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Conserved domains on  [gi|16129980|ref|NP_416544|]
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dTDP-4-dehydrorhamnose reductase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 10793331)

NAD(P)-dependent oxidoreductase, an extended short-chain dehydrogenase similar to bacterial dTDP-4-dehydrorhamnose reductase, dTDP-4-keto-6-deoxy-D-glucose reductase, and mammalian S-adenosylmethionine synthase 2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
1-299 0e+00

dTDP-4-dehydrorhamnose reductase; Provisional


:

Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 625.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    1 MNILLFGKTGQVGWELQRALAPLGNLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLI 80
Cdd:PRK09987   1 MNILLFGKTGQVGWELQRALAPLGNLIALDVHSTDYCGDFSNPEGVAETVRKIRPDVIVNAAAHTAVDKAESEPEFAQLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   81 NATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGN 160
Cdd:PRK09987  81 NATSVEAIAKAANEVGAWVVHYSTDYVFPGTGDIPWQETDATAPLNVYGETKLAGEKALQEHCAKHLIFRTSWVYAGKGN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  161 NFAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIP 240
Cdd:PRK09987 161 NFAKTMLRLAKEREELSVINDQFGAPTGAELLADCTAHAIRVALNKPEVAGLYHLVASGTTTWHDYAALVFEEARKAGIT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129980  241 LALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNELFTTTAI 299
Cdd:PRK09987 241 LALNKLNAVPTSAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLTELFTTTAI 299
 
Name Accession Description Interval E-value
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
1-299 0e+00

dTDP-4-dehydrorhamnose reductase; Provisional


Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 625.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    1 MNILLFGKTGQVGWELQRALAPLGNLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLI 80
Cdd:PRK09987   1 MNILLFGKTGQVGWELQRALAPLGNLIALDVHSTDYCGDFSNPEGVAETVRKIRPDVIVNAAAHTAVDKAESEPEFAQLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   81 NATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGN 160
Cdd:PRK09987  81 NATSVEAIAKAANEVGAWVVHYSTDYVFPGTGDIPWQETDATAPLNVYGETKLAGEKALQEHCAKHLIFRTSWVYAGKGN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  161 NFAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIP 240
Cdd:PRK09987 161 NFAKTMLRLAKEREELSVINDQFGAPTGAELLADCTAHAIRVALNKPEVAGLYHLVASGTTTWHDYAALVFEEARKAGIT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129980  241 LALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNELFTTTAI 299
Cdd:PRK09987 241 LALNKLNAVPTSAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLTELFTTTAI 299
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
3-293 4.78e-141

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 398.74  E-value: 4.78e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALAPLGnliaFDVHSTDY-CGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLIN 81
Cdd:COG1091   2 ILVTGANGQLGRALVRLLAERG----YEVVALDRsELDITDPEAVAALLEEVRPDVVINAAAYTAVDKAESEPELAYAVN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  82 ATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGNN 161
Cdd:COG1091  78 ATGPANLAEACAELGARLIHISTDYVFDGTKGTPYTEDDPPNPLNVYGRSKLAGEQAVRAAGPRHLILRTSWVYGPHGKN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 162 FAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRvalnkPDVAGLYHLVASGTTTWYDYAALVFEEARKAgipl 241
Cdd:COG1091 158 FVKTMLRLLKEGEELRVVDDQIGSPTYAADLARAILALLE-----KDLSGIYHLTGSGETSWYEFARAIAELAGLD---- 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129980 242 alNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNEL 293
Cdd:COG1091 229 --ALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDWREALAELLAEL 278
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
3-293 1.62e-140

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: 397.41  E-value: 1.62e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980     3 ILLFGKTGQVGWELQRALAPLG-NLIAFDVHstdyCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLIN 81
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGiEVVALTRA----ELDLTDPEAVARLLREIKPDVVVNAAAYTAVDKAESEPDLAYAIN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    82 ATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGNN 161
Cdd:pfam04321  77 ALAPANLAEACAAVGAPLIHISTDYVFDGTKPRPYEEDDETNPLNVYGRTKLAGEQAVRAAGPRHLILRTSWVYGEYGNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   162 FAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIPl 241
Cdd:pfam04321 157 FVKTMLRLAAEREELKVVDDQFGRPTWARDLADVLLQLLERLAADPPYWGVYHLSNSGQTSWYEFARAIFDEAGADPSE- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129980   242 alnkLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNEL 293
Cdd:pfam04321 236 ----VRPITTAEFPTPARRPANSVLDTTKLEATFGIVLRPWREALKEVLDEL 283
rmlD TIGR01214
dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making ...
3-293 1.25e-115

dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273505 [Multi-domain]  Cd Length: 287  Bit Score: 334.75  E-value: 1.25e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980     3 ILLFGKTGQVGWELQRALAPLGNLIAFDVHSTdycGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLINA 82
Cdd:TIGR01214   2 ILITGANGQLGRELVQQLSPEGRVVVALTRSQ---LDLTDPEALERLLRAIRPDAVVNTAAYTDVDGAESDPEKAFAVNA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    83 TSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYA-GKGNN 161
Cdd:TIGR01214  79 LAPQNLARAAARHGARLVHISTDYVFDGEGKRPYREDDATNPLNVYGQSKLAGEQAVRAAGPNALIVRTSWLYGgGGGRN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   162 FAKTMLRLAKEREELAVINDQFGAPTGAELLADCTahaIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIPL 241
Cdd:TIGR01214 159 FVRTMLRLAGRGEELRVVDDQIGSPTYAGDLARVI---AALLQRLARARGVYHLANSGQVSWYEFAQAIFEEAGADGLLL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129980   242 ALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNEL 293
Cdd:TIGR01214 236 HPQEVKPISSKEYPRPARRPAYSVLDNTKLVKTLGLPLPHWREALRRYLQEA 287
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
2-287 1.01e-107

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: 314.18  E-value: 1.01e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLG-NLIAFDV-HSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQL 79
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERGyEVIGTGRsRASLFKLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCESDPELAYR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  80 INATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDmPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVY--AG 157
Cdd:cd05254  81 VNVLAPENLARAAKEVGARLIHISTDYVFDGKKG-PYKEEDAPNPLNVYGKSKLLGEVAVLNANPRYLILRTSWLYgeLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 158 KGNNFAKTMLRLAKEREELAVINDQFGAPTGAELLADctahAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARka 237
Cdd:cd05254 160 NGENFVEWMLRLAAERKEVNVVHDQIGSPTYAADLAD----AILELIERNSLTGIYHLSNSGPISKYEFAKLIADALG-- 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16129980 238 gipLALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVK 287
Cdd:cd05254 234 ---LPDVEIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
 
Name Accession Description Interval E-value
PRK09987 PRK09987
dTDP-4-dehydrorhamnose reductase; Provisional
1-299 0e+00

dTDP-4-dehydrorhamnose reductase; Provisional


Pssm-ID: 182184 [Multi-domain]  Cd Length: 299  Bit Score: 625.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    1 MNILLFGKTGQVGWELQRALAPLGNLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLI 80
Cdd:PRK09987   1 MNILLFGKTGQVGWELQRALAPLGNLIALDVHSTDYCGDFSNPEGVAETVRKIRPDVIVNAAAHTAVDKAESEPEFAQLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   81 NATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGN 160
Cdd:PRK09987  81 NATSVEAIAKAANEVGAWVVHYSTDYVFPGTGDIPWQETDATAPLNVYGETKLAGEKALQEHCAKHLIFRTSWVYAGKGN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  161 NFAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIP 240
Cdd:PRK09987 161 NFAKTMLRLAKEREELSVINDQFGAPTGAELLADCTAHAIRVALNKPEVAGLYHLVASGTTTWHDYAALVFEEARKAGIT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129980  241 LALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNELFTTTAI 299
Cdd:PRK09987 241 LALNKLNAVPTSAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLTELFTTTAI 299
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
3-293 4.78e-141

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 398.74  E-value: 4.78e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALAPLGnliaFDVHSTDY-CGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLIN 81
Cdd:COG1091   2 ILVTGANGQLGRALVRLLAERG----YEVVALDRsELDITDPEAVAALLEEVRPDVVINAAAYTAVDKAESEPELAYAVN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  82 ATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGNN 161
Cdd:COG1091  78 ATGPANLAEACAELGARLIHISTDYVFDGTKGTPYTEDDPPNPLNVYGRSKLAGEQAVRAAGPRHLILRTSWVYGPHGKN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 162 FAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRvalnkPDVAGLYHLVASGTTTWYDYAALVFEEARKAgipl 241
Cdd:COG1091 158 FVKTMLRLLKEGEELRVVDDQIGSPTYAADLARAILALLE-----KDLSGIYHLTGSGETSWYEFARAIAELAGLD---- 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129980 242 alNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNEL 293
Cdd:COG1091 229 --ALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDWREALAELLAEL 278
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
3-293 1.62e-140

