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Conserved domains on  [gi|1929626784|gb|QPA17463|]
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dTDP-glucose 4,6-dehydratase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

dTDP-glucose 4,6-dehydratase( domain architecture ID 11484613)

dTDP-glucose 4,6-dehydratase catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration, and reduction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
1-355 0e+00

dTDP-glucose 4,6-dehydratase; Provisional


:

Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 806.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
Cdd:PRK10217    1 MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY 160
Cdd:PRK10217   81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA 240
Cdd:PRK10217  161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKPLPVYGNGQQIRDWLYVEDHARALYCVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 241 TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHGVAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
Cdd:PRK10217  241 TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPQGVAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1929626784 321 ESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG 355
Cdd:PRK10217  321 ESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG 355
 
Name Accession Description Interval E-value
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
1-355 0e+00

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 806.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
Cdd:PRK10217    1 MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY 160
Cdd:PRK10217   81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA 240
Cdd:PRK10217  161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKPLPVYGNGQQIRDWLYVEDHARALYCVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 241 TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHGVAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
Cdd:PRK10217  241 TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPQGVAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1929626784 321 ESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG 355
Cdd:PRK10217  321 ESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG 355
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
1-351 0e+00

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


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 666.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIINETSDA-VVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVM 79
Cdd:COG1088     1 MMRILVTGGAGFIGSNFVRYLLAKYPGAeVVVLDKLTYAGNLENLADLEDDPRYRFVKGDIRDRELVDELFAEHGPDAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  80 HLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkksAFRFHHISTDEVYGDLHsTDDFFTETTPYAPSSP 159
Cdd:COG1088    81 HFAAESHVDRSIDDPAAFVETNVVGTFNLLEAARKYWVE-------GFRFHHVSTDEVYGSLG-EDGPFTETTPLDPSSP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCV 239
Cdd:COG1088   153 YSASKAASDHLVRAYHRTYGLPVVITRCSNNYGPYQFPEKLIPLFITNALEGKPLPVYGDGKQVRDWLYVEDHCRAIDLV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 240 ATTGKVGETYNIGGHNERKNLDVVETICELLEElapnkphgvahYRDLITFVADRPGHDLRYAIDASKIARELGWLPQET 319
Cdd:COG1088   233 LEKGRPGETYNIGGGNELSNLEVVELICDLLGK-----------PESLITFVKDRPGHDRRYAIDASKIRRELGWKPKVT 301
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1929626784 320 FESGMRKTVQWYLANESWWKQVQDGSYQGERL 351
Cdd:COG1088   302 FEEGLRKTVDWYLDNRDWWEPLKSGAYREERY 333
dTDP_gluc_dehyt TIGR01181
dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and ...
3-338 0e+00

dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and likewise has an NAD cofactor. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273489 [Multi-domain]  Cd Length: 317  Bit Score: 608.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDA-VVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHL 81
Cdd:TIGR01181   1 RILVTGGAGFIGSNFVRYILNEHPDAeVIVLDKLTYAGNLENLADLEDNPRYRFVKGDIGDRELVSRLFTEHQPDAVVHF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkksaFRFHHISTDEVYGDLHSTDdFFTETTPYAPSSPYS 161
Cdd:TIGR01181  81 AAESHVDRSISGPAAFIETNVVGTYTLLEAVRKYWHE--------FRFHHISTDEVYGDLEKGD-AFTETTPLAPSSPYS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 162 ASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVAT 241
Cdd:TIGR01181 152 ASKAASDHLVRAYHRTYGLPALITRCSNNYGPYQFPEKLIPLMITNALAGKPLPVYGDGQQVRDWLYVEDHCRAIYLVLE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 242 TGKVGETYNIGGHNERKNLDVVETICELLEElapnkphgvahYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETFE 321
Cdd:TIGR01181 232 KGRVGETYNIGGGNERTNLEVVETILELLGK-----------DEDLITHVEDRPGHDRRYAIDASKIKRELGWAPKYTFE 300
                         330
                  ....*....|....*..
gi 1929626784 322 SGMRKTVQWYLANESWW 338
Cdd:TIGR01181 301 EGLRKTVQWYLDNEWWW 317
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
2-336 0e+00

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: 576.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDA-VVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLNKYPDYkIINLDKLTYAGNLENLEDVSSSPRYRFVKGDICDAELVDRLFEEEKIDAVIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNaltedkksaFRFHHISTDEVYGDLHSTDDFfTETTPYAPSSPY 160
Cdd:cd05246    81 FAAESHVDRSISDPEPFIRTNVLGTYTLLEAARKYGV---------KRFVHISTDEVYGDLLDDGEF-TETSPLAPTSPY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA 240
Cdd:cd05246   151 SASKAAADLLVRAYHRTYGLPVVITRCSNNYGPYQFPEKLIPLFILNALDGKPLPIYGDGLNVRDWLYVEDHARAIELVL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 241 TTGKVGETYNIGGHNERKNLDVVETICELLEELapnkphgvahyRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
Cdd:cd05246   231 EKGRVGEIYNIGGGNELTNLELVKLILELLGKD-----------ESLITYVKDRPGHDRRYAIDSSKIRRELGWRPKVSF 299
                         330
                  ....*....|....*.
gi 1929626784 321 ESGMRKTVQWYLANES 336
Cdd:cd05246   300 EEGLRKTVRWYLENRW 315
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
5-327 2.80e-127

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 368.03  E-value: 2.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVVV--DKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVrrSSSFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQPDEIYNLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkkSAFRFHHISTDEVYGDLhsTDDFFTETTPYAPSSPYSA 162
Cdd:pfam16363  81 AQSHVDVSFEQPEYTADTNVLGTLRLLEAIRSLGLE------KKVRFYQASTSEVYGKV--QEVPQTETTPFYPRSPYAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGPYH---FPEKLIPLMILNALAGK-SLPVYGNGQQIRDWLYVEDHARAL-- 236
Cdd:pfam16363 153 AKLYADWIVVNYRESYGLFACNGILFNHESPRRgerFVTRKITRGVARIKLGKqEKLYLGNLDAKRDWGHARDYVEAMwl 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 237 ---------YCVATtgkvGETYNIGGHNERKNLDVVETIC-ELLEELAPNKPHGVAHYRdlITFVADRPGHDLRYAIDAS 306
Cdd:pfam16363 233 mlqqdkpddYVIAT----GETHTVREFVEKAFLELGLTITwEGKGEIGYFKASGKVHVL--IDPRYFRPGEVDRLLGDPS 306
                         330       340
                  ....*....|....*....|.
gi 1929626784 307 KIARELGWLPQETFESGMRKT 327
Cdd:pfam16363 307 KAKEELGWKPKVSFEELVREM 327
 
Name Accession Description Interval E-value
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
1-355 0e+00

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 806.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
Cdd:PRK10217    1 MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY 160
Cdd:PRK10217   81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA 240
Cdd:PRK10217  161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKPLPVYGNGQQIRDWLYVEDHARALYCVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 241 TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHGVAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
Cdd:PRK10217  241 TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPQGVAHYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1929626784 321 ESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG 355
Cdd:PRK10217  321 ESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG 355
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
3-347 0e+00

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 672.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:PRK10084    2 KILVTGGAGFIGSAVVRHIINNTQDSVVNVDKLTYAGNLESLADVSDSERYVFEHADICDRAELDRIFAQHQPDAVMHLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKSAFRFHHISTDEVYGDLHSTDD--------FFTETTPY 154
Cdd:PRK10084   82 AESHVDRSITGPAAFIETNIVGTYVLLEAARNYWSALDEDKKNAFRFHHISTDEVYGDLPHPDEvenseelpLFTETTAY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 155 APSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHAR 234
Cdd:PRK10084  162 APSSPYSASKASSDHLVRAWLRTYGLPTIVTNCSNNYGPYHFPEKLIPLVILNALEGKPLPIYGKGDQIRDWLYVEDHAR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 235 ALYCVATTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKphgvAHYRDLITFVADRPGHDLRYAIDASKIARELGW 314
Cdd:PRK10084  242 ALYKVVTEGKAGETYNIGGHNEKKNLDVVLTICDLLDEIVPKA----TSYREQITYVADRPGHDRRYAIDASKISRELGW 317
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1929626784 315 LPQETFESGMRKTVQWYLANESWWKQVQDGSYQ 347
Cdd:PRK10084  318 KPQETFESGIRKTVEWYLANTEWVQNVKSGAYQ 350
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
1-351 0e+00

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


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 666.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIINETSDA-VVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVM 79
Cdd:COG1088     1 MMRILVTGGAGFIGSNFVRYLLAKYPGAeVVVLDKLTYAGNLENLADLEDDPRYRFVKGDIRDRELVDELFAEHGPDAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  80 HLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkksAFRFHHISTDEVYGDLHsTDDFFTETTPYAPSSP 159
Cdd:COG1088    81 HFAAESHVDRSIDDPAAFVETNVVGTFNLLEAARKYWVE-------GFRFHHVSTDEVYGSLG-EDGPFTETTPLDPSSP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCV 239
Cdd:COG1088   153 YSASKAASDHLVRAYHRTYGLPVVITRCSNNYGPYQFPEKLIPLFITNALEGKPLPVYGDGKQVRDWLYVEDHCRAIDLV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 240 ATTGKVGETYNIGGHNERKNLDVVETICELLEElapnkphgvahYRDLITFVADRPGHDLRYAIDASKIARELGWLPQET 319
Cdd:COG1088   233 LEKGRPGETYNIGGGNELSNLEVVELICDLLGK-----------PESLITFVKDRPGHDRRYAIDASKIRRELGWKPKVT 301
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1929626784 320 FESGMRKTVQWYLANESWWKQVQDGSYQGERL 351
Cdd:COG1088   302 FEEGLRKTVDWYLDNRDWWEPLKSGAYREERY 333
dTDP_gluc_dehyt TIGR01181
dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and ...
3-338 0e+00

dTDP-glucose 4,6-dehydratase; This protein is related to UDP-glucose 4-epimerase (GalE) and likewise has an NAD cofactor. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273489 [Multi-domain]  Cd Length: 317  Bit Score: 608.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDA-VVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHL 81
Cdd:TIGR01181   1 RILVTGGAGFIGSNFVRYILNEHPDAeVIVLDKLTYAGNLENLADLEDNPRYRFVKGDIGDRELVSRLFTEHQPDAVVHF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkksaFRFHHISTDEVYGDLHSTDdFFTETTPYAPSSPYS 161
Cdd:TIGR01181  81 AAESHVDRSISGPAAFIETNVVGTYTLLEAVRKYWHE--------FRFHHISTDEVYGDLEKGD-AFTETTPLAPSSPYS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 162 ASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVAT 241
Cdd:TIGR01181 152 ASKAASDHLVRAYHRTYGLPALITRCSNNYGPYQFPEKLIPLMITNALAGKPLPVYGDGQQVRDWLYVEDHCRAIYLVLE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 242 TGKVGETYNIGGHNERKNLDVVETICELLEElapnkphgvahYRDLITFVADRPGHDLRYAIDASKIARELGWLPQETFE 321
Cdd:TIGR01181 232 KGRVGETYNIGGGNERTNLEVVETILELLGK-----------DEDLITHVEDRPGHDRRYAIDASKIKRELGWAPKYTFE 300
                         330
                  ....*....|....*..
gi 1929626784 322 SGMRKTVQWYLANESWW 338
Cdd:TIGR01181 301 EGLRKTVQWYLDNEWWW 317
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
2-336 0e+00

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: 576.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDA-VVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLNKYPDYkIINLDKLTYAGNLENLEDVSSSPRYRFVKGDICDAELVDRLFEEEKIDAVIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNaltedkksaFRFHHISTDEVYGDLHSTDDFfTETTPYAPSSPY 160
Cdd:cd05246    81 FAAESHVDRSISDPEPFIRTNVLGTYTLLEAARKYGV---------KRFVHISTDEVYGDLLDDGEF-TETSPLAPTSPY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA 240
Cdd:cd05246   151 SASKAAADLLVRAYHRTYGLPVVITRCSNNYGPYQFPEKLIPLFILNALDGKPLPIYGDGLNVRDWLYVEDHARAIELVL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 241 TTGKVGETYNIGGHNERKNLDVVETICELLEELapnkphgvahyRDLITFVADRPGHDLRYAIDASKIARELGWLPQETF 320
Cdd:cd05246   231 EKGRVGEIYNIGGGNELTNLELVKLILELLGKD-----------ESLITYVKDRPGHDRRYAIDSSKIRRELGWRPKVSF 299
                         330
                  ....*....|....*.
gi 1929626784 321 ESGMRKTVQWYLANES 336
Cdd:cd05246   300 EEGLRKTVRWYLENRW 315
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
5-327 2.80e-127

