   75 --GMSAVIHtAAAI--------DPLGAasrqtiLDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPnsykeiilnahee 144
Cdd:pfam02719  75 qyGVDVVFH-AAAYkhvplveyNPMEA------IKTNVLGTENVADAAIEAGVKKFVLISTDKAVNP------------- 134
                         170       180
                  ....*....|....*....|....*.
gi 162461808  145 ehhestwSNPYPYSKKMAEKAVLAAN 170
Cdd:pfam02719 135 -------TNVMGATKRLAEKLFQAAN 153
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
7-172 6.25e-09

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: 56.47  E-value: 6.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElQEIRAlfrtFGR---KQEE---ELSKLQTKTKVTVLKGDILDAQCLKRAC--QGMSA 78
Cdd:cd05237    6 LVTGGAGSIGSELVRQILKFGP-KKLIV----FDRdenKLHElvrELRSRFPHDKLRFIIGDVRDKERLRRAFkeRGPDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  79 VIHtAAAI--------DPLGAasrqtiLDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPnsykeiilnaheeehhest 150
Cdd:cd05237   81 VFH-AAALkhvpsmedNPEEA------IKTNVLGTKNVIDAAIENGVEKFVCISTDKAVNP------------------- 134
                        170       180
                 ....*....|....*....|..
gi 162461808 151 wSNPYPYSKKMAEKAVLAANGS 172
Cdd:cd05237  135 -VNVMGATKRVAEKLLLAKNEY 155
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
7-167 8.26e-09

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: 56.09  E-value: 8.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVqeEELQEIRALFRTfGRKQEEE--LSKLQTK-TKVTVLKGDILDAQCLKRACQGMSAVIHTA 83
Cdd:cd05193    2 LVTGASGFVASHVVEQLL--ERGYKVRATVRD-PSKVKKVnhLLDLDAKpGRLELAVADLTDEQSFDEVIKGCAGVFHVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  84 AAIDpLGAASRQTILDVNLKGTQLLLDACVEA-NVPTFIYSSSVLVAG-PNSYKEII--------LNAHEEEHHESTWSn 153
Cdd:cd05193   79 TPVS-FSSKDPNEVIKPAIGGTLNALKAAAAAkSVKRFVLTSSAGSVLiPKPNVEGIvldekswnLEEFDSDPKKSAWV- 156
                        170
                 ....*....|....
gi 162461808 154 pYPYSKKMAEKAVL 167
Cdd:cd05193  157 -YAASKTLAEKAAW 169
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
7-177 1.17e-08

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224011 [Multi-domain]  Cd Length: 588  Bit Score: 56.51  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQeeelQEIRALfRTFGR---KQ---EEELSKLQTKTKVTVLKGDILDAQCLKRACQGMS--A 78
Cdd:COG1086  254 LVTGGGGSIGSELCRQILK----FNPKEI-ILFSRdeyKLyliDMELREKFPELKLRFYIGDVRDRDRVERAMEGHKvdI 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  79 VIHtAAAIDPLGAASRQTILDV--NLKGTQLLLDACVEANVPTFIYSSSVLVAGPnsykeiilnaheeehhestwSNPYP 156
Cdd:COG1086  329 VFH-AAALKHVPLVEYNPEEAIktNVLGTENVAEAAIKNGVKKFVLISTDKAVNP--------------------TNVMG 387
                        170       180
                 ....*....|....*....|.
gi 162461808 157 YSKKMAEKAVLAANGSILKNG 177
Cdd:COG1086  388 ATKRLAEKLFQAANRNVSGTG 408
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
6-130 2.24e-08

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: 54.66  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLVQEEElqEIRALFRTfgrkqEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAV---IHT 82
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGH--QVRALVRS-----PEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAyylVHS 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 162461808  83 AAAIDPLGAASRQTILDVNlkgtqlllDACVEANVPTFIYSSSVLVAG 130
Cdd:cd05245   74 MGSGGDFEEADRRAARNFA--------RAARAAGVKRIIYLGGLIPKG 113
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
7-207 5.52e-08

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


Pssm-ID: 224016 [Multi-domain]  Cd Length: 281  Bit Score: 53.45  E-value: 5.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIralfrtfGRKQEeelsklqtktkvtvlkgDILDAQCLKRACQGMS--AVIHTAA 84
Cdd:COG1091    4 LITGANGQLGTELRRALPGEFEVIAT-------DRAEL-----------------DITDPDAVLEVIRETRpdVVINAAA 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  85 AIDPLGAAS-RQTILDVNLKGTQLLLDACVEANVPtFIYSSSVLV---AGPNSYKEiilnaheeeHHESTWSNPYPYSKK 160
Cdd:COG1091   60 YTAVDKAESePELAFAVNATGAENLARAAAEVGAR-LVHISTDYVfdgEKGGPYKE---------TDTPNPLNVYGRSKL 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162461808 161 MAEKAVLAANGsilknggtlHTCALRLSFIYGEEcqvTSTTVKTALK 207
Cdd:COG1091  130 AGEEAVRAAGP---------RHLILRTSWVYGEY---GNNFVKTMLR 164
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
7-135 5.57e-08