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: 397.41  E-value: 1.62e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980     3 ILLFGKTGQVGWELQRALAPLG-NLIAFDVHstdyCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLIN 81
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGiEVVALTRA----ELDLTDPEAVARLLREIKPDVVVNAAAYTAVDKAESEPDLAYAIN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    82 ATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGNN 161
Cdd:pfam04321  77 ALAPANLAEACAAVGAPLIHISTDYVFDGTKPRPYEEDDETNPLNVYGRTKLAGEQAVRAAGPRHLILRTSWVYGEYGNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   162 FAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIPl 241
Cdd:pfam04321 157 FVKTMLRLAAEREELKVVDDQFGRPTWARDLADVLLQLLERLAADPPYWGVYHLSNSGQTSWYEFARAIFDEAGADPSE- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129980   242 alnkLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNEL 293
Cdd:pfam04321 236 ----VRPITTAEFPTPARRPANSVLDTTKLEATFGIVLRPWREALKEVLDEL 283
rmlD TIGR01214
dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making ...
3-293 1.25e-115

dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273505 [Multi-domain]  Cd Length: 287  Bit Score: 334.75  E-value: 1.25e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980     3 ILLFGKTGQVGWELQRALAPLGNLIAFDVHSTdycGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLINA 82
Cdd:TIGR01214   2 ILITGANGQLGRELVQQLSPEGRVVVALTRSQ---LDLTDPEALERLLRAIRPDAVVNTAAYTDVDGAESDPEKAFAVNA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    83 TSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYA-GKGNN 161
Cdd:TIGR01214  79 LAPQNLARAAARHGARLVHISTDYVFDGEGKRPYREDDATNPLNVYGQSKLAGEQAVRAAGPNALIVRTSWLYGgGGGRN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   162 FAKTMLRLAKEREELAVINDQFGAPTGAELLADCTahaIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIPL 241
Cdd:TIGR01214 159 FVRTMLRLAGRGEELRVVDDQIGSPTYAGDLARVI---AALLQRLARARGVYHLANSGQVSWYEFAQAIFEEAGADGLLL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129980   242 ALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNEL 293
Cdd:TIGR01214 236 HPQEVKPISSKEYPRPARRPAYSVLDNTKLVKTLGLPLPHWREALRRYLQEA 287
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
2-287 1.01e-107

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: 314.18  E-value: 1.01e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLG-NLIAFDV-HSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQL 79
Cdd:cd05254   1 KILITGATGMLGRALVRLLKERGyEVIGTGRsRASLFKLDLTDPDAVEEAIRDYKPDVIINCAAYTRVDKCESDPELAYR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  80 INATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDmPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVY--AG 157
Cdd:cd05254  81 VNVLAPENLARAAKEVGARLIHISTDYVFDGKKG-PYKEEDAPNPLNVYGKSKLLGEVAVLNANPRYLILRTSWLYgeLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 158 KGNNFAKTMLRLAKEREELAVINDQFGAPTGAELLADctahAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARka 237
Cdd:cd05254 160 NGENFVEWMLRLAAERKEVNVVHDQIGSPTYAADLAD----AILELIERNSLTGIYHLSNSGPISKYEFAKLIADALG-- 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16129980 238 gipLALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVK 287
Cdd:cd05254 234 ---LPDVEIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDWKEALR 280
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2-273 2.58e-31

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 118.16  E-value: 2.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLGN-LIAFDVHSTD------------YCGDFSNPEGVAETVRsiRPDIIVNAAAHTAVd 68
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHeVVGLDRSPPGaanlaalpgvefVRGDLRDPEALAAALA--GVDAVVHLAAPAGV- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  69 kAESEPEFAQLINATSVEAIAKAANEVG-AWVIHYSTDYVFpGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKH- 146
Cdd:COG0451  78 -GEEDPDETLEVNVEGTLNLLEAARAAGvKRFVYASSSSVY-GDGEGPIDEDTPLRPVSPYGASKLAAELLARAYARRYg 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 147 ---LIFRTSWVYAGKGNNFAKTMLRLAKEREELAVINDqfgaptGAELL-----ADCtAHAIRVALNKPDVAG-LYHLVA 217
Cdd:COG0451 156 lpvTILRPGNVYGPGDRGVLPRLIRRALAGEPVPVFGD------GDQRRdfihvDDV-ARAIVLALEAPAAPGgVYNVGG 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129980 218 SGTTTWYDYAALVfeeARKAGIPLALNklnavpttaYPTPARRPHNSRLNTEKFQQ 273
Cdd:COG0451 229 GEPVTLRELAEAI---AEALGRPPEIV---------YPARPGDVRPRRADNSKARR 272
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
3-215 2.82e-27