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 368.03  E-value: 2.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVVV--DKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVrrSSSFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQPDEIYNLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkkSAFRFHHISTDEVYGDLhsTDDFFTETTPYAPSSPYSA 162
Cdd:pfam16363  81 AQSHVDVSFEQPEYTADTNVLGTLRLLEAIRSLGLE------KKVRFYQASTSEVYGKV--QEVPQTETTPFYPRSPYAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGPYH---FPEKLIPLMILNALAGK-SLPVYGNGQQIRDWLYVEDHARAL-- 236
Cdd:pfam16363 153 AKLYADWIVVNYRESYGLFACNGILFNHESPRRgerFVTRKITRGVARIKLGKqEKLYLGNLDAKRDWGHARDYVEAMwl 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 237 ---------YCVATtgkvGETYNIGGHNERKNLDVVETIC-ELLEELAPNKPHGVAHYRdlITFVADRPGHDLRYAIDAS 306
Cdd:pfam16363 233 mlqqdkpddYVIAT----GETHTVREFVEKAFLELGLTITwEGKGEIGYFKASGKVHVL--IDPRYFRPGEVDRLLGDPS 306
                         330       340
                  ....*....|....*....|.
gi 1929626784 307 KIARELGWLPQETFESGMRKT 327
Cdd:pfam16363 307 KAKEELGWKPKVSFEELVREM 327
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
2-341 4.91e-93

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 291.26  E-value: 4.91e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALV-RYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH 80
Cdd:PLN02260    7 KNILITGAAGFIASHVAnRLIRNYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASADLVNYLLITEGIDTIMH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARaywnaLTEDKKsafRFHHISTDEVYGDlhsTDDFFTETTPYA----P 156
Cdd:PLN02260   87 FAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACK-----VTGQIR---RFIHVSTDEVYGE---TDEDADVGNHEAsqllP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 157 SSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARAL 236
Cdd:PLN02260  156 TNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMQGKPLPIHGDGSNVRSYLYCEDVAEAF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 237 YCVATTGKVGETYNIGGHNERKNLDVVETICELLeELAPNKphgvahyrdLITFVADRPGHDLRYAIDASKIaRELGWLP 316
Cdd:PLN02260  236 EVVLHKGEVGHVYNIGTKKERRVIDVAKDICKLF-GLDPEK---------SIKFVENRPFNDQRYFLDDQKL-KKLGWQE 304
                         330       340
                  ....*....|....*....|....*
gi 1929626784 317 QETFESGMRKTVQWYLANESWWKQV 341
Cdd:PLN02260  305 RTSWEEGLKKTMEWYTSNPDWWGDV 329
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
4-252 7.32e-87

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: 261.85  E-value: 7.32e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDaVVVVDKLTYAGNLMSLAPVAqserfaFEKVDICDRAELARVFTEHQPDCVMHLAA 83
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYE-VIGLDRLTSASNTARLADLR------FVEGDLTDRDALEKLLADVRPDAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDEVYGDLHST-DDFFTETTPYAPSSPYSA 162
Cdd:pfam01370  74 VGGVGASIEDPEDFIEANVLGTLNLLEAARKA---------GVKRFLFASSSEVYGDGAEIpQEETTLTGPLAPNSPYAA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGPY---HFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCV 239
Cdd:pfam01370 145 AKLAGEWLVLAYAAAYGLRAVILRLFNVYGPGdneGFVSRVIPALIRRILEGKPILLWGDGTQRRDFLYVDDVARAILLA 224
                         250
                  ....*....|....
gi 1929626784 240 ATTGKV-GETYNIG 252
Cdd:pfam01370 225 LEHGAVkGEIYNIG 238
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
3-333 1.10e-76

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 237.95  E-value: 1.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLmslapvAQSERFAFEKVDICDRAELARVFteHQPDCVMHLA 82
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANL------AALPGVEFVRGDLRDPEALAAAL--AGVDAVVHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDrsIDGPAAFIETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDEVYGDlhsTDDFFTETTPYAPSSPYSA 162
Cdd:COG0451    73 APAGVG--EEDPDETLEVNVEGTLNLLEAARAA---------GVKRFVYASSSSVYGD---GEGPIDEDTPLRPVSPYGA 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPekLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVATT 242
Cdd:COG0451   139 SKLAAELLARAYARRYGLPVTILRPGNVYGPGDRG--VLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEA 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 243 GK-VGETYNIGGHNERKNLDVVETICELLeelapNKPhgvahyrdlITFVADRPGHDLR-YAIDASKIARELGWLPQETF 320
Cdd:COG0451   217 PAaPGGVYNVGGGEPVTLRELAEAIAEAL-----GRP---------PEIVYPARPGDVRpRRADNSKARRELGWRPRTSL 282
                         330
                  ....*....|...
gi 1929626784 321 ESGMRKTVQWYLA 333
Cdd:COG0451   283 EEGLRETVAWYRA 295
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
3-331 5.74e-69

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: 218.24  E-value: 5.74e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIInETSDAVVVVDKLtYAGNLMSLAPVAqsERFAFEKVDICDRAELARVFTEhqPDCVMHLA 82
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLL-ERGHEVIVLDNL-STGKKENLPEVK--PNVKFIEGDIRDDELVEFAFEG--VDYVFHQA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltEDKksafRFHHISTDEVYGDlhsTDDF-FTETTPYAPSSPYS 161
Cdd:cd05256    75 AQASVPRSIEDPIKDHEVNVLGTLNLLEAARKA-----GVK----RFVYASSSSVYGD---PPYLpKDEDHPPNPLSPYA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 162 ASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEK----LIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALY 237
Cdd:cd05256   143 VSKYAGELYCQVFARLYGLPTVSLRYFNVYGPRQDPNGgyaaVIPIFIERALKGEPPTIYGDGEQTRDFTYVEDVVEANL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 238 CVATTGKVGETYNIGGHNERKNLDVVETICELLEELAPnkphgvahyrdlITFVADRPGHDLRYAIDASKIARELGWLPQ 317
Cdd:cd05256   223 LAATAGAGGEVYNIGTGKRTSVNELAELIREILGKELE------------PVYAPPRPGDVRHSLADISKAKKLLGWEPK 290
                         330
                  ....*....|....
gi 1929626784 318 ETFESGMRKTVQWY 331
Cdd:cd05256   291 VSFEEGLRLTVEWF 304
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
4-251 1.21e-65

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 205.83  E-value: 1.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDAVVVVDKLtyagnlmslapvaqserfafekvdicdraelarvftehqpDCVMHLAA 83
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRGSPKVLVVSRR----------------------------------------DVVVHNAA 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRSID----GPAAFIETNIVGTYTLLEAARAYWNaltedKKSAFRFHHISTDEVYGDlhstddfftettpYAPSSP 159
Cdd:cd02266    41 ILDDGRLIDltgsRIERAIRANVVGTRRLLEAARELMK-----AKRLGRFILISSVAGLFG-------------APGLGG 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHLVRAWLRTY---GLPTLITNCSNNYGPYHFPEKLIPLMILnalagkslpvyGNGQQIRDWLYVEDHARAL 236
Cdd:cd02266   103 YAASKAALDGLAQQWASEGwgnGLPATAVACGTWAGSGMAKGPVAPEEIL-----------GNRRHGVRTMPPEEVARAL 171
                         250
                  ....*....|....*
gi 1929626784 237 YCVATTGKVGETYNI 251
Cdd:cd02266   172 LNALDRPKAGVCYII 186
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
4-252 9.98e-61

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: 193.67  E-value: 9.98e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDaVVVVDKLtyagnlmslapvaqserfafekvdicdraelarvftehqpDCVMHLAA 83
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLERGHE-VVVIDRL----------------------------------------DVVVHLAA 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkksafRFHHISTDEVYGDLHSTDdfFTETTPYAPSSPYSAS 163
Cdd:cd08946    40 LVGVPASWDNPDEDFETNVVGTLNLLEAARKAGVK---------RFVYASSASVYGSPEGLP--EEEETPPRPLSPYGVS 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 164 KASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFP--EKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVAT 241
Cdd:cd08946   109 KLAAEHLLRSYGESYGLPVVILRLANVYGPGQRPrlDGVVNDFIRRALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALE 188
                         250
                  ....*....|..
gi 1929626784 242 TG-KVGETYNIG 252
Cdd:cd08946   189 NPlEGGGVYNIG 200
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
2-331 2.43e-56

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: 186.73  E-value: 2.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDaVVVVDKLT---YAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTehQPDCV 78
Cdd:cd05258     1 MRVLITGGAGFIGSNLARFFLKQGWE-VIGFDNLMrrgSFGNLAWLKANREDGGVRFVHGDIRNRNDLEDLFE--DIDLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  79 MHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnalteDKKSAFRFhhISTDEVYGDL----------------- 141
Cdd:cd05258    78 IHTAAQPSVTTSASSPRLDFETNALGTLNVLEAARQH------APNAPFIF--TSTNKVYGDLpnylpleeletryelap 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 142 -HSTDDFFTETTPYAPS-SPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKL---IPLMILNALAGKSLPV 216
Cdd:cd05258   150 eGWSPAGISESFPLDFShSLYGASKGAADQYVQEYGRIFGLKTVVFRCGCLTGPRQFGTEDqgwVAYFLKCAVTGKPLTI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 217 YGNG-QQIRDWLYVEDHARaLYCVATTGK---VGETYNIGG--HNerkNLDVVETIcELLEELAPNKPHgvahyrdlITF 290
Cdd:cd05258   230 FGYGgKQVRDVLHSADLVN-LYLRQFQNPdrrKGEVFNIGGgrEN---SVSLLELI-ALCEEITGRKME--------SYK 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1929626784 291 VADRPGhDLRYAI-DASKIARELGWLPQETFESGMRKTVQWY 331
Cdd:cd05258   297 DENRPG-DQIWYIsDIRKIKEKPGWKPERDPREILAEIYAWI 337
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
3-334 2.77e-50

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: 170.98  E-value: 2.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIInETSDAVVVVDKLT--YAGNLMS--LAPVAQSERFAFEKVDICDRAELARVFTEHQPDCV 78
Cdd:cd05253     2 KILVTGAAGFIGFHVAKRLL-ERGDEVVGIDNLNdyYDVRLKEarLELLGKSGGFKFVKGDLEDREALRRLFKDHEFDAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  79 MHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDEVYGDlhSTDDFFTETTPYA-PS 157
Cdd:cd05253    81 IHLAAQAGVRYSLENPHAYVDSNIVGFLNLLELCRHF---------GVKHLVYASSSSVYGL--NTKMPFSEDDRVDhPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 158 SPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHA---- 233
Cdd:cd05253   150 SLYAATKKANELMAHTYSHLYGIPTTGLRFFTVYGPWGRPDMALFLFTKAILEGKPIDVFNDGNMSRDFTYIDDIVegvv 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 234 RALYCVATTGKVG--------------ETYNIGGHNERKNLDVVETICELLeelapnkphGVAHYRDLITFvadRPGHDL 299
Cdd:cd05253   230 RALDTPAKPNPNWdaeapdpstssapyRVYNIGNNSPVKLMDFIEALEKAL---------GKKAKKNYLPM---QKGDVP 297
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1929626784 300 RYAIDASKIARELGWLPQETFESGMRKTVQWYLAN 334
Cdd:cd05253   298 ETYADISKLQRLLGYKPKTSLEEGVKRFVEWYKEN 332
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
3-334 1.35e-47

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


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 163.24  E-value: 1.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKLTyAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHqpDCVMHLA 82
Cdd:cd05257     1 NVLVTGADGFIGSHLTERLLREGHE-VRALDIYN-SFNSWGLLDNAVHDRFHFISGDVRDASEVEYLVKKC--DVVFHLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNAltedkksafRFHHISTDEVYGdlHSTDDFFTETTP----YAPSS 158
Cdd:cd05257    77 ALIAIPYSYTAPLSYVETNVFGTLNVLEAACVLYRK---------RVVHTSTSEVYG--TAQDVPIDEDHPllyiNKPRS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYC 238
Cdd:cd05257   146 PYSASKQGADRLAYSYGRSFGLPVTIIRPFNTYGPRQSARAVIPTIISQRAIGQRLINLGDGSPTRDFNFVKDTARGFID 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 239 VATTGK-VGETYNIGGHNE-----RKNLDVVEticELLEELAPNkphgvahYRDLITFvadRPGHD--LRYAIDASKIAR 310
Cdd:cd05257   226 ILDAIEaVGEIINNGSGEEisignPAVELIVE---ELGEMVLIV-------YDDHREY---RPGYSevERRIPDIRKAKR 292
                         330       340
                  ....*....|....*....|....
gi 1929626784 311 ELGWLPQETFESGMRKTVQWYLAN 334
Cdd:cd05257   293 LLGWEPKYSLRDGLRETIEWFKDQ 316
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
3-332 4.87e-46

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: 159.30  E-value: 4.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:cd05260     1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHLYINKDRITLHYGDLTDSSSLRRAIEKVRPDEIYHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARaywnalteDKKSAFRFHHISTDEVYGDLHSTDdfFTETTPYAPSSPYSA 162
Cdd:cd05260    81 AQSHVKVSFDDPEYTAEVNAVGTLNLLEAIR--------ILGLDARFYQASSSEEYGKVQELP--QSETTPFRPRSPYAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGPYH---FPEKLIPLMILNALAGKSLPVY-GNGQQIRDWLYVEDHARALYC 238
Cdd:cd05260   151 SKLYADWITRNYREAYGLFAVNGRLFNHEGPRRgetFVTRKITRQVARIKAGLQPVLKlGNLDAKRDWGDARDYVEAYWL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 239 VATTGKVGETYNIGGHNERknldvVETICEL-LEELAPNKPHGVAhyRDLITFvadRPGhDLRYAI-DASKIARELGWLP 316
Cdd:cd05260   231 LLQQGEPDDYVIATGETHS-----VREFVELaFEESGLTGDIEVE--IDPRYF---RPT-EVDLLLgDPSKAREELGWKP 299
                         330
                  ....*....|....*.
gi 1929626784 317 QETFESGMRKTVQWYL 332
Cdd:cd05260   300 EVSFEELVREMLDADL 315
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
3-334 2.84e-45