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: 53.83  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLV-QEEELQEIRALFRTFGRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAA- 84
Cdd:cd05258    4 LITGGAGFIGSNLARFFLkQGWEVIGFDNLMRRGSFGNLAWLKANREDGGVRFVHGDIRNRNDLEDLFEDIDLIIHTAAq 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162461808  85 -AIDpLGAASRQTILDVNLKGTQLLLDACVEANV-PTFIYSSSVLVAG--PNSYK 135
Cdd:cd05258   84 pSVT-TSASSPRLDFETNALGTLNVLEAARQHAPnAPFIFTSTNKVYGdlPNYLP 137
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
7-193 2.36e-07

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: 51.95  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqeiralfRTFG----------RKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGM 76
Cdd:cd05253    4 LVTGAAGFIGFHVAKRLLERGD--------EVVGidnlndyydvRLKEARLELLGKSGGFKFVKGDLEDREALRRLFKDH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  77 S--AVIHTAAAidplgAASRQTI------LDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIilnahEEEHHE 148
Cdd:cd05253   76 EfdAVIHLAAQ-----AGVRYSLenphayVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYGLNTKMPF-----SEDDRV 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 162461808 149 STWSNPYPYSKKMAEkaVLAANGSILKNggtLHTCALRLSFIYGE 193
Cdd:cd05253  146 DHPISLYAATKKANE--LMAHTYSHLYG---IPTTGLRFFTVYGP 185
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-170 2.78e-07

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: 51.65  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLV----------------QEEELQEIRALFRTFGRKQEEELSKlqtktKVTVLKGDI------L 64
Cdd:TIGR01746   3 LLTGATGFLGAYLLEELLrrstrakviclvradsEEHAMERLREALRSYRLWHENLAME-----RIEVVAGDLskprlgL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   65 DAQCLKRACQGMSAVIHTAAAIDPLGaaSRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGPNSYKEIILNAHEE 144
Cdd:TIGR01746  78 SDAEWERLAENVDTIVHNGALVNHVY--PYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVTEDDAT 155
                         170       180
                  ....*....|....*....|....*.
gi 162461808  145 EHHESTWSNPYPYSKKMAEKAVLAAN 170
Cdd:TIGR01746 156 VTPYPGLAGGYTQSKWVAELLVREAS 181
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
7-164 3.01e-07

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 51.74  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFRTFGRKQEEELSKLQTKTKvTVLKGDILDAQCLKR--ACQGMSAVIHTAA 84
Cdd:PRK10675   4 LVTGGSGYIGSHTCVQLLQNGHDVVILDNLCNSKRSVLPVIERLGGKHP-TFVEGDIRNEALLTEilHDHAIDTVIHFAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  85 aIDPLGAASRQTI--LDVNLKGTQLLLDACVEANVPTFIYSSSVLVAGpnsYKEIIlnAHEEEHHESTWSNPYPYSKKMA 162
Cdd:PRK10675  83 -LKAVGESVQKPLeyYDNNVNGTLRLISAMRAANVKNLIFSSSATVYG---DQPKI--PYVESFPTGTPQSPYGKSKLMV 156

                 ..
gi 162461808 163 EK 164
Cdd:PRK10675 157 EQ 158
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
8-126 3.35e-07

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 51.36  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLVQEEELqeIRALFRTFGrKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAID 87
Cdd:PLN02896  15 VTGATGYIGSWLVKLLLQRGYT--VHATLRDPA-KSLHLLSKWKEGDRLRLFRADLQEEGSFDEAVKGCDGVFHVAASME 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 162461808  88 --------PLGAASRQTILDVNLKGTQLLLDACVEAN-VPTFIYSSSV 126
Cdd:PLN02896  92 fdvssdhnNIEEYVQSKVIDPAIKGTLNVLKSCLKSKtVKRVVFTSSI 139
PRK07201 PRK07201
SDR family oxidoreductase;
7-166 3.80e-07