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: 105.07  E-value: 2.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALAPLG-NLIAFDvhstdycgdfsnpegvaetvrsiRPDIIVNAAAHTAVDKAESEPEFAQLIN 81
Cdd:cd08946   1 ILVTGGAGFIGSHLVRRLLERGhEVVVID-----------------------RLDVVVHLAALVGVPASWDNPDEDFETN 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  82 ATSVEAIAKAANEVG-AWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKH----LIFRTSWVYA 156
Cdd:cd08946  58 VVGTLNLLEAARKAGvKRFVYASSASVYGSPEGLPEEEETPPRPLSPYGVSKLAAEHLLRSYGESYglpvVILRLANVYG 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129980 157 GKG----NNFAKTMLRLAKEREELAVIND--QFGAPTGAELLADCTAHAIRVALNkpdVAGLYHL 215
Cdd:cd08946 138 PGQrprlDGVVNDFIRRALEGKPLTVFGGgnQTRDFIHVDDVVRAILHALENPLE---GGGVYNI 199
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
3-181 5.05e-16

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: 75.80  E-value: 5.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980     3 ILLFGKTGQVGWELQRALAPLG-NLIAFDVHSTDYC-----------GDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKA 70
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGyEVIGLDRLTSASNtarladlrfveGDLTDRDALEKLLADVRPDAVIHLAAVGGVGAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    71 ESEPEFAQLINATSVEAIAKAANEVGAWVIHY-STDYVFPGNGDMP---WLETDATAPLNVYGETKLAGEKALQEYCAKH 146
Cdd:pfam01370  81 IEDPEDFIEANVLGTLNLLEAARKAGVKRFLFaSSSEVYGDGAEIPqeeTTLTGPLAPNSPYAAAKLAGEWLVLAYAAAY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 16129980   147 ----LIFRTSWVY-----AGKGNNFAKTMLRLAKEREELAVIND 181
Cdd:pfam01370 161 glraVILRLFNVYgpgdnEGFVSRVIPALIRRILEGKPILLWGD 204
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
2-240 5.02e-10

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: 59.29  E-value: 5.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLGNLIAFDVHSTDYCGD----FSNPEGVAETVRSIRPDIIVNAAAHTAV-DKAESEPEF 76
Cdd:cd05232   1 KVLVTGANGFIGRALVDKLLSRGEEVRIAVRNAENAEPsvvlAELPDIDSFTDLFLGVDAVVHLAARVHVmNDQGADPLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  77 A-QLINATSVEAIAKAANEVGA-WVIHYSTDYVF-PGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKH----LIF 149
Cdd:cd05232  81 DyRKVNTELTRRLARAAARQGVkRFVFLSSVKVNgEGTVGAPFDETDPPAPQDAYGRSKLEAERALLELGASDgmevVIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 150 RTSWVYaGKG--NNFAkTMLRLAKEREELavindqfgaPTGAE------LLADCTAHAIRVALNKPDVAGLYHLVASGTT 221
Cdd:cd05232 161 RPPMVY-GPGvrGNFA-RLMRLIDRGLPL---------PPGAVknrrslVSLDNLVDAIYLCISLPKAANGTFLVSDGPP 229
                       250
                ....*....|....*....
gi 16129980 222 twYDYAALVFEEARKAGIP 240
Cdd:cd05232 230 --VSTAELVDEIRRALGKP 246
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
1-243 1.11e-09

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: 58.03  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   1 MNILLFGKTGQVGWELQRALAPLG-NLIAF---DVHSTDYC------------GDFSNPEGVAETVRSIrpDIIVNAAA- 63
Cdd:cd05271   1 MVVTVFGATGFIGRYVVNRLAKRGsQVIVPyrcEAYARRLLvmgdlgqvlfveFDLRDDESIRKALEGS--DVVINLVGr 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  64 --HTAVDKAEsepefaqLINATSVEAIAKAANEVGAW-VIHYSTdyvfpgngdmpwLETDATAPlNVYGETKLAGEKALQ 140
Cdd:cd05271  79 lyETKNFSFE-------DVHVEGPERLAKAAKEAGVErLIHISA------------LGADANSP-SKYLRSKAEGEEAVR 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 141 EYCAKHLIFRTSWVYaGKGNNFaktMLRLAKEREELAVINdqfGAPTGAE----LLADCTAHAIRVALNKPDVAGL-YHL 215
Cdd:cd05271 139 EAFPEATIVRPSVVF-GREDRF---LNRFAKLLAFLPFPP---LIGGGQTkfqpVYVGDVAEAIARALKDPETEGKtYEL 211
                       250       260       270
                ....*....|....*....|....*....|..
gi 16129980 216 VASGTTTWYDY----AALVFEEARKAGIPLAL 243
Cdd:cd05271 212 VGPKVYTLAELvellRRLGGRKRRVLPLPLWL 243
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
1-177 4.41e-09