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


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 157.49  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKLTYaGNLMSLApvaqsERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:COG1087     2 KILVTGGAGYIGSHTVVALLEAGHE-VVVLDNLSN-GHREAVP-----KGVPFVEGDLRDRAALDRVFAEHDIDAVIHFA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnalteDKKsafRFHHISTDEVYGDlhSTDDFFTETTPYAPSSPYSA 162
Cdd:COG1087    75 ALKAVGESVEKPLKYYRNNVVGTLNLLEAMREA------GVK---RFVFSSSAAVYGE--PESVPITEDAPTNPTNPYGR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGL--------------PtlitncSNNYGPYHFPEK-LIPLmILNALAGK--SLPVYGN------ 219
Cdd:COG1087   144 SKLMVEQILRDLARAYGLryvalryfnpagahP------SGRIGEDHGPPThLIPL-VLQVALGKreKLSVFGDdyptpd 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 220 GQQIRDWLYVED----HARALYCVATTGKVgETYNIG---GHNerkNLDVVETICElleelapnkphgvAHYRDL-ITFV 291
Cdd:COG1087   217 GTCVRDYIHVVDladaHVLALEYLLAGGGS-EVFNLGtgrGYS---VLEVIDAFER-------------VTGRPIpYEIA 279
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1929626784 292 ADRPGhDLR--YAiDASKIARELGWLPQETFESGMRKTVQWYLAN 334
Cdd:COG1087   280 PRRPG-DPAalVA-DSEKARRELGWKPKYDLEDIIADAWRWQQKN 322
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
3-330 1.04e-44

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: 155.55  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSdAVVVVDkltyagnlMSLAPVAQSE-RFAFEKVDICDRAELARVFteHQPDCVMHL 81
Cdd:cd05264     1 RVLIVGGNGFIGSHLVDALLEEGP-QVRVFD--------RSIPPYELPLgGVDYIKGDYENRADLESAL--VGIDTVIHL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAARaywnaltEDKKSAFRFhhISTD-EVYGDLHSTDdfFTETTPYAPSSPY 160
Cdd:cd05264    70 ASTTNPATSNKNPILDIQTNVAPTVQLLEACA-------AAGIGKIIF--ASSGgTVYGVPEQLP--ISESDPTLPISSY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEK---LIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALY 237
Cdd:cd05264   139 GISKLAIEKYLRLYQYLYGLDYTVLRISNPYGPGQRPDGkqgVIPIALNKILRGEPIEIWGDGESIRDYIYIDDLVEALM 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 238 CVATTGKVGETYNIG-GHNerknldvvETICELLEELapNKPHGvahyRDLITFVADRPGHDLRYAI-DASKIARELGWL 315
Cdd:cd05264   219 ALLRSKGLEEVFNIGsGIG--------YSLAELIAEI--EKVTG----RSVQVIYTPARTTDVPKIVlDISRARAELGWS 284
                         330
                  ....*....|....*
gi 1929626784 316 PQETFESGMRKTVQW 330
Cdd:cd05264   285 PKISLEDGLEKTWQW 299
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-331 2.04e-44

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


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 155.39  E-value: 2.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKLTyAGNLMSLAPVAQsERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:cd05247     1 KVLVTGGAGYIGSHTVVELLEAGYD-VVVLDNLS-NGHREALPRIEK-IRIEFYEGDIRDRAALDKVFAEHKIDAVIHFA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedKKSAFRFHhiSTDEVYGDLHSTDdfFTETTPYAPSSPYSA 162
Cdd:cd05247    78 ALKAVGESVQKPLKYYDNNVVGTLNLLEAMRAH-------GVKNFVFS--SSAAVYGEPETVP--ITEEAPLNPTNPYGR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLI--------TNCSNNYGPYHFPEK-LIPLmILNALAGK--SLPVYGN------GQQIRD 225
Cdd:cd05247   147 TKLMVEQILRDLAKAPGLNYVIlryfnpagAHPSGLIGEDPQIPNnLIPY-VLQVALGRreKLAIFGDdyptpdGTCVRD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 226 WLYVED----HARALYCVATTGKVgETYNIGGHNERKNLDVVETICElleelapnkphgvAHYRDL-ITFVADRPGHDLR 300
Cdd:cd05247   226 YIHVVDladaHVLALEKLENGGGS-EIYNLGTGRGYSVLEVVEAFEK-------------VSGKPIpYEIAPRRAGDPAS 291
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1929626784 301 YAIDASKIARELGWLPQETFESGMRKTVQWY 331
Cdd:cd05247   292 LVADPSKAREELGWKPKRDLEDMCEDAWNWQ 322
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
2-331 1.11e-40

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


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 145.09  E-value: 1.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDaVVVVDKLtYAGNLMSLAPVAQSERFAFEKVDICDraelarvFTEHQPDCVMHL 81
Cdd:cd05230     1 KRILITGGAGFLGSHLCDRLLEDGHE-VICVDNF-FTGRKRNIEHLIGHPNFEFIRHDVTE-------PLYLEVDQIYHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAAraywnaltedKKSAFRFHHISTDEVYGD--LHST-DDFFTETTPYAPSS 158
Cdd:cd05230    72 ACPASPVHYQYNPIKTLKTNVLGTLNMLGLA----------KRVGARVLLASTSEVYGDpeVHPQpESYWGNVNPIGPRS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPE--KLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARAL 236
Cdd:cd05230   142 CYDEGKRVAETLCMAYHRQHGVDVRIARIFNTYGPRMHPNdgRVVSNFIVQALRGEPITVYGDGTQTRSFQYVSDLVEGL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 237 YCVATTGKVGETYNIGGHNERKNLDVVETICELleeLAPNKPhgvahyrdlITFVADRPGHDLRYAIDASKIARELGWLP 316
Cdd:cd05230   222 IRLMNSDYFGGPVNLGNPEEFTILELAELVKKL---TGSKSE---------IVFLPLPEDDPKRRRPDISKAKELLGWEP 289
                         330
                  ....*....|....*
gi 1929626784 317 QETFESGMRKTVQWY 331
Cdd:cd05230   290 KVPLEEGLRRTIEYF 304
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
2-331 9.23e-38

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


Pssm-ID: 187562 [Multi-domain]  Cd Length: 336  Bit Score: 137.83  E-value: 9.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQseRFAFEKVDICDRAELARVFTEHQPDCVMHL 81
Cdd:cd05252     5 KRVLVTGHTGFKGSWLSLWLQELGAKVIGYSLDPPTNPNLFELANLDN--KISSTRGDIRDLNALREAIREYEPEIVFHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAARAywnaltedKKSAFRFHHISTDEVYGDLHSTDDfFTETTPYAPSSPYS 161
Cdd:cd05252    83 AAQPLVRLSYKDPVETFETNVMGTVNLLEAIRE--------TGSVKAVVNVTSDKCYENKEWGWG-YRENDPLGGHDPYS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 162 ASKASSDHLVRAWLRTYGLPTL---------ITNCSNNYGPYHFPE-KLIPlMILNALAGKSLPVYGNGQQIRDWLYVED 231
Cdd:cd05252   154 SSKGCAELIISSYRNSFFNPENygkhgiaiaSARAGNVIGGGDWAEdRIVP-DCIRAFEAGERVIIRNPNAIRPWQHVLE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 232 HARALYCVAT-----TGKVGETYNIGGHNERKN--LDVVETICELLEELAPNKPHGVAHyrdlitfvadrpGHDLRYA-I 303
Cdd:cd05252   233 PLSGYLLLAEklyerGEEYAEAWNFGPDDEDAVtvLELVEAMARYWGEDARWDLDGNSH------------PHEANLLkL 300
                         330       340
                  ....*....|....*....|....*...
gi 1929626784 304 DASKIARELGWLPQETFESGMRKTVQWY 331
Cdd:cd05252   301 DCSKAKTMLGWRPRWNLEETLEFTVAWY 328
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
4-251 1.97e-37

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: 132.53  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDaVVVVDKLTYAGNLMSLAPVAQSErfafekvdICDRAELARVFTEHQPDCVMHLAA 83
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHE-VTLLVRNTKRLSKEDQEPVAVVE--------GDLRDLDSLSDAVQGVDVVIHLAG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRsidgpaAFIETNIVGTYTLLEAARAYWnaltedkksAFRFHHISTDEVYGDLHstddfftETTPYAPSSPYSAS 163
Cdd:cd05226    72 APRDTR------DFCEVDVEGTRNVLEAAKEAG---------VKHFIFISSLGAYGDLH-------EETEPSPSSPYLAV 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 164 KASSDHLVRAWlrtyGLPTLITNCSNNYGpyhfpekliplmilnalagkslpvygngqqirdwlyveDHARALYCVATT- 242
Cdd:cd05226   130 KAKTEAVLREA----SLPYTIVRPGVIYG--------------------------------------DLARAIANAVVTp 167

                  ....*....
gi 1929626784 243 GKVGETYNI 251
Cdd:cd05226   168 GKKNETFNA 176
EDH_00030 TIGR04180
NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family; This clade within the NAD ...
4-317 2.88e-36

NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family; This clade within the NAD dependent epimerase/dehydratase superfamily (pfam01370) is characterized by inclusion of its members within a cassette of seven distinctive enzymes. These include four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD), an aminotransferase and a nucleotidyltransferase in addition to the epimerase/dehydratase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analagous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar. Although this cassette is widely distributed in bacteria, the family nomenclature arises from the instance in Leptospira interrogans serovar Lai, str. 56601, where it appears as the 30th gene in the 91-gene lipopolysaccharide biosynthesis cluster.


Pssm-ID: 275033 [Multi-domain]  Cd Length: 297  Bit Score: 133.20  E-value: 2.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSD--AVVVVDKLTYAGNLMSLAPVAQSErfaFEKV--DICDrAELARVFTEHQpDCVM 79
Cdd:TIGR04180   1 VLVTGADGFIGSHLVEALVRQGYEvrAFVLYNSFNSWGWLDTSPPEVKDK---IEVVtgDIRD-PDSVRKAMKGC-DVVF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  80 HLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDEVYGdlhsTDDF--FTETTPYAPS 157
Cdd:TIGR04180  76 HLAALIAIPYSYIAPDSYVDTNVTGTLNVLQAARDL---------GVEKVVHTSTSEVYG----TAQYvpIDEKHPLQGQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 158 SPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALY 237
Cdd:TIGR04180 143 SPYSASKIGADQLALSFYRSFNTPVTIIRPFNTYGPRQSARAVIPTIITQIASGKRRIKLGSLSPTRDFNYVTDTVRGFI 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 238 CVATTGK-VGETYNIGGHNERKNLDVVETICELLeelapNKPhgvahyrdlITFVAD----RPGHD--LRYAIDASKIAR 310
Cdd:TIGR04180 223 AIAESDKtVGEVINIGSNFEISIGDTVKLIAEIM-----GSE---------VEIETDeerlRPEKSevERLWCDNSKIKE 288

                  ....*..
gi 1929626784 311 ELGWLPQ 317
Cdd:TIGR04180 289 LTGWQPK 295
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
4-328 7.64e-36

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: 132.04  E-value: 7.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDaVVVVDKLtYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEhqpDCVMHLAA 83
Cdd:cd05234     2 ILVTGGAGFIGSHLVDRLLEEGNE-VVVVDNL-SSGRRENIEPEFENKAFRFVKRDLLDTADKVAKKDG---DTVFHLAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRSIDGPAAFIETNIVGTYTLLEAARAywnalTEDKKSAFRfhhiSTDEVYGDlhsTDDFFT-ETTPYAPSSPYSA 162
Cdd:cd05234    77 NPDVRLGATDPDIDLEENVLATYNVLEAMRA-----NGVKRIVFA----SSSTVYGE---AKVIPTpEDYPPLPISVYGA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGP-------YHFPEKLI--PlmilnalagKSLPVYGNGQQIRDWLYVEDha 233
Cdd:cd05234   145 SKLAAEALISAYAHLFGFQAWIFRFANIVGPrsthgviYDFINKLKrnP---------NELEVLGDGRQRKSYLYVSD-- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 234 ralyCVATTGKVGE-------TYNIGghnERKNLDVVETICELLEELapnkphGVahyRDLITFV-ADR--PGHDLRYAI 303
Cdd:cd05234   214 ----CVDAMLLAWEkstegvnIFNLG---NDDTISVNEIAEIVIEEL------GL---KPRFKYSgGDRgwKGDVPYMRL 277
                         330       340
                  ....*....|....*....|....*
gi 1929626784 304 DASKiARELGWLPQETFESGMRKTV 328
Cdd:cd05234   278 DIEK-LKALGWKPRYNSEEAVRKTV 301
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
4-331 1.12e-34