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 51.88  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFRTFGRKQEEELSKLQTKTKVTVLKGDI------LDAQCLKRACQgMSAVI 80
Cdd:PRK07201   4 FVTGGTGFIGRRLVSRLLDRRREATVHVLVRRQSLSRLEALAAYWGADRVVPLVGDLtepglgLSEADIAELGD-IDHVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  81 HTAAAIDPLGAASRQTIldVNLKGTQLLLDACVEANVPTFIYSSSVLVAG--PNSYKEIILNAHEEEHHestwsnPYPYS 158
Cdd:PRK07201  83 HLAAIYDLTADEEAQRA--ANVDGTRNVVELAERLQAATFHHVSSIAVAGdyEGVFREDDFDEGQGLPT------PYHRT 154

                 ....*...
gi 162461808 159 KKMAEKAV 166
Cdd:PRK07201 155 KFEAEKLV 162
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
7-161 4.23e-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: 51.15  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLvQEEELQEIRALfrtfgrkqeEELSKlQTKTKVTVLK--GDILDAQCLKRACQGMS------A 78
Cdd:cd05248    3 IVTGGAGFIGSNLVKAL-NERGITDILVV---------DNLSN-GEKFKNLVGLkiADYIDKDDFKDWVRKGDenfkieA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  79 VIHtaaaidpLGAASRQT------ILDVNLKGTQLLLDACVEANVPtFIYSSSVLVAG--PNSYKEIILNAHEEEhhest 150
Cdd:cd05248   72 IFH-------QGACSDTTetdgkyMMDNNYQYTKELLHYCLEKKIR-FIYASSAAVYGngSLGFAEDIETPNLRP----- 138
                        170
                 ....*....|.
gi 162461808 151 wSNPYPYSKKM 161
Cdd:cd05248  139 -LNVYGYSKLL 148
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-130 6.44e-07

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: 50.38  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEelQEIRAlFRTFGRKQEEELSKLQTKTKVTVLKGDILDAQcLKRACQGMSAVIHTAAAI 86
Cdd:cd05234    3 LVTGGAGFIGSHLVDRLLEEG--NEVVV-VDNLSSGRRENIEPEFENKAFRFVKRDLLDTA-DKVAKKDGDTVFHLAANP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 162461808  87 D-PLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAG 130
Cdd:cd05234   79 DvRLGATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSSTVYG 123
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
8-165 8.14e-07

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 50.40  E-value: 8.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLVQEEelQEIRALFRTF-GRKQEEELSKLQ-TKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAA 85
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRG--YTVKATVRDLtDRKKTEHLLALDgAKERLKLFKADLLEESSFEQAIEGCDAVFHTASP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGAASRQTILDVNLKGTQLLLDACVE-ANVPTFIYSSSVLVA-------GPNSYKEIILNAHEEEHHEStwSNPYPY 157
Cdd:PLN02986  88 VFFTVKDPQTELIDPALKGTINVLNTCKEtPSVKRVILTSSTAAVlfrqppiEANDVVDETFFSDPSLCRET--KNWYPL 165

                 ....*...
gi 162461808 158 SKKMAEKA 165
Cdd:PLN02986 166 SKILAENA 173
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
7-241 1.36e-06

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: 49.16  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLvQEEELQEIralfrTFGRKQEEelsklqtktkvtVLKGDILDAQCLKRACQGMS--AVIHTAA 84
Cdd:cd05254    3 LITGATGMLGRALVRLL-KERGYEVI-----GTGRSRAS------------LFKLDLTDPDAVEEAIRDYKpdVIINCAA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  85 AIDPLGAAS--RQTILdVNLKGTQLLLDACVEANVPtFIYSSSVLV----AGPnsYKeiilnaheEEHHestwSNP---Y 155
Cdd:cd05254   65 YTRVDKCESdpELAYR-VNVLAPENLARAAKEVGAR-LIHISTDYVfdgkKGP--YK--------EEDA----PNPlnvY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 156 PYSKKMAEKAVLAANGsilknggtlHTCALRLSFIYGEECqVTSTTVKTALKNnsiIKKNATFSIANPVYvGNAAWAHIL 235
Cdd:cd05254  129 GKSKLLGEVAVLNANP---------RYLILRTSWLYGELK-NGENFVEWMLRL---AAERKEVNVVHDQI-GSPTYAADL 194

                 ....*.
gi 162461808 236 AARSLQ 241
Cdd:cd05254  195 ADAILE 200
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
7-124 1.70e-06

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: 48.81  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQeIRALFRTFGRKQEEELSKLQtktkVTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:cd05251    2 LVFGATGKQGGSVVRALLKDPGFK-VRALTRDPSSPAAKALAAPG----VEVVQGDLDDPESLEAALKGVYGVFLVTDFW 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 162461808  87 DPLGAASRQtildvnlKGTqLLLDACVEANVPTFIYSS 124
Cdd:cd05251   77 EAGGEDEIA-------QGK-NVVDAAKRAGVQHFVFSS 106
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
8-171 3.46e-06