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: 56.24  E-value: 4.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   1 MNILLFGKTGQVGWELQRALA---PLGNLIAFDV----------HSTDYCGDFSNPEgVAETVRSIRPDIIVNAAAHtaV 67
Cdd:cd05238   1 MKVLITGASGFVGQRLAERLLsdvPNERLILIDVvspkapsgapRVTQIAGDLAVPA-LIEALANGRPDVVFHLAAI--V 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  68 D-KAESEPEFAQLINATSVEAIAKAA--NEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCA 144
Cdd:cd05238  78 SgGAEADFDLGYRVNVDGTRNLLEALrkNGPKPRFVFTSSLAVYGLPLPNPVTDHTALDPASSYGAQKAMCELLLNDYSR 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 16129980 145 KH----LIFRTSWVYAGKGN-NFAKTMLRLAKEREELA 177
Cdd:cd05238 158 RGfvdgRTLRLPTVCVRPGRpNKAASAFASTIIREPLV 195
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
38-155 4.54e-08

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: 53.32  E-value: 4.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  38 GDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPE-FAQlINATSVEAIAKAANEvgAWV---IHYSTDYVFpgnGD 113
Cdd:cd05246  58 GDICDAELVDRLFEEEKIDAVIHFAAESHVDRSISDPEpFIR-TNVLGTYTLLEAARK--YGVkrfVHISTDEVY---GD 131
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 16129980 114 MP----WLETDATAPLNVYGETKLAGEKALQEYCAKH----LIFRTSWVY 155
Cdd:cd05246 132 LLddgeFTETSPLAPTSPYSASKAAADLLVRAYHRTYglpvVITRCSNNY 181
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
3-185 1.33e-07

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: 50.48  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALAPLGN-LIAFDVHST-----------DYCGDFSNPEGVAETVRsiRPDIIVNAAAHTAVDKA 70
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHeVTLLVRNTKrlskedqepvaVVEGDLRDLDSLSDAVQ--GVDVVIHLAGAPRDTRD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  71 ESEpefaQLINATsvEAIAKAANEVGAWVIHYSTDyvfpGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFR 150
Cdd:cd05226  79 FCE----VDVEGT--RNVLEAAKEAGVKHFIFISS----LGAYGDLHEETEPSPSSPYLAVKAKTEAVLREASLPYTIVR 148
                       170       180       190
                ....*....|....*....|....*....|....*
gi 16129980 151 TSWVYagkgNNFAKTMLRLAKEREelaVINDQFGA 185
Cdd:cd05226 149 PGVIY----GDLARAIANAVVTPG---KKNETFNA 176
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
38-136 1.92e-07

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 51.39  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    38 GDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPE-FAQlINATSV----EAIAKAANEVGAWVIHYSTDYVFPGNG 112
Cdd:pfam16363  56 GDLTDSSNLVRLLAEVQPDEIYNLAAQSHVDVSFEQPEyTAD-TNVLGTlrllEAIRSLGLEKKVRFYQASTSEVYGKVQ 134
                          90       100
                  ....*....|....*....|....
gi 16129980   113 DMPWLETDATAPLNVYGETKLAGE 136
Cdd:pfam16363 135 EVPQTETTPFYPRSPYAAAKLYAD 158
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
14-151 2.91e-07

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: 50.98  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980    14 WELQRALAPLGNLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLINATSVEAIAKAAN 93
Cdd:pfam02719  37 YEIRQELREKFNDPKLRFFIVPVIGDVRDRERLERAMEQYGVDVVFHAAAYKHVPLVEYNPMEAIKTNVLGTENVADAAI 116
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129980    94 EVGA-WVIHYSTDyvfpgngdmpwletDATAPLNVYGETKLAGEKALQEYCAKHLIFRT 151
Cdd:pfam02719 117 EAGVkKFVLISTD--------------KAVNPTNVMGATKRLAEKLFQAANRESGSGGT 161
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
3-269 1.64e-06