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: 129.33  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDAVVVVdkltyagnlMSLAPVAQSERFAFEKV--DICDRAELARVFTehQPDCVMHL 81
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRALV---------RSGSDAVLLDGLPVEVVegDLTDAASLAAAMK--GCDRVFHL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAesHVDRSIDGPAAFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYGDlhSTDDFFTETTPYAPSS--- 158
Cdd:cd05228    70 AA--FTSLWAKDRKELYRTNVEGTRNVLDAAL---------EAGVRRVVHTSSIAALGG--PPDGRIDETTPWNERPfpn 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PYSASKASSDHLVRAWLRTyGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKsLPVYGNGQQirDWLYVEDHARALYC 238
Cdd:cd05228   137 DYYRSKLLAELEVLEAAAE-GLDVVIVNPSAVFGPGDEGPTSTGLDVLDYLNGK-LPAYPPGGT--SFVDVRDVAEGHIA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 239 VATTGKVGETYNIGGHNERknldvVETICELLEELAPNKP----------HGVAHYRDLITFVADRPG-------HDLR- 300
Cdd:cd05228   213 AMEKGRRGERYILGGENLS-----FKQLFETLAEITGVKPprrtippwllKAVAALSELKARLTGKPPlltprtaRVLRr 287
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1929626784 301 -YAIDASKIARELGWlPQETFESGMRKTVQWY 331
Cdd:cd05228   288 nYLYSSDKARRELGY-SPRPLEEALRDTLAWL 318
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
3-332 2.97e-28

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


Pssm-ID: 187550 [Multi-domain]  Cd Length: 300  Bit Score: 111.52  E-value: 2.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIiNETSDAVVVVdkLTYagnlmslapvaqserfafEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:cd05239     1 KILVTGHRGLVGSAIVRVL-ARRGYENVVF--RTS------------------KELDLTDQEAVRAFFEKEKPDYVIHLA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AesHV---DRSIDGPAAFIETNIVGTYTLLEAARAYwnaltEDKKSAFrfhhISTDEVYGDLH----STDDFFTEttPYA 155
Cdd:cd05239    60 A--KVggiVANMTYPADFLRDNLLINDNVIHAAHRF-----GVKKLVF----LGSSCIYPDLApqpiDESDLLTG--PPE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 156 PSS-PYSASKASSDHLVRAWLRTYGLP--TLITncSNNYGP-YHFPEK---LIPLMI---LNALA--GKSLPVYGNGQQI 223
Cdd:cd05239   127 PTNeGYAIAKRAGLKLCEAYRKQYGCDyiSVMP--TNLYGPhDNFDPEnshVIPALIrkfHEAKLrgGKEVTVWGSGTPR 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 224 RDWLYVEDHARALYCVATTGKVGETYNIGGHNERKNLDVVETICELLEelapnkphgvahYRDLITFVADRPGHDLRYAI 303
Cdd:cd05239   205 REFLYSDDLARAIVFLLENYDEPIIVNVGSGVEISIRELAEAIAEVVG------------FKGEIVFDTSKPDGQPRKLL 272
                         330       340
                  ....*....|....*....|....*....
gi 1929626784 304 DASKIaRELGWLPQETFESGMRKTVQWYL 332
Cdd:cd05239   273 DVSKL-RALGWFPFTPLEQGIRETYEWYL 300
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
3-334 5.41e-25

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


Pssm-ID: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 103.33  E-value: 5.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSdAVVVVDkltyagNLMSLAPVAQSERFAFEKVDIcDRAELARVFTEhQPDCVMHLA 82
Cdd:cd05273     2 RALVTGAGGFIGSHLAERLKAEGH-YVRGAD------WKSPEHMTQPTDDDEFHLVDL-REMENCLKATE-GVDHVFHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDG-PAAFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYG---DLHSTDDFFTE--TTPYAP 156
Cdd:cd05273    73 ADMGGMGYIQSnHAVIMYNNTLINFNMLEAAR---------INGVERFLFASSACVYPefkQLETTVVRLREedAWPAEP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 157 SSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYH----FPEKLIPLM---ILNALAGKSLPVYGNGQQIRDWLYV 229
Cdd:cd05273   144 QDAYGWEKLATERLCQHYNEDYGIETRIVRFHNIYGPRGtwdgGREKAPAAMcrkVATAKDGDRFEIWGDGLQTRSFTYI 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 230 EDHARALYcVATTGKVGETYNIGGHNERKNLDVVETICEL------LEELAPnKPHGVAHYrdlitfvadrpghdlryAI 303
Cdd:cd05273   224 DDCVEGLR-RLMESDFGEPVNLGSDEMVSMNELAEMVLSFsgkpleIIHHTP-GPQGVRGR-----------------NS 284
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1929626784 304 DASKIARELGWLPQETFESGMRKTVQWYLAN 334
Cdd:cd05273   285 DNTLLKEELGWEPNTPLEEGLRITYFWIKEQ 315
PLN02240 PLN02240
UDP-glucose 4-epimerase
2-314 4.93e-24

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 101.19  E-value: 4.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDaVVVVDKLTYAGNLmSLAPVAQ-----SERFAFEKVDICDRAELARVFTEHQPD 76
Cdd:PLN02240    6 RTILVTGGAGYIGSHTVLQLLLAGYK-VVVIDNLDNSSEE-ALRRVKElagdlGDNLVFHKVDLRDKEALEKVFASTRFD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  77 CVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltEDKKSAFRfhhiSTDEVYGDLHSTDdfFTETTPYAP 156
Cdd:PLN02240   84 AVIHFAGLKAVGESVAKPLLYYDNNLVGTINLLEVMAKH-----GCKKLVFS----SSATVYGQPEEVP--CTEEFPLSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 157 SSPYSASKASSDHLVR-------AW----LRTYglptlitncsNNYG----------PYHFPEKLIPLMILNALAGK-SL 214
Cdd:PLN02240  153 TNPYGRTKLFIEEICRdihasdpEWkiilLRYF----------NPVGahpsgrigedPKGIPNNLMPYVQQVAVGRRpEL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 215 PVYGN------GQQIRDWLYVED----HARALYCVATTGKVG-ETYNIGGHNERKNLDVVETIcelleELAPNK--Phgv 281
Cdd:PLN02240  223 TVFGNdyptkdGTGVRDYIHVMDladgHIAALRKLFTDPDIGcEAYNLGTGKGTSVLEMVAAF-----EKASGKkiP--- 294
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1929626784 282 ahyrdlITFVADRPGHDLRYAIDASKIARELGW 314
Cdd:PLN02240  295 ------LKLAPRRPGDAEEVYASTEKAEKELGW 321
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
3-328 1.72e-23

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 100.47  E-value: 1.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINEtSDAVVVVDKLtYAGNLMSLAPVAQSERFAFEKVDICDRAELarvftehQPDCVMHLA 82
Cdd:PLN02166  122 RIVVTGGAGFVGSHLVDKLIGR-GDEVIVIDNF-FTGRKENLVHLFGNPRFELIRHDVVEPILL-------EVDQIYHLA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAAraywnaltedKKSAFRFHHISTDEVYGD--LH-STDDFFTETTPYAPSSP 159
Cdd:PLN02166  193 CPASPVHYKYNPVKTIKTNVMGTLNMLGLA----------KRVGARFLLTSTSEVYGDplEHpQKETYWGNVNPIGERSC 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPE--KLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALY 237
Cdd:PLN02166  263 YDEGKRTAETLAMDYHRGAGVEVRIARIFNTYGPRMCLDdgRVVSNFVAQTIRKQPMTVYGDGKQTRSFQYVSDLVDGLV 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 238 CVATTGKVGeTYNIGGHNERKNLDVVETICELLE-----ELAPNkphgvahyrdlitfVADRPgHdlRYAIDASKIAREL 312
Cdd:PLN02166  343 ALMEGEHVG-PFNLGNPGEFTMLELAEVVKETIDssatiEFKPN--------------TADDP-H--KRKPDISKAKELL 404
                         330
                  ....*....|....*.
gi 1929626784 313 GWLPQETFESGMRKTV 328
Cdd:PLN02166  405 NWEPKISLREGLPLMV 420
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
2-321 5.80e-23

GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440706 [Multi-domain]  Cd Length: 321  Bit Score: 97.46  E-value: 5.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINE----------TSDavvvvdkltyaGNLMSLAPVAQSERFAFEKVDICDRAELARVFT 71
Cdd:COG1089     1 KTALITGITGQDGSYLAELLLEKgyevhgivrrSST-----------FNTERIDHLGIDDRLFLHYGDLTDSSSLIRIIQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  72 EHQPDCVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnalteDKKSafRFHHISTDEVYGDLHSTDDffTET 151
Cdd:COG1089    70 EVQPDEIYNLAAQSHVGVSFEQPEYTADVTALGTLRLLEAIRIL------GPKT--RFYQASSSEMFGLVQEVPQ--SET 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 152 TPYAPSSPYSASKASSDHLVRAWLRTYGLPTlitnCS----NNYGPyhfpekLIPLM-----ILNALA----GKSLPVY- 217
Cdd:COG1089   140 TPFYPRSPYAVAKLYAHWITVNYREAYGLFA----CNgilfNHESP------RRGETfvtrkITRAVAriklGLQDKLYl 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 218 GNGQQIRDWLYVEDHARALYCVATTGKvGETYNIgghnerknldvveticelleelAPNKPHGVahyRDLITFVADRPGH 297
Cdd:COG1089   210 GNLDAKRDWGHAPDYVEAMWLMLQQDK-PDDYVI----------------------ATGETHSV---REFVELAFAEVGL 263
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1929626784 298 DLRYAI-------------------DASKIARELGWLPQETFE 321
Cdd:COG1089   264 DWEWKVyveidpryfrpaevdlllgDPSKAKKKLGWKPKTSFE 306
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
3-330 8.07e-23

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 97.58  E-value: 8.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKLtyAGNLMSLAPVAQ---SERFAFEKVDICDRAELARVFTEHQPDCVM 79
Cdd:PRK10675    2 RVLVTGGSGYIGSHTCVQLLQNGHD-VVILDNL--CNSKRSVLPVIErlgGKHPTFVEGDIRNEALLTEILHDHAIDTVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  80 HLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAywnaltedkKSAFRFHHISTDEVYGDLHSTDdfFTETTPYA-PSS 158
Cdd:PRK10675   79 HFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRA---------ANVKNLIFSSSATVYGDQPKIP--YVESFPTGtPQS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PYSASKASSDHLVR-------AW---LRTYGLPtLITNCSNNYG--PYHFPEKLIPLMILNALAGK-SLPVYGN------ 219
Cdd:PRK10675  148 PYGKSKLMVEQILTdlqkaqpDWsiaLLRYFNP-VGAHPSGDMGedPQGIPNNLMPYIAQVAVGRRdSLAIFGNdypted 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 220 GQQIRDWLYVED----HARALYCVATTGKVgETYNIGGHNERKNLDVVETICElleelAPNKPhgVAHYrdlitFVADRP 295
Cdd:PRK10675  227 GTGVRDYIHVMDladgHVAAMEKLANKPGV-HIYNLGAGVGSSVLDVVNAFSK-----ACGKP--VNYH-----FAPRRE 293
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1929626784 296 GHDLRYAIDASKIARELGWLPQETFESGMRKTVQW 330
Cdd:PRK10675  294 GDLPAYWADASKADRELNWRVTRTLDEMAQDTWHW 328
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
3-333 2.15e-22

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


Pssm-ID: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 95.83  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVaqseRFAfekvDICDRAELARVFTEHQP----DCV 78
Cdd:cd05248     1 MIIVTGGAGFIGSNLVKALNERGITDILVVDNLSNGEKFKNLVGL----KIA----DYIDKDDFKDWVRKGDEnfkiEAI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  79 MHLAAEShvDRSIDGPAAFIETNIVGTYTLLEAARAyWNAltedkksafRFHHISTDEVYGDlhSTDDFFTETTPYA--P 156
Cdd:cd05248    73 FHQGACS--DTTETDGKYMMDNNYQYTKELLHYCLE-KKI---------RFIYASSAAVYGN--GSLGFAEDIETPNlrP 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 157 SSPYSASKASSDHlvraWLRTYGLPTLITNCS----NNYGPYHFPEKLIPLMILNA----LAG------KSLPVYGNGQQ 222
Cdd:cd05248   139 LNVYGYSKLLFDQ----WARRHGKEVLSQVVGlryfNVYGPREYHKGRMASVVFHLfnqiKAGekvklfKSSDGYADGEQ 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 223 IRDWLYVEDHARALYCVATTGKVGETYNIGGHNERKNLDVVEticelleelAPNKPHGVAHYRDLITFVADRPGhdlRYA 302
Cdd:cd05248   215 LRDFVYVKDVVKVNLFFLENPSVSGIFNVGTGRARSFNDLAS---------ATFKALGKEVKIEYIDFPEDLRG---KYQ 282
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1929626784 303 ----IDASKIaRELGWLPQ-ETFESGMRKTVQWYLA 333
Cdd:cd05248   283 sfteADISKL-RAAGYTKEfHSLEEGVKDYVKNYLA 317
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
3-316 3.62e-22