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: 48.11  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLVQeeelqeirALFRTFGRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAID 87
Cdd:cd05262    5 VTGATGFIGSAVVRELVA--------AGHEVVGLARSDAGAAKLEAAGAQVHRGDLEDLDILRKAAAEADAVIHLAFTHD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  88 PLGAAsrqTILDVNLKGTQLLLDACVEANVPtFIYSSSVLVAGPnsykeiilNAHEEEHHESTWSNPYPYSKKMAEKAVL 167
Cdd:cd05262   77 FDNFA---QACEVDRRAIEALGEALRGTGKP-LIYTSGIWLLGP--------TGGQEEDEEAPDDPPTPAARAVSEAAAL 144

                 ....
gi 162461808 168 AANG 171
Cdd:cd05262  145 ELAE 148
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
7-134 3.49e-06

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: 48.09  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVqeEELQEIRALFRTfgrkqeeeLSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAaai 86
Cdd:cd05229    3 HVLGASGPIGREVARELR--RRGWDVRLVSRS--------GSKLAWLPGVEIVAADAMDASSVIAAARGADVIYHCA--- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 dplGAASRQ--TILDVNLKGTqllLDACvEANVPTFIYSSSVLVAGPNSY 134
Cdd:cd05229   70 ---NPAYTRweELFPPLMENV---VAAA-EANGAKLVLPGNVYMYGPQAG 112
PLN02650 PLN02650
dihydroflavonol-4-reductase
8-168 4.04e-06

dihydroflavonol-4-reductase


Pssm-ID: 178256 [Multi-domain]  Cd Length: 351  Bit Score: 48.28  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLVQEEELqeIRALFRTFG--RKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAA 85
Cdd:PLN02650  10 VTGASGFIGSWLVMRLLERGYT--VRATVRDPAnvKKVKHLLDLPGATTRLTLWKADLAVEGSFDDAIRGCTGVFHVATP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGAASRQTILDVNLKGTQLLLDACVEA-NVPTFIYSSSvlvAGPNSYKEiilnaHEEE-HHESTWSN---------- 153
Cdd:PLN02650  88 MDFESKDPENEVIKPTVNGMLSIMKACAKAkTVRRIVFTSS---AGTVNVEE-----HQKPvYDEDCWSDldfcrrkkmt 159
                        170
                 ....*....|....*..
gi 162461808 154 --PYPYSKKMAEKAVLA 168
Cdd:PLN02650 160 gwMYFVSKTLAEKAAWK 176
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
7-121 4.74e-06

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: 47.68  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELqEIRALFRtfgrkQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:cd05259    3 AIAGATGTLGGPIVSALLASPGF-TVTVLTR-----PSSTSSNEFQPSGVKVVPVDYASHESLVAALKGVDAVISALGGA 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 162461808  87 DPlgaasrqtildvnlkGTQL-LLDACVEANVPTFI 121
Cdd:cd05259   77 AI---------------GDQLkLIDAAIAAGVKRFI 97
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
7-133 6.04e-06

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: 47.27  E-value: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVqeEELQEIRALFRTFGRKQEEELSklqtktKVTVLKGDILDAQCLKRACQGMSAV--IHTAA 84
Cdd:cd05269    2 LVTGATGKLGTAVVELLL--AKVASVVALVRNPEKAKAFAAD------GVEVRQGDYDDPETLERAFEGVDRLllISPSD 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 162461808  85 AIDPLGAASRqtildvnlkgtqlLLDACVEANVPTFIYsSSVLVAGPNS 133
Cdd:cd05269   74 LEDRIQQHKN-------------FIDAAKQAGVKHIVY-LSASGADEDS 108
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
7-193 6.47e-06

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: 47.27  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFRtfgrkQEEELSKLQTKTKVtvlkgdILDAQClkracqgmSAVIHTAAAI 86
Cdd:pfam04321   2 LITGANGQLGTELRRLLAERGI--EVVALTR-----AELDLTDPEAVARL------LREIKP--------DVVVNAAAYT 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   87 DPLGAAS-RQTILDVNLKGTQLLLDACVEANVPtFIYSSSVLV---AGPNSYKEiilnahEEEhhestwSNP---YPYSK 159
Cdd:pfam04321  61 AVDKAESePDLAYAINALAPANLAEACAAVGAP-LIHISTDYVfdgTKPRPYEE------DDE------TNPlnvYGRTK 127
                         170       180       190
                  ....*....|....*....|....*....|....
gi 162461808  160 KMAEKAVLAANGSILknggtlhtcALRLSFIYGE 193
Cdd:pfam04321 128 LAGEQAVRAAGPRHL---------ILRTSWVYGE 152
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
7-121 1.01e-05