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


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 48.47  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGkTGQVGWELQRALAPLGnliaFDVHST------DYCGDFSNPEGVA----ETVRSIRPDIIVNAAAHTAVDKAES 72
Cdd:cd05266   1 VLILG-CGYLGQRLARQLLAQG----WQVTGTtrspekLAADRPAGVTPLAadltQPGLLADVDHLVISLPPPAGSYRGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  73 EPEFAQLInatsVEAIAKAANEVgaWVIHYSTDYVFPG-NGDmpWL-ETDATAPLNVYGETKLAGEKALQEYCAKHL-IF 149
Cdd:cd05266  76 YDPGLRAL----LDALAQLPAVQ--RVIYLSSTGVYGDqQGE--WVdETSPPNPSTESGRALLEAEQALLALGSKPTtIL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 150 RTSWVYAGK---GNNFAKTMLRLAKEREELAVINdqfgaptgaelLADCtAHAIRVALNKPDVAGLYHLVASGTTT---W 223
Cdd:cd05266 148 RLAGIYGPGrhpLRRLAQGTGRPPAGNAPTNRIH-----------VDDL-VGALAFALQRPAPGPVYNVVDDLPVTrgeF 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 16129980 224 YDYAalvfeeARKAGIPLALNklnavPTTAYPTPARRPHNSRLNTE 269
Cdd:cd05266 216 YQAA------AELLGLPPPPF-----IPFAFLREGKRVSNDRLKAE 250
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
3-145 3.25e-06

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: 47.61  E-value: 3.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALAPLG--NLIAFD-----------------VHSTD--YCGDFSNPEGVAETVRSIRPDIIVNA 61
Cdd:cd05237   5 ILVTGGAGSIGSELVRQILKFGpkKLIVFDrdenklhelvrelrsrfPHDKLrfIIGDVRDKERLRRAFKERGPDIVFHA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  62 AAHTAVDKAESEPEFAQLINATSVEAIAKAANEVG-AWVIHYSTDyvfpgngdmpwletDATAPLNVYGETKLAGEK--- 137
Cdd:cd05237  85 AALKHVPSMEDNPEEAIKTNVLGTKNVIDAAIENGvEKFVCISTD--------------KAVNPVNVMGATKRVAEKlll 150

                ....*...
gi 16129980 138 ALQEYCAK 145
Cdd:cd05237 151 AKNEYSSS 158
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
2-181 7.25e-06

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: 46.52  E-value: 7.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLGN-LIAFDVHST----DYCGDFSNPE---------GVAETVRSIRPDIIVNAAAHTAV 67
Cdd:cd05234   1 RILVTGGAGFIGSHLVDRLLEEGNeVVVVDNLSSgrreNIEPEFENKAfrfvkrdllDTADKVAKKDGDTVFHLAANPDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  68 DKAESEPEFAQLINATSVEAIAKAANEVGA-WVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKH 146
Cdd:cd05234  81 RLGATDPDIDLEENVLATYNVLEAMRANGVkRIVFASSSTVYGEAKVIPTPEDYPPLPISVYGASKLAAEALISAYAHLF 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16129980 147 ----LIFR-TSWVyaGKGNN------FaktMLRLAKEREELAVIND 181
Cdd:cd05234 161 gfqaWIFRfANIV--GPRSThgviydF---INKLKRNPNELEVLGD 201
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
36-150 9.79e-06

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


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 46.16  E-value: 9.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  36 YCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVdkAES--EPE--FAQliNATSVEAIAKAANEVGAW-VIHYSTDYVFpG 110
Cdd:COG1087  48 VEGDLRDRAALDRVFAEHDIDAVIHFAALKAV--GESveKPLkyYRN--NVVGTLNLLEAMREAGVKrFVFSSSAAVY-G 122
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 16129980 111 NGD-MPWLETDATAPLNVYGETKLAGEKALQEYCA----KHLIFR 150
Cdd:COG1087 123 EPEsVPITEDAPTNPTNPYGRSKLMVEQILRDLARayglRYVALR 167
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
56-150 1.40e-05

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


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 45.58  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  56 DIIVNAAAHTAVDKAESEpefAQLINATSVEAIAKAANEVGAWVIHY-STDYVFPGNGDMPWLETDATAPL----NVYGE 130
Cdd:COG3320  89 DAIVHLAALVNLVAPYSE---LRAVNVLGTREVLRLAATGRLKPFHYvSTIAVAGPADRSGVFEEDDLDEGqgfaNGYEQ 165
                        90       100
                ....*....|....*....|...
gi 16129980 131 TKLAGEKALQEYCAKHL---IFR 150
Cdd:COG3320 166 SKWVAEKLVREARERGLpvtIYR 188
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
2-146 1.44e-05