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 94.43  E-value: 3.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKltyagnlmslapvaqserfafEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:COG1091     1 RILVTGANGQLGRALVRLLAERGYE-VVALDR---------------------SELDITDPEAVAALLEEVRPDVVINAA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwNAltedkksafRFHHISTDEVY-GDlhsTDDFFTETTPYAPSSPYS 161
Cdd:COG1091    59 AYTAVDKAESEPELAYAVNATGPANLAEACAEL-GA---------RLIHISTDYVFdGT---KGTPYTEDDPPNPLNVYG 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 162 ASKASSDHLVRAW------LRTYGLptlitncsnnYGPYH--FPEKLIPLmilnALAGKSLPVYGNgqQIRDWLYVEDHA 233
Cdd:COG1091   126 RSKLAGEQAVRAAgprhliLRTSWV----------YGPHGknFVKTMLRL----LKEGEELRVVDD--QIGSPTYAADLA 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 234 RALYCVATTGKVGeTYNIGGHNERKNLDVVETICELLEELAPNKPHGVAHYRDLitfvADRPghdlRY-AIDASKIAREL 312
Cdd:COG1091   190 RAILALLEKDLSG-IYHLTGSGETSWYEFARAIAELAGLDALVEPITTAEYPTP----AKRP----ANsVLDNSKLEATL 260

                  ....
gi 1929626784 313 GWLP 316
Cdd:COG1091   261 GIKP 264
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-327 4.91e-21

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: 91.64  E-value: 4.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLApvaqserfafEKVDIcdraeLARVFTEHQPDCVMHLA 82
Cdd:cd05232     1 KVLVTGANGFIGRALVDKLLSRGEEVRIAVRNAENAEPSVVLA----------ELPDI-----DSFTDLFLGVDAVVHLA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHV--DRSIDGPAAFIETNIVGTYTLLEAARAywnaltEDKKsafRFHHISTDEVYGDlHSTDDFFTETTPYAPSSPY 160
Cdd:cd05232    66 ARVHVmnDQGADPLSDYRKVNTELTRRLARAAAR------QGVK---RFVFLSSVKVNGE-GTVGAPFDETDPPAPQDAY 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPyHFPEKLIPLMilnALAGKSLPV-YGNGQQIRDWLYVEDHARALY-C 238
Cdd:cd05232   136 GRSKLEAERALLELGASDGMEVVILRPPMVYGP-GVRGNFARLM---RLIDRGLPLpPGAVKNRRSLVSLDNLVDAIYlC 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 239 VATTGKVGETYNIGGHNERKNLDVVETICELLEELAP--NKPHGV-AHYRDLI--TFVADRPGHDLRYaiDASKIARELG 313
Cdd:cd05232   212 ISLPKAANGTFLVSDGPPVSTAELVDEIRRALGKPTRllPVPAGLlRFAAKLLgkRAVIQRLFGSLQY--DPEKTQNELG 289
                         330
                  ....*....|....
gi 1929626784 314 WLPQETFESGMRKT 327
Cdd:cd05232   290 WRPPISLEEGLQET 303
PLN02206 PLN02206
UDP-glucuronate decarboxylase
3-324 1.41e-20

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 92.35  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINEtSDAVVVVDKLtYAGNLMSLAPVAQSERFAFEKVDICDRAELarvftehQPDCVMHLA 82
Cdd:PLN02206  121 RVVVTGGAGFVGSHLVDRLMAR-GDSVIVVDNF-FTGRKENVMHHFSNPNFELIRHDVVEPILL-------EVDQIYHLA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAAraywnaltedKKSAFRFHHISTDEVYGD--LH-STDDFFTETTPYAPSSP 159
Cdd:PLN02206  192 CPASPVHYKFNPVKTIKTNVVGTLNMLGLA----------KRVGARFLLTSTSEVYGDplQHpQVETYWGNVNPIGVRSC 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPE--KLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALY 237
Cdd:PLN02206  262 YDEGKRTAETLTMDYHRGANVEVRIARIFNTYGPRMCIDdgRVVSNFVAQALRKEPLTVYGDGKQTRSFQFVSDLVEGLM 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 238 CVATTGKVGeTYNIGGHNERKNLDVVETICELLE-----ELAPNK---PHgvahyrdlitfvADRPghdlryaiDASKIA 309
Cdd:PLN02206  342 RLMEGEHVG-PFNLGNPGEFTMLELAKVVQETIDpnakiEFRPNTeddPH------------KRKP--------DITKAK 400
                         330
                  ....*....|....*
gi 1929626784 310 RELGWLPQETFESGM 324
Cdd:PLN02206  401 ELLGWEPKVSLRQGL 415
heptose_epim TIGR02197
ADP-L-glycero-D-manno-heptose-6-epimerase; This family consists of examples of ...
4-333 7.68e-20

ADP-L-glycero-D-manno-heptose-6-epimerase; This family consists of examples of ADP-L-glycero-D-mannoheptose-6-epimerase, an enzyme involved in biosynthesis of the inner core of lipopolysaccharide (LPS) for Gram-negative bacteria. This enzyme is homologous to UDP-glucose 4-epimerase (TIGR01179) and belongs to the NAD dependent epimerase/dehydratase family (pfam01370). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274028 [Multi-domain]  Cd Length: 314  Bit Score: 88.49  E-value: 7.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLApvaqSERFAfekvDICDRAELARVFTEH---QPDCVMH 80
Cdd:TIGR02197   1 IIVTGGAGFIGSNLVKALNERGITDILVVDNLRDGHKFLNLA----DLVIA----DYIDKEDFLDRLEKGafgKIEAIFH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  81 LAAESHVDRSiDGPAAFiETNIVGTYTLLEAARAyWNAltedkksafRFHHISTDEVYGDlhSTDDFFTETTPYAPSSPY 160
Cdd:TIGR02197  73 QGACSDTTET-DGEYMM-ENNYQYSKRLLDWCAE-KGI---------PFIYASSAATYGD--GEAGFREGRELERPLNVY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCS--NNYGPYHFPEKLIPLMILNA----LAG------KSLPVYGNGQQIRDWLY 228
Cdd:TIGR02197 139 GYSKFLFDQYVRRRVLPEALSAQVVGLRyfNVYGPREYHKGKMASVAFHLfnqiKAGgnvklfKSSEGFKDGEQLRDFVY 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 229 VEDHARALYCVATTGKVGeTYNIGGHNERKNLDVVETiceLLEELAPNKPhgvahyrdlITFVadrpghDLRYAI----- 303
Cdd:TIGR02197 219 VKDVVDVNLWLLENGVSG-IFNLGTGRARSFNDLADA---VFKALGKDEK---------IEYI------PMPEALrgryq 279
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1929626784 304 -----DASKIARELGWLPQETFESGMRKTVQWYLA 333
Cdd:TIGR02197 280 yftqaDITKLRAAGYYGPFTTLEEGVKDYVQWLLA 314
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
4-325 9.42e-20

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


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 88.19  E-value: 9.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETS-DAVVVVDKLtyagnlmslAPVAQSERFAFEKVDICDRAeLARVFTEHQPDCVMHLA 82
Cdd:cd05240     1 ILVTGAAGGLGRLLARRLAASPRvIGVDGLDRR---------RPPGSPPKVEYVRLDIRDPA-AADVFREREADAVVHLA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AEshVDRSIDGPAAFiETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDEVYGDLHSTDDFFTETTPY--APSSPY 160
Cdd:cd05240    71 FI--LDPPRDGAERH-RINVDGTQNVLDACAAA---------GVPRVVVTSSVAVYGAHPDNPAPLTEDAPLrgSPEFAY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTY-GLPTLITNCSNNYGPyhfpekliplMILNALAGKSLPVYGNGQQIRD----WLYVEDHARA 235
Cdd:cd05240   139 SRDKAEVEQLLAEFRRRHpELNVTVLRPATILGP----------GTRNTTRDFLSPRRLPVPGGFDppfqFLHEDDVARA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 236 LYCVATTGKVGeTYNIGGhnerknlDVVETICELLEELA------PNKPHGVAHYRDLITFVADRPG--HDLRYA--IDA 305
Cdd:cd05240   209 LVLAVRAGATG-IFNVAG-------DGPVPLSLVLALLGrrpvplPSPLPAALAAARRLGLRPLPPEqlDFLQYPpvMDT 280
                         330       340
                  ....*....|....*....|
gi 1929626784 306 SKIARELGWLPQETFESGMR 325
Cdd:cd05240   281 TRARVELGWQPKHTSAEVLR 300
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
4-331 1.88e-19

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


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 87.87  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPvaqsERFAFEKVDICDRAELARvfTEHQPDCVMHLAA 83
Cdd:cd05241     2 VLVTGGSGFFGERLVKQLLERGGTYVRSFDIAPPGEALSAWQH----PNIEFLKGDITDRNDVEQ--ALSGADCVFHTAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRSIDgpaAFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYG---DLHSTDdfftETTPYAP--SS 158
Cdd:cd05241    76 IVPLAGPRD---LYWEVNVGGTQNVLDACQ---------RCGVQKFVYTSSSSVIFggqNIHNGD----ETLPYPPldSD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHfpEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYC 238
Cdd:cd05241   140 MYAETKAIAEIIVLEANGRDDLLTCALRPAGIFGPGD--QGLVPILFEWAEKGLVKFVFGRGNNLVDFTYVHNLAHAHIL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 239 VAT-----TGKVGETYNIGG---HNERKNLDVVETICELLEELAPNKPHGVAHYRDLIT-FVADRPGHDLRYAI------ 303
Cdd:cd05241   218 AAAalvkgKTISGQTYFITDaepHNMFELLRPVWKALGFGSRPKIRLSGPLAYCAALLSeLVSFMLGPYFVFSPfyvral 297
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1929626784 304 ------DASKIARELGWLPQETFESGMRKTVQWY 331
Cdd:cd05241   298 vtpmyfSIAKAQKDLGYAPRYSNEEGLIETLNWY 331
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
2-173 8.15e-19

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: 85.36  E-value: 8.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDAVVVVD---------KLTYAGNLMSLapvaqseRFAFEKVDICDRAELARVFTE 72
Cdd:cd05237     3 KTILVTGGAGSIGSELVRQILKFGPKKLIVFDrdenklhelVRELRSRFPHD-------KLRFIIGDVRDKERLRRAFKE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  73 HQPDCVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDE-VYgdlhstddfftet 151
Cdd:cd05237    76 RGPDIVFHAAALKHVPSMEDNPEEAIKTNVLGTKNVIDAAIEN---------GVEKFVCISTDKaVN------------- 133
                         170       180
                  ....*....|....*....|..
gi 1929626784 152 tpyaPSSPYSASKASSDHLVRA 173
Cdd:cd05237   134 ----PVNVMGATKRVAEKLLLA 151
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
3-331 1.16e-18

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


Pssm-ID: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 85.25  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIInETSDAVVVVDKLTyAGNLMSLAPVaqsERFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:cd08957     2 KVLITGGAGQIGSHLIEHLL-ERGHQVVVIDNFA-TGRREHLPDH---PNLTVVEGSIADKALVDKLFGDFKPDAVVHTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AeSHVDrsidgPAAFIE---TNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSP 159
Cdd:cd08957    77 A-AYKD-----PDDWYEdtlTNVVGGANVVQAAK---------KAGVKRLIYFQTALCYGLKPMQQPIRLDHPRAPPGSS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHlvraWLRTYGLPTLITNCSNNYGPYHF--PeklIPLMILNALAGKSLPVygnGQQIRDWLYVEDHAR-AL 236
Cdd:cd08957   142 YAISKTAGEY----YLELSGVDFVTFRLANVTGPRNVigP---LPTFYQRLKAGKKCFV---TDTRRDFVFVKDLARvVD 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 237 YCVATTGKVGeTYNIG---GHNERKNLD-VVETICELLEELAPNKPHGVahyRDLITFVadrpghdlryaIDASKIAREL 312
Cdd:cd08957   212 KALDGIRGHG-AYHFSsgeDVSIKELFDaVVEALDLPLRPEVEVVELGP---DDVPSIL-----------LDPSRTFQDF 276
                         330
                  ....*....|....*....
gi 1929626784 313 GWLPQETFESGMRKTVQWY 331
Cdd:cd08957   277 GWKEFTPLSETVSAALAWY 295
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
2-336 2.36e-18

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


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 84.76  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYII--NETsdaVVVVDKLT--YAGNLMSLAPVAQSE---RFAFEKVDIcdraelaRVFTEHQ 74
Cdd:PRK15181   16 KRWLITGVAGFIGSGLLEELLflNQT---VIGLDNFStgYQHNLDDVRTSVSEEqwsRFIFIQGDI-------RKFTDCQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  75 PDC-----VMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYGDlhSTDDFFT 149
Cdd:PRK15181   86 KACknvdyVLHQAALGSVPRSLKDPIATNSANIDGFLNMLTAAR---------DAHVSSFTYAASSSTYGD--HPDLPKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 150 ETTPYAPSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFP----EKLIPLMILNALAGKSLPVYGNGQQIRD 225
Cdd:PRK15181  155 EERIGRPLSPYAVTKYVNELYADVFARSYEFNAIGLRYFNVFGRRQNPngaySAVIPRWILSLLKDEPIYINGDGSTSRD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 226 WLYVEDHARALYCVATTGKVG---ETYNIGGHNERKNLDVVETICELLEELAPNKPHGVAHYRDLitfvadRPGHDLRYA 302
Cdd:PRK15181  235 FCYIENVIQANLLSATTNDLAsknKVYNVAVGDRTSLNELYYLIRDGLNLWRNEQSRAEPIYKDF------RDGDVKHSQ 308
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1929626784 303 IDASKIARELGWLPQETFESGMRKTVQWYLANES 336
Cdd:PRK15181  309 ADITKIKTFLSYEPEFDIKEGLKQTLKWYIDKHS 342
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
5-331 7.36e-18