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: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRmlvqeEELQ---EIRALFRTFGRKQEEElsklqtkTKVTVLKGDILDAQCLKRACQGMSAVihta 83
Cdd:cd05244    3 AIIGATGRTGSAIVR-----EALArghEVTALVRDPAKLPAEH-------EKLKVVQGDVLDLEDVKEALEGQDAV---- 66
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 162461808  84 aaIDPLGAASRQTILDVNLKGTQLLLDACVEANVPTFI 121
Cdd:cd05244   67 --ISALGTRNDLSPTTLHSEGTRNIVSAMKAAGVKRLI 102
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
7-147 1.53e-05

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


Pssm-ID: 223774 [Multi-domain]  Cd Length: 275  Bit Score: 46.05  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEelQEIRALFRTfgrkqeEELSKLQTKtKVTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:COG0702    4 LVTGATGFVGGAVVRELLARG--HEVRAAVRN------PEAAAALAG-GVEVVLGDLRDPKSLVAGAKGVDGVLLISGLL 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162461808  87 DPLGAASRQTILDVnlkgtqllLDACVEANVPTFIY-SSSVLVAGPNSYKEIILNAHEEEHH 147
Cdd:COG0702   75 DGSDAFRAVQVTAV--------VRAAEAAGAGVKHGvSLSVLGADAASPSALARAKAAVEAA 128
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
7-124 1.78e-05

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: 45.41  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQEEelQEIRALFRTfgrKQEEELSKLQTKtKVTVLKGDILDAQCLKRACQGMSAVIHTaaai 86
Cdd:pfam05368   2 LVFGATGQQGGSVVRASLKAG--HKVRALVRD---PKSELAKSLKEA-GVELVKGDLDDKESLVEALKGVDVVFSV---- 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 162461808   87 dpLGAASRQTILDvnlkGTqLLLDACVEANVPTFIYSS 124
Cdd:pfam05368  72 --TGFWAGKEIED----GK-KLADAAKEAGVKHFIPSS 102
PRK05865 PRK05865
sugar epimerase family protein;
8-130 2.19e-05

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 46.57  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIV-RMLVQEEELQEIralfrtfGRKQEEELSklqtkTKVTVLKGDILDAQCLKRACQGMSAVIHTAAAI 86
Cdd:PRK05865   5 VTGASGVLGRGLTaRLLSQGHEVVGI-------ARHRPDSWP-----SSADFIAADIRDATAVESAMTGADVVAHCAWVR 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 162461808  87 DPlgaaSRQtildVNLKGTQLLLDACVEANVPTFIYSSSVLVAG 130
Cdd:PRK05865  73 GR----NDH----INIDGTANVLKAMAETGTGRIVFTSSGHQPR 108
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
8-236 5.56e-05

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 44.70  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLVQEEelQEIRALFR-TFGRKQEEELSKLQ-TKTKVTVLKGDILDAQCLKRACQGMSAVIHTAA- 84
Cdd:PLN02662   9 VTGASGYIASWLVKLLLQRG--YTVKATVRdPNDPKKTEHLLALDgAKERLHLFKANLLEEGSFDSVVDGCEGVFHTASp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  85 ----AIDPlgaasRQTILDVNLKGTQLLLDACveANVPTF----IYSS--SVLVAGPNSYKEIILNaheeehhESTWSNP 154
Cdd:PLN02662  87 fyhdVTDP-----QAELIDPAVKGTLNVLRSC--AKVPSVkrvvVTSSmaAVAYNGKPLTPDVVVD-------ETWFSDP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 155 ---------YPYSKKMAEKAvlAANGSilKNGGtLHTCALRLSFIYGEECQVT-STTVKTALK--NNSIIKKNATFSIAN 222
Cdd:PLN02662 153 afceesklwYVLSKTLAEEA--AWKFA--KENG-IDMVTINPAMVIGPLLQPTlNTSAEAILNliNGAQTFPNASYRWVD 227
                        250
                 ....*....|....
gi 162461808 223 pvyVGNAAWAHILA 236
Cdd:PLN02662 228 ---VRDVANAHIQA 238
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-126 6.45e-05