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: 45.77  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLG-NLIAFDVHSTDYC----------GDFSNPEGVAETVRSIrpDIIVNAAAHTAVDKA 70
Cdd:cd05264   1 RVLIVGGNGFIGSHLVDALLEEGpQVRVFDRSIPPYElplggvdyikGDYENRADLESALVGI--DTVIHLASTTNPATS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  71 ESEP--EFAQLINATS--VEAIAKAANEVgawVIHYSTDYVFPGNGD-MPWLETDATAPLNVYGETKLAGEKALQEYCAK 145
Cdd:cd05264  79 NKNPilDIQTNVAPTVqlLEACAAAGIGK---IIFASSGGTVYGVPEqLPISESDPTLPISSYGISKLAIEKYLRLYQYL 155

                .
gi 16129980 146 H 146
Cdd:cd05264 156 Y 156
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
1-223 1.80e-05

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


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 44.97  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   1 MNILLFGKTGQVGWELQRALAPLG----------NLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDkA 70
Cdd:cd05265   1 MKILIIGGTRFIGKALVEELLAAGhdvtvfnrgrTKPDLPEGVEHIVGDRNDRDALEELLGGEDFDVVVDTIAYTPRQ-V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  71 ES-----EPEFAQLINATSVEAIAKAANEVGAWVIHystdyvfpGNGDMPWLETDATaplnvYGETKLAGEKALQEYCA- 144
Cdd:cd05265  80 ERaldafKGRVKQYIFISSASVYLKPGRVITESTPL--------REPDAVGLSDPWD-----YGRGKRAAEDVLIEAAAf 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980 145 KHLIFRTSWVYaGKGNNFAKT---MLRLAKeREELAVIND-----QFGapTGAELladctAHAI-RVALNKPDVAGLYHL 215
Cdd:cd05265 147 PYTIVRPPYIY-GPGDYTGRLayfFDRLAR-GRPILVPGDghslvQFI--HVKDL-----ARALlGAAGNPKAIGGIFNI 217

                ....*...
gi 16129980 216 VASGTTTW 223
Cdd:cd05265 218 TGDEAVTW 225
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
3-159 1.20e-04

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: 43.04  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALA--------------PLGNLIAFDVHSTDycGDFSNPEGVAETVRSIrpDIIVNAAAHTAVd 68
Cdd:cd05228   1 ILVTGATGFLGSNLVRALLaqgyrvralvrsgsDAVLLDGLPVEVVE--GDLTDAASLAAAMKGC--DRVFHLAAFTSL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  69 kaesEPEFAQLINATSVEA---IAKAANEVGAW-VIHYSTDYVFPGNGDMPWLET---DATAPLNVYGETKLAGEKALQE 141
Cdd:cd05228  76 ----WAKDRKELYRTNVEGtrnVLDAALEAGVRrVVHTSSIAALGGPPDGRIDETtpwNERPFPNDYYRSKLLAELEVLE 151
                       170       180
                ....*....|....*....|.
gi 16129980 142 YCAKHL---IFRTSWVYaGKG 159
Cdd:cd05228 152 AAAEGLdvvIVNPSAVF-GPG 171
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
1-159 1.57e-04

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


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 42.34  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   1 MNILLFGKTGQVGWELQRALAPLGNLIAFDVHstdycgDFSNPEGVAETVRSIrpDIIVNAAAhtaVDKAESEPEFaQLI 80
Cdd:cd05261   1 MKILITGAKGFIGKNLIARLKEQKDDDIFFYD------RESDESELDDFLQGA--DFIFHLAG---VNRPKDEAEF-ESG 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  81 NATSVEAIAKAANEVGAWV-IHYSTdyvfpgngdmpwlETDATAPlNVYGETKLAGEKALQEYCAKH----LIFRTSWVY 155
Cdd:cd05261  69 NVGLTERLLDALTRNGKKPpILLSS-------------SIQAALD-NPYGKSKLAAEELLQEYARETgapvYIYRLPNVF 134

                ....
gi 16129980 156 aGKG 159
Cdd:cd05261 135 -GKW 137
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
2-136 2.44e-04

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


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 42.20  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   2 NILLFGKTGQVGWELQRALAPLGnliaFDVH---------STDYC--------------GDFSNPEGVAETVRSIRPDII 58
Cdd:cd05260   1 RALITGITGQDGSYLAEFLLEKG----YEVHgivrrsssfNTDRIdhlyinkdritlhyGDLTDSSSLRRAIEKVRPDEI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  59 VNAAAHTAVDKAESEPEFAQLINATSV----EAIAKAAneVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLA 134
Cdd:cd05260  77 YHLAAQSHVKVSFDDPEYTAEVNAVGTlnllEAIRILG--LDARFYQASSSEEYGKVQELPQSETTPFRPRSPYAVSKLY 154