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


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 83.18  E-value: 7.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVVVDkltyAGNLMSLAPvAQSERFAFEKVDICDRAELARVFTEHQPDCVMHLAAE 84
Cdd:cd09813     3 LVVGGSGFLGRHLVEQLLRRGNPTVHVFD----IRPTFELDP-SSSGRVQFHTGDLTDPQDLEKAFNEKGPNVVFHTASP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  85 SHvdRSidGPAAFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHIST-DEVYG--DLHSTDdfftETTPYA--PSSP 159
Cdd:cd09813    78 DH--GS--NDDLYYKVNVQGTRNVIEACR---------KCGVKKLVYTSSaSVVFNgqDIINGD----ESLPYPdkHQDA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSASKASSDHLV-RAWLRTYGLPTLITNCSNNYGPYHfpEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYC 238
Cdd:cd09813   141 YNETKALAEKLVlKANDPESGLLTCALRPAGIFGPGD--RQLVPGLLKAAKNGKTKFQIGDGNNLFDFTYVENVAHAHIL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 239 VA---TTGKV-----GETYNIGGHNERKNLDVVETICELLEELAPNKPH-------GVAHYRDLITFVADRPGHD--LRY 301
Cdd:cd09813   219 AAdalLSSSHaetvaGEAFFITNDEPIYFWDFARAIWEGLGYERPPSIKlprpvalYLASLLEWTCKVLGKEPTFtpFRV 298
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1929626784 302 AI-------DASKIARELGWLPQETFESGMRKTVQWY 331
Cdd:cd09813   299 ALlcstryfNIEKAKKRLGYTPVVTLEEGIERTLQWF 335
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
3-253 1.25e-17

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: 81.90  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKltyagnlmslapvaqseRFAFEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:cd05254     1 KILITGATGMLGRALVRLLKERGYEVIGTGRS-----------------RASLFKLDLTDPDAVEEAIRDYKPDVIINCA 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAAraywnaltedKKSAFRFHHISTDEVY-GDlhstDDFFTETTPYAPSSPYS 161
Cdd:cd05254    64 AYTRVDKCESDPELAYRVNVLAPENLARAA----------KEVGARLIHISTDYVFdGK----KGPYKEEDAPNPLNVYG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 162 ASKAssdhLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNgqQIRDWLYVEDHARALYCVAT 241
Cdd:cd05254   130 KSKL----LGEVAVLNANPRYLILRTSWLYGELKNGENFVEWMLRLAAERKEVNVVHD--QIGSPTYAADLADAILELIE 203
                         250
                  ....*....|..
gi 1929626784 242 TGKVGETYNIGG 253
Cdd:cd05254   204 RNSLTGIYHLSN 215
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
4-173 2.73e-17

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: 81.02  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLM--SLAPVAQSERFAFEKV----DICDRAELARVFTEHQPDC 77
Cdd:pfam02719   1 VLVTGGGGSIGSELCRQILKFNPKKIILFSRDELKLYEIrqELREKFNDPKLRFFIVpvigDVRDRERLERAMEQYGVDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  78 VMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedkkSAFRFHHISTDE-VYgdlhstddfftettpyaP 156
Cdd:pfam02719  81 VFHAAAYKHVPLVEYNPMEAIKTNVLGTENVADAAIEA---------GVKKFVLISTDKaVN-----------------P 134
                         170
                  ....*....|....*..
gi 1929626784 157 SSPYSASKASSDHLVRA 173
Cdd:pfam02719 135 TNVMGATKRLAEKLFQA 151
PLN02653 PLN02653
GDP-mannose 4,6-dehydratase
46-321 5.50e-17

GDP-mannose 4,6-dehydratase


Pssm-ID: 178259 [Multi-domain]  Cd Length: 340  Bit Score: 80.97  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  46 PVAQSERFAFEKVDICDRAELARVFTEHQPDCVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnalTEDKKS 125
Cdd:PLN02653   55 PHPNKARMKLHYGDLSDASSLRRWLDDIKPDEVYNLAAQSHVAVSFEMPDYTADVVATGALRLLEAVRLH----GQETGR 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 126 AFRFHHISTDEVYGdlhSTDDFFTETTPYAPSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPY---HFPEKLIP 202
Cdd:PLN02653  131 QIKYYQAGSSEMYG---STPPPQSETTPFHPRSPYAVAKVAAHWYTVNYREAYGLFACNGILFNHESPRrgeNFVTRKIT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 203 LMILNALAGKSLPVY-GNGQQIRDWLYVEDHARAL-----------YCVATtgkvGETYnigghnerknldvveTICELL 270
Cdd:PLN02653  208 RAVGRIKVGLQKKLFlGNLDASRDWGFAGDYVEAMwlmlqqekpddYVVAT----EESH---------------TVEEFL 268
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626784 271 EElapnkPHGVA--HYRDLItfVAD----RPGHDLRYAIDASKIARELGWLPQETFE 321
Cdd:PLN02653  269 EE-----AFGYVglNWKDHV--EIDpryfRPAEVDNLKGDASKAREVLGWKPKVGFE 318
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
5-335 3.24e-16

GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 78.20  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVVvdkLTYAgnlmslapvaqserfafeKVDICDRAELARVFTEHQPDCVMHLAAE 84
Cdd:PLN02725    1 FVAGHRGLVGSAIVRKLEALGFTNLVL---RTHK------------------ELDLTRQADVEAFFAKEKPTYVILAAAK 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  85 -SHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltEDKKSAFrfhhISTDEVYGDL--HSTDDFFTETTPYAPSSP-Y 160
Cdd:PLN02725   60 vGGIHANMTYPADFIRENLQIQTNVIDAAYRH-----GVKKLLF----LGSSCIYPKFapQPIPETALLTGPPEPTNEwY 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYH-F-PEK--LIPLMI-----LNALAGKSLPVYGNGQQIRDWLYVED 231
Cdd:PLN02725  131 AIAKIAGIKMCQAYRIQYGWDAISGMPTNLYGPHDnFhPENshVIPALIrrfheAKANGAPEVVVWGSGSPLREFLHVDD 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 232 HARALYCVATTGKVGETYNIGGHNErknldvvETICELLEELApnkphGVAHYRDLITFVADRPGHDLRYAIDASKIaRE 311
Cdd:PLN02725  211 LADAVVFLMRRYSGAEHVNVGSGDE-------VTIKELAELVK-----EVVGFEGELVWDTSKPDGTPRKLMDSSKL-RS 277
                         330       340
                  ....*....|....*....|....
gi 1929626784 312 LGWLPQETFESGMRKTVQWYLANE 335
Cdd:PLN02725  278 LGWDPKFSLKDGLQETYKWYLENY 301
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
3-323 1.31e-14

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


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 73.57  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALV-RYIINETSDAVVVVDKltyagnlmsLAPVAQSERFAFEKV--DICDRAELARVFtEHQPDCVM 79
Cdd:cd05238     2 KVLITGASGFVGQRLAeRLLSDVPNERLILIDV---------VSPKAPSGAPRVTQIagDLAVPALIEALA-NGRPDVVF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  80 HLAAesHVDRSIDGPAA-FIETNIVGTYTLLEAARaywnalteDKKSAFRFHHISTDEVYGDlhSTDDFFTETTPYAPSS 158
Cdd:cd05238    72 HLAA--IVSGGAEADFDlGYRVNVDGTRNLLEALR--------KNGPKPRFVFTSSLAVYGL--PLPNPVTDHTALDPAS 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PYSASKAS-----SDHLVRAWLRTYG--LPTLITN-CSNNYGPYHFPEKLIPLMilnaLAGKS--LPVygnGQQIRDWLY 228
Cdd:cd05238   140 SYGAQKAMcelllNDYSRRGFVDGRTlrLPTVCVRpGRPNKAASAFASTIIREP----LVGEEagLPV---AEQLRYWLK 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 229 VED-------HARALYCVATTGKVGETYNIGghnerknldvVETICELLEELAPNKPHGVAhyrDLITFVADR------- 294
Cdd:cd05238   213 SVAtavanfvHAAELPAEKFGPRRDLTLPGL----------SVTVGEELRALIPVAGLPAL---MLITFEPDEeikrivf 279
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1929626784 295 --PGHdlryaIDASKiARELGWLPQETFESG 323
Cdd:cd05238   280 gwPTR-----FDATR-AQSLGFVADSSLAAG 304
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
5-240 1.58e-14

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


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 72.78  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLApvAQSERFAFEKVDICDRAELARVFTEhqPDCVMHLAAE 84
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDF--SKSNVIKYIQGDVTDKDDLDNALEG--VDVVIHTASA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  85 SHVdRSIDGPAAFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYGDLHSTDDFFT--ETTPY--APSSPY 160
Cdd:pfam01073  77 VDV-FGKYTFDEIMKVNVKGTQNVLEACV---------KAGVRVLVYTSSAEVVGPNSYGQPILNgdEETPYesTHQDAY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 161 SASKASSDHLVrawLRTYGLP-----TLITNC---SNNYGPYHfpEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDH 232
Cdd:pfam01073 147 PRSKAIAEKLV---LKANGRPlknggRLYTCAlrpAGIYGEGD--RLLVPFIVNLAKLGLAKFKTGDDNNLSDRVYVGNV 221

                  ....*...
gi 1929626784 233 ARALYCVA 240
Cdd:pfam01073 222 AWAHILAA 229
PRK11908 PRK11908
bifunctional UDP-4-keto-pentose/UDP-xylose synthase;
1-333 1.20e-13

bifunctional UDP-4-keto-pentose/UDP-xylose synthase;


Pssm-ID: 183375 [Multi-domain]  Cd Length: 347  Bit Score: 70.90  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIInETSDAVVvvdkltYAGNLMS--LAPVAQSERFAFEKVDICDRAELARvFTEHQPDCV 78
Cdd:PRK11908    1 MKKVLILGVNGFIGHHLSKRIL-ETTDWEV------YGMDMQTdrLGDLVNHPRMHFFEGDITINKEWIE-YHVKKCDVI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  79 MHLAAeshvdrsIDGPAAFIEtNIVGTYTL-LEAARAYWNALTEDKKsafrfHHI--STDEVYGdLHSTDDFFTETTP-- 153
Cdd:PRK11908   73 LPLVA-------IATPATYVK-QPLRVFELdFEANLPIVRSAVKYGK-----HLVfpSTSEVYG-MCPDEEFDPEASPlv 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 154 YAP-SSP---YSASKASSDHLVRAWLRTYGLPTLITNCSNNYGP----YHFPE----KLIPLMILNALAGKSLPVYGNGQ 221
Cdd:PRK11908  139 YGPiNKPrwiYACSKQLMDRVIWAYGMEEGLNFTLFRPFNWIGPgldsIYTPKegssRVVTQFLGHIVRGEPISLVDGGS 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 222 QIRDWLYVEDHARALY-------CVATtgkvGETYNIGghNERKNLDVVEtICELLEELAPNKPhGVAHYRDLITFVADR 294
Cdd:PRK11908  219 QKRAFTDIDDGIDALMkiienkdGVAS----GKIYNIG--NPKNNHSVRE-LANKMLELAAEYP-EYAESAKKVKLVETT 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1929626784 295 PG-------HDLRYAIDA-SKIARELGWLPQETFESGMRKTVQWYLA 333
Cdd:PRK11908  291 SGayygkgyQDVQNRVPKiDNTMQELGWAPKTTMDDALRRIFEAYRG 337
SQD1_like_SDR_e cd05255
UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) ...
3-236 9.27e-13

UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) SDRs; Arabidopsis thaliana UDP-sulfoquinovose-synthase ( SQD1), an extended SDR, catalyzes the transfer of SO(3)(-) to UDP-glucose in the biosynthesis of plant sulfolipids. Members of this subgroup share the conserved SDR catalytic residues, and a partial match to the characteristic extended-SDR 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: 187565 [Multi-domain]  Cd Length: 382  Bit Score: 68.57  E-value: 9.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGN----LMSLAPVAQ-SERF-----------AFEKVDICDRAEL 66
Cdd:cd05255     2 KVLILGGDGYCGWPTALHLSKRGHEVCIVDNLVRRRIDvelgLESLTPIASiHERLrawkeltgktiEFYVGDACDYEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  67 ARVFTEHQPDCVMHLAAESHVDRS-IDGPAAfIET---NIVGTYTLLeaaraywNALTEDKKSAfRFHHISTDEVYG--D 140
Cdd:cd05255    82 AELLASHEPDAVVHFAEQRSAPYSmIDREHA-NYTqhnNVIGTLNLL-------FAIKEFDPDC-HLVKLGTMGEYGtpN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 141 LHSTDDFFTETT---------PYAPSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMI------ 205
Cdd:cd05255   153 IDIPEGYITIEHngrrdtlpyPKQAGSWYHLSKVHDSHNIMFACKAWGIRITDLNQGVVYGTKTEETEADERLInrfdyd 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1929626784 206 ------LN-----ALAGKSLPVYGNGQQIRDWLYVEDHARAL 236
Cdd:cd05255   233 gvfgtvLNrfcvqAAIGHPLTVYGKGGQTRGFISIRDTVQCL 274
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
4-173 2.09e-12