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: 43.24  E-value: 6.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808     7 LVTGAGGFLGQRIVRMLVQ---------------EEELQEIRALFRTFGRkqeeelsklqtktKVTVLKGDILDAQCLKR 71
Cdd:smart00822   4 LITGGLGGLGRALARWLAErgarrlvllsrsgpdAPGAAALLAELEAAGA-------------RVTVVACDVADRDALAA 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162461808    72 ACQGMSA-------VIHTAAAID--PLGAASRQTILDVN---LKGTQLLLDACVEANVPTFIYSSSV 126
Cdd:smart00822  71 VLAAIPAvegpltgVIHAAGVLDdgVLASLTPERFAAVLapkAAGAWNLHELTADLPLDFFVLFSSI 137
PLN02686 PLN02686
cinnamoyl-CoA reductase
8-175 6.99e-05

cinnamoyl-CoA reductase


Pssm-ID: 215370  Cd Length: 367  Bit Score: 44.39  E-value: 6.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIV-RMLVQ----------EEELQEIRALfRTFGRKQeeelsklQTKTKVTVLKGDILDAQCLKRACQGM 76
Cdd:PLN02686  58 VTGGVSFLGLAIVdRLLRHgysvriavdtQEDKEKLREM-EMFGEMG-------RSNDGIWTVMANLTEPESLHEAFDGC 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  77 SAVIHTAAAIDPLGAAS-RQTILDVNLKGTQLLLDACVE-ANVPTFIYSSSVLVAG-----PNSYKEIIlnaheeehHES 149
Cdd:PLN02686 130 AGVFHTSAFVDPAGLSGyTKSMAELEAKASENVIEACVRtESVRKCVFTSSLLACVwrqnyPHDLPPVI--------DEE 201
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 162461808 150 TWSNP---------YPYSKKMAEKAVL-AANGSILK 175
Cdd:PLN02686 202 SWSDEsfcrdnklwYALGKLKAEKAAWrAARGKGLK 237
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
7-192 1.14e-04

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: 43.62  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVqeEELQEIRAlfrtfgrkqeEELSKLQTKTKVT----VLKGDILDAQCLKRACQGMSAVIHT 82
Cdd:cd05273    4 LVTGAGGFIGSHLAERLK--AEGHYVRG----------ADWKSPEHMTQPTdddeFHLVDLREMENCLKATEGVDHVFHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  83 AAAIDPLGAASRQ--TILDVNLKGTQLLLDACVEANVPTFIYSSSVLVAgPNSYKEIILNA--HEEEHHESTWSNPYPYS 158
Cdd:cd05273   72 AADMGGMGYIQSNhaVIMYNNTLINFNMLEAARINGVERFLFASSACVY-PEFKQLETTVVrlREEDAWPAEPQDAYGWE 150
                        170       180       190
                 ....*....|....*....|....*....|....
gi 162461808 159 KKMAEKAVLAANGSIlknggTLHTCALRLSFIYG 192
Cdd:cd05273  151 KLATERLCQHYNEDY-----GIETRIVRFHNIYG 179
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
7-126 3.12e-04

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 41.01  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVqEEELQEIRALFRTFG--RKQEEELSKLQTK-TKVTVLKGDILDAQCLKRACQGMSA----- 78
Cdd:pfam08659   4 LITGGLGGLGRELARWLA-ERGARHLVLLSRSAAprPDAQALIAELEARgVEVVVVACDVSDPDAVAALLAEIKAegppi 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 162461808   79 --VIHTA-----AAIDPLGAASRQTILDVNLKGTQLLLDACVEANVPTFIYSSSV 126
Cdd:pfam08659  83 rgVIHAAgvlrdALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSI 137
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion];
7-134 3.30e-04

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion];


Pssm-ID: 226674 [Multi-domain]  Cd Length: 246  Bit Score: 41.85  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVqEEELQEIRAlfrtfGRKQE--EELSKLQTKTKVTVLKGDILDAQCLKRACQGMSA------ 78
Cdd:COG4221   10 LITGASSGIGEATARALA-EAGAKVVLA-----ARREErlEALADEIGAGAALALALDVTDRAAVEAAIEALPEefgrid 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162461808  79 -VIHTA--AAIDPLGAASR---QTILDVNLKG----TQLLLDACVEANVPTFIYSSSvlVAGPNSY 134
Cdd:COG4221   84 iLVNNAglALGDPLDEADLddwDRMIDTNVKGllngTRAVLPGMVERKSGHIINLGS--IAGRYPY 147
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
7-192 5.68e-04

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


Pssm-ID: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 41.33  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEElqEIRAL--FRTfGRKQEeelskLQTKTKVTVLKGDILDAQCLKRACQGMS--AVIHT 82
Cdd:cd08957    4 LITGGAGQIGSHLIEHLLERGH--QVVVIdnFAT-GRREH-----LPDHPNLTVVEGSIADKALVDKLFGDFKpdAVVHT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  83 AAAI-DPLGAAS-RQTildvNLKGTQLLLDACVEANVPTFIYSSSVLVAG-PNSYKEIILNaheeeHHESTWSNPYPYSK 159
Cdd:cd08957   76 AAAYkDPDDWYEdTLT----NVVGGANVVQAAKKAGVKRLIYFQTALCYGlKPMQQPIRLD-----HPRAPPGSSYAISK 146
                        170       180       190
                 ....*....|....*....|....*....|...
gi 162461808 160 KMAEKAVLAANgsilknggtLHTCALRLSFIYG 192
Cdd:cd08957  147 TAGEYYLELSG---------VDFVTFRLANVTG 170
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
7-125 7.25e-04