                ..
gi 16129980 135 GE 136
Cdd:cd05260 155 AD 156
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
1-155 3.63e-04

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: 41.51  E-value: 3.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   1 MNILLFGKTGQVGWELQRALAPLGN-LIAFD-------------------------VHstdycGDFSNPEGVAETVRsiR 54
Cdd:cd05258   1 MRVLITGGAGFIGSNLARFFLKQGWeVIGFDnlmrrgsfgnlawlkanredggvrfVH-----GDIRNRNDLEDLFE--D 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  55 PDIIVNAAAHTAVDKAESEPEFAQLINATS----VEAIAKAANEvgAWVIHYSTDYVFpgnGDMPW---LETDATA---- 123
Cdd:cd05258  74 IDLIIHTAAQPSVTTSASSPRLDFETNALGtlnvLEAARQHAPN--APFIFTSTNKVY---GDLPNylpLEELETRyela 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16129980 124 -------------PLNV----YGETKLAGEKALQEYCA----KHLIFRTSWVY 155
Cdd:cd05258 149 pegwspagisesfPLDFshslYGASKGAADQYVQEYGRifglKTVVFRCGCLT 201
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
3-150 5.69e-04

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


Pssm-ID: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 40.76  E-value: 5.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   3 ILLFGKTGQVGWELQRALAPL---GNLIAFD--------VHSTDY----CGDFSNPEgvaETVRSIRPDIIVN-AAAHTA 66
Cdd:cd05272   2 ILITGGLGQIGSELAKLLRKRygkDNVIASDirkppahvVLSGPFeyldVLDFKSLE---EIVVNHKITWIIHlAALLSA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  67 VdkAESEPEFAQLINATSVEAIAKAANEVGAWVIHYSTDYVF-PGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAK 145
Cdd:cd05272  79 V--GEKNPPLAWDVNMNGLHNVLELAREHNLRIFVPSTIGAFgPTTPRNNTPDDTIQRPRTIYGVSKVAAELLGEYYHHK 156

                ....*.
gi 16129980 146 H-LIFR 150
Cdd:cd05272 157 FgVDFR 162
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
1-136 6.17e-04

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: 40.78  E-value: 6.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980   1 MNILLFGKTGQVGWELQRALAPLGN-LIAFDVhSTDYC----------------------GDFSNPEGVAETVRSIRPDI 57
Cdd:cd05253   1 MKILVTGAAGFIGFHVAKRLLERGDeVVGIDN-LNDYYdvrlkearlellgksggfkfvkGDLEDREALRRLFKDHEFDA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  58 IVNAAAHTAVDKAESEPEFAQLINATSVEAIAKAANEVGawVIHY---STDYVFPGNGDMPWLETDATA-PLNVYGETKL 133
Cdd:cd05253  80 VIHLAAQAGVRYSLENPHAYVDSNIVGFLNLLELCRHFG--VKHLvyaSSSSVYGLNTKMPFSEDDRVDhPISLYAATKK 157

                ...
gi 16129980 134 AGE 136
Cdd:cd05253 158 ANE 160
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
36-150 1.62e-03

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: 39.56  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  36 YCGDFSNPE-GVAETV---RSIRPDIIVNAAA--HTAVDKAESEPEfaqliNATSVEAIAKAANEVGAWVIHY-STDYVF 108
Cdd:cd05235  67 VVGDLSKPNlGLSDDDyqeLAEEVDVIIHNGAnvNWVYPYEELKPA-----NVLGTKELLKLAATGKLKPLHFvSTLSVF 141
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129980 109 PGNGDMPWLETDATAPL-------NVYGETKLAGEKALQEYCAKHL---IFR 150
Cdd:cd05235 142 SAEEYNALDDEESDDMLesqnglpNGYIQSKWVAEKLLREAANRGLpvaIIR 193
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
38-143 5.04e-03

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: 37.97  E-value: 5.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129980  38 GDFSNPEGVAETVRsiRPDIIVNAAAHTAVDKAESEPEFAQLINATSVEAIAKAANEVGAW-VIHYSTDYVFPGNGDMPW 116
Cdd:cd05256  52 GDIRDDELVEFAFE--GVDYVFHQAAQASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVKrFVYASSSSVYGDPPYLPK 129
                        90       100
                ....*....|....*....|....*..
gi 16129980 117 LETDATAPLNVYGETKLAGEKALQEYC 143
Cdd:cd05256 130 DEDHPPNPLSPYAVSKYAGELYCQVFA 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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