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: 66.53  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRyIINETSDAVVVVDKltyagnlmslapvaqserfafEKVDICDRAELARVFTEHQPDCVMHLAA 83
Cdd:pfam04321   1 ILITGANGQLGTELRR-LLAERGIEVVALTR---------------------AELDLTDPEAVARLLREIKPDVVVNAAA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwNALtedkksafrFHHISTDEVY-GDlhsTDDFFTETTPYAPSSPYSA 162
Cdd:pfam04321  59 YTAVDKAESEPDLAYAINALAPANLAEACAAV-GAP---------LIHISTDYVFdGT---KPRPYEEDDETNPLNVYGR 125
                         170
                  ....*....|.
gi 1929626784 163 SKASSDHLVRA 173
Cdd:pfam04321 126 TKLAGEQAVRA 136
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
2-184 4.31e-12

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: 65.61  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDAVVVV----------DKLTYAGNLMSLAPVAQSERFAFEKVDIC---------D 62
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDARVYCLvrasdeaaarERLEALLERYGLWLELDASRVVVVAGDLTqprlglseaE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  63 RAELARvftehQPDCVMHLAAESHVDRSidgPAAFIETNIVGTYTLLEAARAywnaltedkKSAFRFHHISTDEVYGDLH 142
Cdd:COG3320    81 FQELAE-----EVDAIVHLAALVNLVAP---YSELRAVNVLGTREVLRLAAT---------GRLKPFHYVSTIAVAGPAD 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1929626784 143 sTDDFFTET---TPYAPSSPYSASKASSDHLVRAWlRTYGLPTLI 184
Cdd:COG3320   144 -RSGVFEEDdldEGQGFANGYEQSKWVAEKLVREA-RERGLPVTI 186
rmlD TIGR01214
dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making ...
3-236 5.63e-12

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: 65.50  E-value: 5.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKltyagnlmslapvaqserfafEKVDICDRAELARVFTEHQPDCVMHLA 82
Cdd:TIGR01214   1 RILITGANGQLGRELVQQLSPEGRV-VVALTR---------------------SQLDLTDPEALERLLRAIRPDAVVNTA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAAFIETNIVGTYTLLEAARAYwnaltedkksAFRFHHISTDEVYgDLHSTDDfFTETTPYAPSSPYSA 162
Cdd:TIGR01214  59 AYTDVDGAESDPEKAFAVNALAPQNLARAAARH----------GARLVHISTDYVF-DGEGKRP-YREDDATNPLNVYGQ 126
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929626784 163 SKASSDHLVRAwlrtYGLPTLITNCSNNYGpYHFPEKLIPLMILNALAGKSLPVYGNgqQIRDWLYVEDHARAL 236
Cdd:TIGR01214 127 SKLAGEQAVRA----AGPNALIVRTSWLYG-GGGGRNFVRTMLRLAGRGEELRVVDD--QIGSPTYAGDLARVI 193
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
2-270 1.47e-10

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: 60.77  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDavvvVDKLTyAGNlmslAPVAQSERFAFEKVDICDRAELARVFTEHQPDCV--M 79
Cdd:cd05265     1 MKILIIGGTRFIGKALVEELLAAGHD----VTVFN-RGR----TKPDLPEGVEHIVGDRNDRDALEELLGGEDFDVVvdT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  80 HLAAESHVDRSIDgpaAFIETniVGTYTLleaaraywnaltedkksafrfhhISTDEVYGD-LHSTDDF----FTETTPY 154
Cdd:cd05265    72 IAYTPRQVERALD---AFKGR--VKQYIF-----------------------ISSASVYLKpGRVITEStplrEPDAVGL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 155 APSSPYSASKASSDHLVRawlRTYGLPTLITNCSNNYGPYHFPEKLiPLMILNALAGKSLPVYGNGQQIRDWLYVEDHAR 234
Cdd:cd05265   124 SDPWDYGRGKRAAEDVLI---EAAAFPYTIVRPPYIYGPGDYTGRL-AYFFDRLARGRPILVPGDGHSLVQFIHVKDLAR 199
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1929626784 235 ALYCVATTGK-VGETYNIGGHNERKNLDVVETICELL 270
Cdd:cd05265   200 ALLGAAGNPKaIGGIFNITGDEAVTWDELLEACAKAL 236
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
4-196 1.64e-09

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


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 58.15  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVR---------YIINETSDAVVVVDKLTYAGnlmslapvAQSERFAFEKVDIC---------DRAE 65
Cdd:cd05263     1 VFVTGGTGFLGRHLVKrllengfkvLVLVRSESLGEAHERIEEAG--------LEADRVRVLEGDLTqpnlglsaaASRE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  66 LARvftehQPDCVMHLAAESHVDRSIDGPAAfieTNIVGTYTLLEAARAywnaltedkKSAFRFHHISTDEV----YGDL 141
Cdd:cd05263    73 LAG-----KVDHVIHCAASYDFQAPNEDAWR---TNIDGTEHVLELAAR---------LDIQRFHYVSTAYVagnrEGNI 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929626784 142 HSTDDFFTETTPyapsSPYSASKASSDHLVRAWLRTYGL----PTLITNCSNN------YGPYHF 196
Cdd:cd05263   136 RETELNPGQNFK----NPYEQSKAEAEQLVRAAATQIPLtvyrPSIVVGDSKTgriekiDGLYEL 196
PLN02572 PLN02572
UDP-sulfoquinovose synthase
2-250 3.35e-08

UDP-sulfoquinovose synthase


Pssm-ID: 215310 [Multi-domain]  Cd Length: 442  Bit Score: 54.80  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDaVVVVDKLTYAG-----NLMSLAPVA------------QSERFAFEKVDICDRA 64
Cdd:PLN02572   48 KKVMVIGGDGYCGWATALHLSKRGYE-VAIVDNLCRRLfdhqlGLDSLTPIAsihervrrwkevSGKEIELYVGDICDFE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  65 ELARVFTEHQPDCVMHLAAE-----SHVDRSidgPAAFIET-NIVGTYTLLEAAraywnaltedKKSAFRFH--HISTDE 136
Cdd:PLN02572  127 FLSEAFKSFEPDAVVHFGEQrsapySMIDRS---RAVFTQHnNVIGTLNVLFAI----------KEFAPDCHlvKLGTMG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 137 VYGD---------LHSTDDFFTETTPYA--PSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGpYHFPEKLIPLMI 205
Cdd:PLN02572  194 EYGTpnidieegyITITHNGRTDTLPYPkqASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYG-VRTDETMMDEEL 272
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 206 LN------------------ALAGKSLPVYGNGQQIRDWLYVEDHARalyCV-------ATTGKVgETYN 250
Cdd:PLN02572  273 INrldydgvfgtalnrfcvqAAVGHPLTVYGKGGQTRGFLDIRDTVR---CIeiaianpAKPGEF-RVFN 338
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
6-189 3.49e-08

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


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 53.77  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   6 ITGGAGFIGSALVRYIINETSDAVVVV------------DKLTYAGNLMSLAPVAqsERFAFEKV-----DIC------- 61
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIYllvrakdgesalERLRQELEKYPLFDAL--LKEALERIvpvagDLSepnlgls 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  62 --DRAELARvftehQPDCVMHLAAESHVDRSIDgpaAFIETNIVGTYTLLEAARAYwnaltedkKSAFRFHHIST----- 134
Cdd:pfam07993  79 eeDFQELAE-----EVDVIIHSAATVNFVEPYD---DARAVNVLGTREVLRLAKQG--------KQLKPFHHVSTayvng 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929626784 135 -------DEVYGDLHST--DDFFTETTPYAPSSPYSASKASSDHLVRAWlRTYGLPTLITNCSN 189
Cdd:pfam07993 143 ergglveEKPYPEGEDDmlLDEDEPALLGGLPNGYTQTKWLAEQLVREA-ARRGLPVVIYRPSI 205
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
3-115 7.55e-08

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: 53.08  E-value: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINE-TSDAVVVVDKLTYAGNLMSLAPvaqserfaFEKVDICDRAELARVFTEHQPDCVMHL 81
Cdd:cd05272     1 RILITGGLGQIGSELAKLLRKRyGKDNVIASDIRKPPAHVVLSGP--------FEYLDVLDFKSLEEIVVNHKITWIIHL 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1929626784  82 AA------ESHVDRSIDgpaafieTNIVGTYTLLEAARAY 115
Cdd:cd05272    73 AAllsavgEKNPPLAWD-------VNMNGLHNVLELAREH 105
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
3-192 2.02e-07

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: 51.59  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAqserfafekvdicdraelarvftehqpDCVMHLA 82
Cdd:cd05261     2 KILITGAKGFIGKNLIARLKEQKDDDIFFYDRESDESELDDFLQGA---------------------------DFIFHLA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AeshVDRSIDgPAAFIETNIVGTYTLLEaaraywnALTEDKKSAfrfhHIstdevygdlhstddFFTETTPYAPSSPYSA 162
Cdd:cd05261    55 G---VNRPKD-EAEFESGNVGLTERLLD-------ALTRNGKKP----PI--------------LLSSSIQAALDNPYGK 105
                         170       180       190
                  ....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYG 192
Cdd:cd05261   106 SKLAAEELLQEYARETGAPVYIYRLPNVFG 135
PRK07201 PRK07201
SDR family oxidoreductase;
5-173 5.14e-07

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 51.49  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVVVdkLTYAGNLMSLApvAQSERFAFEKV-----DIC---------DRAELARVf 70
Cdd:PRK07201    4 FVTGGTGFIGRRLVSRLLDRRREATVHV--LVRRQSLSRLE--ALAAYWGADRVvplvgDLTepglglseaDIAELGDI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  71 tehqpDCVMHLAAEshVDRSIDgPAAFIETNIVGTYTLLEAARAYWNALtedkksafrFHHISTDEVYGDL--HSTDDFF 148
Cdd:PRK07201   79 -----DHVVHLAAI--YDLTAD-EEAQRAANVDGTRNVVELAERLQAAT---------FHHVSSIAVAGDYegVFREDDF 141
                         170       180
                  ....*....|....*....|....*
gi 1929626784 149 TETTPYapSSPYSASKASSDHLVRA 173
Cdd:PRK07201  142 DEGQGL--PTPYHRTKFEAEKLVRE 164
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
4-237 5.72e-07

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 50.33  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLaPVAQSERFAFEKVDICdraelarvftehqpDCVMHLAA 83
Cdd:TIGR01777   1 ILITGGTGFIGRALTQRLTKRGHEVTILTRSPPPGANTKWE-GYKPWAGEDADSLEGA--------------DAVINLAG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  84 ESHVDR--SIDGPAAFIETNIVGTYTLLEAARAYwnaltEDKKSAFrfhhISTDEV--YGdlHSTDDFFTETTPyAPSSP 159
Cdd:TIGR01777  66 EPIADKrwTEERKQEIRDSRIDTTRLLVEAIAAA-----EQKPKVF----ISASAVgyYG--PSEDREYTEEDS-PAGDD 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 160 YSAskassdHLVRAWLRT------YGLPTLITNCSNNYGPY-HFPEKLIPLMILNaLAGKslpvYGNGQQIRDWLYVEDH 232
Cdd:TIGR01777 134 FLA------ELCRDWEEAaqaaedLGTRVVLLRTGIVLGPKgGALAKMLLPFRLG-LGGP----LGSGRQWFSWIHIEDL 202

                  ....*
gi 1929626784 233 ARALY 237
Cdd:TIGR01777 203 VQLIL 207
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
3-345 1.98e-06

GDP-D-mannose-3',5'-epimerase


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 49.04  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINEtSDAVVVVDkltyagnlmslapvaQSERFAFEKVDICDRAELA--RVFTEHQPDC--- 77
Cdd:PLN02695   23 RICITGAGGFIASHIARRLKAE-GHYIIASD---------------WKKNEHMSEDMFCHEFHLVdlRVMENCLKVTkgv 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  78 --VMHLAAEShvdrsidGPAAFIET--------NIVGTYTLLEAARAywNALTedkksafRFHHISTDEVYGDLH--STD 145
Cdd:PLN02695   87 dhVFNLAADM-------GGMGFIQSnhsvimynNTMISFNMLEAARI--NGVK-------RFFYASSACIYPEFKqlETN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 146 DFFTETT--PYAPSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHF----PEKLIPLMILNAL-AGKSLPVYG 218
Cdd:PLN02695  151 VSLKESDawPAEPQDAYGLEKLATEELCKHYTKDFGIECRIGRFHNIYGPFGTwkggREKAPAAFCRKALtSTDEFEMWG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 219 NGQQIRDWLYVEDharalyCVA-----TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNK----PHGVAHYRDlit 289
Cdd:PLN02695  231 DGKQTRSFTFIDE------CVEgvlrlTKSDFREPVNIGSDEMVSMNEMAEIALSFENKKLPIKhipgPEGVRGRNS--- 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626784 290 fvadrpghdlryaiDASKIARELGWLPQETFESGMRKTVQWylANESWWKQVQDGS 345
Cdd:PLN02695  302 --------------DNTLIKEKLGWAPTMRLKDGLRITYFW--IKEQIEKEKAEGS 341
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
1-166 4.11e-06