GDP-mannose 4,6 dehydratase;


Pssm-ID: 435301 [Multi-domain]  Cd Length: 327  Bit Score: 40.99  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808    7 LVTGAGGFLGQRIVRMLVQEEElqEIRALFR-----TFGRKqeEELSKLQTKTKVTVLKGDILDAQCLKRACQGMS--AV 79
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGY--EVHGIVRrsssfNTGRL--EHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQpdEI 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 162461808   80 IHTAAAIDPLG--AASRQTIlDVNLKGTQLLLDACVEANVP---TFIYSSS 125
Cdd:pfam16363  77 YNLAAQSHVDVsfEQPEYTA-DTNVLGTLRLLEAIRSLGLEkkvRFYQAST 126
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-113 1.02e-03

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 40.14  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQ-----------EEELQEIRALFRTFGRkqeeelsklqtktKVTVLKGDILDAQCLKRACQG 75
Cdd:PRK05653   9 LVTGASRGIGRAIALRLAAdgakvviydsnEEAAEALAAELRAAGG-------------EARVLVFDVSDEAAVRALIEA 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 162461808  76 MSAV------------IHTAAAIDPLGAASRQTILDVNLKGTQLLLDACV 113
Cdd:PRK05653  76 AVEAfgaldilvnnagITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAAL 125
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
7-222 1.14e-03

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


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 40.03  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVrmlVQEEELQEIRALFRTFGRKQEEelsklqtktkvtvlkgdildaqcLKRACQGMSAVIHTAAAI 86
Cdd:cd05261    4 LITGAKGFIGKNLI---ARLKEQKDDDIFFYDRESDESE-----------------------LDDFLQGADFIFHLAGVN 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  87 DPLGAASrqtILDVNLKGTQLLLDACVEA-NVPTFIYSSSVlvagpnsykeiilnaheeehhESTWSNPYPYSKKMAEKA 165
Cdd:cd05261   58 RPKDEAE---FESGNVGLTERLLDALTRNgKKPPILLSSSI---------------------QAALDNPYGKSKLAAEEL 113
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 166 VLAANGsilKNGGTLHTcaLRLSFIYGEECqvtsttvktaLKN-NSIIkknATFS--IAN 222
Cdd:cd05261  114 LQEYAR---ETGAPVYI--YRLPNVFGKWC----------RPNyNSAV---ATFCynIAR 155
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
7-104 2.34e-03

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 38.99  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEelQEIRALFRTFGrkQEEELSKLQTKTKVTVLKGDILDAQC--LKRACQGMSAVIHTA- 83
Cdd:cd05331    2 IVTGAAQGIGRAVARHLLQAG--ATVIALDLPFV--LLLEYGDPLRLTPLDVADAAAVREVCsrLLAEHGPIDALVNCAg 77
                         90       100
                 ....*....|....*....|....*
gi 162461808  84 ----AAIDPLGAASRQTILDVNLKG 104
Cdd:cd05331   78 vlrpGATDPLSTEDWEQTFAVNVTG 102
PRK12826 PRK12826
SDR family oxidoreductase;
7-131 2.48e-03

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 39.13  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRML-----------VQEEELQEIRALFRTFGRKqeeelsklqtktkVTVLKGDILDAQCLKRACQ- 74
Cdd:PRK12826  10 LVTGAARGIGRAIAVRLaadgaevivvdICGDDAAATAELVEAAGGK-------------ARARQVDVRDRAALKAAVAa 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162461808  75 ------GMSAVIHTAAaIDPLGAASR------QTILDVNLKGTQLLLDAC----VEANVPTFIYSSSvlVAGP 131
Cdd:PRK12826  77 gvedfgRLDILVANAG-IFPLTPFAEmddeqwERVIDVNLTGTFLLTQAAlpalIRAGGGRIVLTSS--VAGP 146
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
7-111 3.00e-03

dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224013 [Multi-domain]  Cd Length: 340  Bit Score: 39.13  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEELQEIRALFR-TF-GRKqeEELSKLQTKTKVTVLKGDILDAQCLKRACQGMS--AVIHT 82
Cdd:COG1088    4 LVTGGAGFIGSNFVRYILNKHPDDHVVNLDKlTYaGNL--ENLADVEDSPRYRFVQGDICDRELVDRLFKEYQpdAVVHF 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 162461808  83 AAA-------IDPlgAASRQTildvNLKGTQLLLDA 111
Cdd:COG1088   82 AAEshvdrsiDGP--APFIQT----NVVGTYTLLEA 111
PLN00198 PLN00198
anthocyanidin reductase; Provisional
8-237 5.77e-03

anthocyanidin reductase; Provisional


Pssm-ID: 215100 [Multi-domain]  Cd Length: 338  Bit Score: 38.33  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLvqeeeLQEIRALFRTF----GRKQEEELSKLQTKTKVTVLKGDILDAQCLKRACQGMSAVIHTA 83
Cdd:PLN00198  14 VIGGTGFLASLLIKLL-----LQKGYAVNTTVrdpeNQKKIAHLRALQELGDLKIFGADLTDEESFEAPIAGCDLVFHVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  84 AAIDPLGAASRQTILDVNLKGTQLLLDACVEA-NVPTFIYSSSVLVAGPNSYKEIILNAHEE---------EHHESTWSn 153
Cdd:PLN00198  89 TPVNFASEDPENDMIKPAIQGVHNVLKACAKAkSVKRVILTSSAAAVSINKLSGTGLVMNEKnwtdvefltSEKPPTWG- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808 154 pYPYSKKMAEKAV--LAANGSI--------LKNGGTL-----HTCALRLSFIYGEECQVtsttvkTALKNNSIIKKNATF 218
Cdd:PLN00198 168 -YPASKTLAEKAAwkFAEENNIdlitviptLMAGPSLtsdipSSLSLAMSLITGNEFLI------NGLKGMQMLSGSISI 240
                        250
                 ....*....|....*....
gi 162461808 219 sianpVYVGNAAWAHILAA 237
Cdd:PLN00198 241 -----THVEDVCRAHIFLA 254
PLN02989 PLN02989
cinnamyl-alcohol dehydrogenase family protein
8-165 5.77e-03

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178569 [Multi-domain]  Cd Length: 325  Bit Score: 38.09  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   8 VTGAGGFLGQRIVRMLVQEEelQEIRALFRT-FGRKQEEELSKLQ-TKTKVTVLKGDILDAQCLKRACQGMSAVIHTAAA 85
Cdd:PLN02989  10 VTGASGYIASWIVKLLLFRG--YTINATVRDpKDRKKTDHLLALDgAKERLKLFKADLLDEGSFELAIDGCETVFHTASP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808  86 IDPLGAASRQT-ILDVNLKGTQLLLDACVE-ANVPTFIYSSSVLVA-------GPNS-YKEIILNAHEEEHHESTWsnpY 155
Cdd:PLN02989  88 VAITVKTDPQVeLINPAVNGTINVLRTCTKvSSVKRVILTSSMAAVlapetklGPNDvVDETFFTNPSFAEERKQW---Y 164
                        170
                 ....*....|
gi 162461808 156 PYSKKMAEKA 165
Cdd:PLN02989 165 VLSKTLAEDA 174
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-132 7.12e-03

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 223959 [Multi-domain]  Cd Length: 251  Bit Score: 37.49  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   7 LVTGAGGFLGQRIVRMLVQEEelQEIRALFRTFGRKQEEELSKLQTKT---KVTVLKGDILD--------AQCLKRACQG 75
Cdd:COG1028    9 LVTGASSGIGRAIARALAREG--ARVVVAARRSEEEAAEALAAAIKEAgggRAAAVAADVSDdeesvealVAAAEEEFGR 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162461808  76 MSAVIHTAAAIDPLGAASRQT------ILDVNLKGTQLLLDACVEANVP-TFIYSSSVLVAGPN 132
Cdd:COG1028   87 IDILVNNAGIAGPDAPLEELTeedwdrVIDVNLLGAFLLTRAALPLMKKqRIVNISSVAGLGGP 150
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
6-115 9.30e-03

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 37.27  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162461808   6 CLVTGAGGFLGQRIVRMLVqeEELQEIRALfrTFGRKQEEELSK---LQTKTKVTVLKGDILDAQCLKR---ACQGM--- 76
Cdd:cd05367    2 IILTGASRGIGRALAEELL--KRGSPSVVV--LLARSEEPLQELkeeLRPGLRVTTVKADLSDAAGVEQlleAIRKLdge 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 162461808  77 -SAVIHTAAAIDPLGAASRQTI------LDVNLKGTQLLLDACVEA 115
Cdd:cd05367   78 rDLLINNAGSLGPVSKIEFIDLdelqkyFDLNLTSPVCLTSTLLRA 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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