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 47.25  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   1 MRKILITGGAGFIGSALVRYIINEtSDAVVVV----DKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEHQ-- 74
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKE-GANVIIVarseSKLEEAVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVek 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  75 ---PDCVMHLAAESH----VDRSIDGPAAFIETNIVGTytlLEAARAywnALTEDKKSafRFHHIStdevygdlhstddF 147
Cdd:cd08939    80 ggpPDLVVNCAGISIpglfEDLTAEEFERGMDVNYFGS---LNVAHA---VLPLMKEQ--RPGHIV-------------F 138
                         170       180
                  ....*....|....*....|..
gi 1929626784 148 FTETTPYAPS---SPYSASKAS 166
Cdd:cd08939   139 VSSQAALVGIygySAYCPSKFA 160
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
3-244 9.33e-06

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


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 46.88  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSAlvryIINETSDA----VVVVDKLTYAGNLMS-LAPVAQSERFAFEKVD-ICDRAELARVFTEHqpD 76
Cdd:cd05227     1 LVLVTGATGFIASH----IVEQLLKAgykvRGTVRSLSKSAKLKAlLKAAGYNDRLEFVIVDdLTAPNAWDEALKGV--D 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  77 CVMHLAAESHVDrSIDGPAAFIETNIVGTYTLLEAARAYWN----ALTEDKKSAFRFHHISTDEVYGDLHSTDDFFTETt 152
Cdd:cd05227    75 YVIHVASPFPFT-GPDAEDDVIDPAVEGTLNVLEAAKAAGSvkrvVLTSSVAAVGDPTAEDPGKVFTEEDWNDLTISKS- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 153 pyAPSSPYSASKASSDHLVRAWLRTYGL-PTLIT-NCSNNYGPYHFPEKLIP-LMILNALAGKSLP-----VYGNGQQIR 224
Cdd:cd05227   153 --NGLDAYIASKTLAEKAAWEFVKENKPkFELITiNPGYVLGPSLLADELNSsNELINKLLDGKLPaippnLPFGYVDVR 230
                         250       260
                  ....*....|....*....|.
gi 1929626784 225 DwlyVED-HARALYCVATTGK 244
Cdd:cd05227   231 D---VADaHVRALESPEAAGQ 248
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
4-174 1.42e-05

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 45.74  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVRYIINEtSDAVVVVDKltyagNLMSLAPVAQSERF----AFEKVDICDRAELARVFTEHQ----- 74
Cdd:cd05233     1 ALVTGASSGIGRAIARRLARE-GAKVVLADR-----NEEALAELAAIEALggnaVAVQADVSDEEDVEALVEEALeefgr 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  75 PDCVMHLAAESHVDRSIDGPAAF----IETNIVGTYTLleaARAYWNALTEDKKSAFrfhhISTDEVYGdlhstddffte 150
Cdd:cd05233    75 LDILVNNAGIARPGPLEELTDEDwdrvLDVNLTGVFLL---TRAALPHMKKQGGGRI----VNISSVAG----------- 136
                         170       180
                  ....*....|....*....|....
gi 1929626784 151 TTPYAPSSPYSASKASSDHLVRAW 174
Cdd:cd05233   137 LRPLPGQAAYAASKAALEGLTRSL 160
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
3-184 1.43e-05

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: 46.11  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVdkLTYAG-----------NLMSLAPVAQSERFAfEKVDIC---------- 61
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELLKRKNVSKIYC--LVRAKdeeaalerlidNLKEYGLNLWDELEL-SRIKVVvgdlskpnlg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  62 ----DRAELARVFtehqpDCVMHLAAE-SHVDRSidgpAAFIETNIVGTYTLLEaaraywnaLTEDKKSAfRFHHIST-- 134
Cdd:cd05235    78 lsddDYQELAEEV-----DVIIHNGANvNWVYPY----EELKPANVLGTKELLK--------LAATGKLK-PLHFVSTls 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1929626784 135 ---DEVYGDLHSTDDFFTETTPYAPSSPYSASKASSDHLVRAwLRTYGLPTLI 184
Cdd:cd05235   140 vfsAEEYNALDDEESDDMLESQNGLPNGYIQSKWVAEKLLRE-AANRGLPVAI 191
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
4-277 2.55e-05

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


Pssm-ID: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 45.30  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGGAGFIGSALVR------YIINETSDAVVVVDKLTYAGNLMslapvAQSERFAFEKVDICDRAElarvFTEHQPDC 77
Cdd:cd05193     1 VLVTGASGFVASHVVEqllergYKVRATVRDPSKVKKVNHLLDLD-----AKPGRLELAVADLTDEQS----FDEVIKGC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  78 --VMHLAAEshVDRSIDGPAAFIETNIVGTYTLLEAARAywnaltedKKSAFRFHHIST-----------DEVYGDLHST 144
Cdd:cd05193    72 agVFHVATP--VSFSSKDPNEVIKPAIGGTLNALKAAAA--------AKSVKRFVLTSSagsvlipkpnvEGIVLDEKSW 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 145 DDFFTETTPYAPSSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIR 224
Cdd:cd05193   142 NLEEFDSDPKKSAWVYAASKTLAEKAAWKFADENNIDLITVIPTLTIGTIFDSETPSSSGWAMSLITGNEGVSPALALIP 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929626784 225 DWLYV--EDHARALYCVATTGKVGETYNIGGHNErknldVVETICELLEELAPNK 277
Cdd:cd05193   222 PGYYVhvVDICLAHIGCLELPIARGRYICTAGNF-----DWNTLLKTLRKKYPSY 271
PLN02427 PLN02427
UDP-apiose/xylose synthase
3-330 4.82e-05

UDP-apiose/xylose synthase


Pssm-ID: 178047 [Multi-domain]  Cd Length: 386  Bit Score: 44.85  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVVD----KLTYagnLMSLAPVAQSERFAFEKVDICDRAELARVFTehQPDCV 78
Cdd:PLN02427   16 TICMIGAGGFIGSHLCEKLMTETPHKVLALDvyndKIKH---LLEPDTVPWSGRIQFHRINIKHDSRLEGLIK--MADLT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  79 MHLAAeshvdrsIDGPAAFIETNIVGTYTLLEAARAYWNALTEDKKsafRFHHISTDEVYGDlhSTDDFFTETTPYA--P 156
Cdd:PLN02427   91 INLAA-------ICTPADYNTRPLDTIYSNFIDALPVVKYCSENNK---RLIHFSTCEVYGK--TIGSFLPKDHPLRqdP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 157 S--------SP------------YSASKASSDHLVRAWLRTYGLPTLITNCSNNYGP-YHF------PEKLIPLMIL--- 206
Cdd:PLN02427  159 AfyvlkedeSPcifgsiekqrwsYACAKQLIERLIYAEGAENGLEFTIVRPFNWIGPrMDFipgidgPSEGVPRVLAcfs 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 207 -NALAGKSLPVYGNGQQIRDWLYVEDHARA-LYCVATTGKV-GETYNIGG-HNERknldVVETICELLEELApNKPHGVA 282
Cdd:PLN02427  239 nNLLRREPLKLVDGGQSQRTFVYIKDAIEAvLLMIENPARAnGHIFNVGNpNNEV----TVRQLAEMMTEVY-AKVSGEP 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1929626784 283 HYRDLITFVADRP----GHD--LRYAIDASKIARELGWLPQETFESGMRKTVQW 330
Cdd:PLN02427  314 ALEEPTVDVSSKEfygeGYDdsDKRIPDMTIINKQLGWNPKTSLWDLLESTLTY 367
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-331 6.48e-05

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


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 44.42  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSD--AVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTEhqPDCVMHLA 82
Cdd:cd09811     3 LVTGGGGFLGQHIIRLLLERKEElkEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQG--VSVVIHTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AEshVDrsIDGPA---AFIETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYGDLHSTDDFFT--ETTPYAPS 157
Cdd:cd09811    81 AI--VD--VFGPPnyeELEEVNVNGTQAVLEACV---------QNNVKRLVYTSSIEVAGPNFKGRPIFNgvEDTPYEDT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 158 S--PYSASKASSDHLVrawLRTYGLP-----TLITNCSNNYGPY----HFPEKLIPLMILN--------ALAGKSLPVY- 217
Cdd:cd09811   148 StpPYASSKLLAENIV---LNANGAPlkqggYLVTCALRPMYIYgegsHFLTEIFDFLLTNngwlfpriKGSGVNPLVYv 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 218 GNGQqirdWLYVEdHARALYCVATT--GKVGETYNIGGHN--ERKNLDVVETICELLEELAPNKPHGVAHY--------- 284
Cdd:cd09811   225 GNVA----WAHIL-AAKALQVPDKAirGQFYFISDDTPHNsySDFNYELLKELGLRLKTSWWYVPLFLLYFlaflleivs 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929626784 285 RDLITFVADRPGHDLR--------YAIDASKIARELGWLPQETFESGMRKTVQWY 331
Cdd:cd09811   300 FLLRPYVKYRPRYNRHavaltnsmFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
PRK09186 PRK09186
flagellin modification protein A; Provisional
2-72 1.23e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.05  E-value: 1.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDAVVV-VDKLTYAGNLMSLAPVAQSERFAFEKVDICDRAELARVFTE 72
Cdd:PRK09186    5 KTILITGAGGLIGSALVKAILEAGGIVIAAdIDKEALNELLESLGKEFKSKKLSLVELDITDQESLEEFLSK 76
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
4-270 1.38e-04

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: 42.69  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   4 ILITGgAGFIGSALVRYIINETSDAVVVV--DKLTYAGNLMSLAPVAQserfafekvDICDRAELARVftehqPDCVMHL 81
Cdd:cd05266     1 VLILG-CGYLGQRLARQLLAQGWQVTGTTrsPEKLAADRPAGVTPLAA---------DLTQPGLLADV-----DHLVISL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAESHVDRsidgpaafietnivgtYTLLEAARAYWNALtedkKSAFRFHHI---STDEVYGDlhSTDDFFTETTPYAPSS 158
Cdd:cd05266    66 PPPAGSYR----------------GGYDPGLRALLDAL----AQLPAVQRViylSSTGVYGD--QQGEWVDETSPPNPST 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 159 PysaskaSSDHLVRA---WLRTYGLPTLITNCSNNYGPyhfpEKLIplmiLNALAGKSlPVYGNGQQIRDWLYVEDHARA 235
Cdd:cd05266   124 E------SGRALLEAeqaLLALGSKPTTILRLAGIYGP----GRHP----LRRLAQGT-GRPPAGNAPTNRIHVDDLVGA 188
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1929626784 236 LYCVATTGKVGETYNI--GGHNERKnlDVVETICELL 270
Cdd:cd05266   189 LAFALQRPAPGPVYNVvdDLPVTRG--EFYQAAAELL 223
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
2-187 1.56e-04

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 42.71  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   2 RKILITGGAGFIGSALVRYIINETSDAVVV---VDKLTYAGNLMSLAPvaqSERFAFEKVDICDRAELARVFTEH----- 73
Cdd:cd08930     3 KIILITGAAGLIGKAFCKALLSAGARLILAdinAPALEQLKEELTNLY---KNRVIALELDITSKESIKELIESYlekfg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  74 QPDCVMHLAAESHVDRSI---DGPAAFIETNI---VGTYTLLeaARAYWNALTEDKKSAFRFhhISTDevYGDLHSTDDF 147
Cdd:cd08930    80 RIDILINNAYPSPKVWGSrfeEFPYEQWNEVLnvnLGGAFLC--SQAFIKLFKKQGKGSIIN--IASI--YGVIAPDFRI 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1929626784 148 FTETTPYAPSSpYSASKASSDHLVRaWLRTYGLPTLI-TNC 187
Cdd:cd08930   154 YENTQMYSPVE-YSVIKAGIIHLTK-YLAKYYADTGIrVNA 192
PRK07041 PRK07041
SDR family oxidoreductase;
5-113 5.51e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 40.79  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   5 LITGGAGFIGSALVRYIINETSDAVVV---VDKLTYAgnlmsLAPVAQSERFAFEKVDICDRAELARVFTEHQP-DCVMH 80
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIAsrsRDRLAAA-----ARALGGGAPVRTAALDITDEAAVDAFFAEAGPfDHVVI 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1929626784  81 LAA--ESHVDRSIDGPAA--FIETNIVGTYTLLEAAR 113
Cdd:PRK07041   76 TAAdtPGGPVRALPLAAAqaAMDSKFWGAYRVARAAR 112
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
3-174 5.94e-04

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


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 41.20  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVV-DKLTYAGNLMSLAPVAQSERFafekvdicDRAELARVftehqpDCVMHL 81
Cdd:COG1090     1 KILITGGTGFIGSALVAALLARGHEVVVLTrRPPKAPDEVTYVAWDPETGGI--------DAAALEGA------DAVINL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  82 AAEshvdrSI-DGP------AAFIETNIVGTYTLLEAARAywnalTEDKKSAFrfhhISTDEV--YGDlhSTDDFFTETT 152
Cdd:COG1090    67 AGA-----SIaDKRwtearkQEILDSRVDSTRLLVEAIAA-----AANPPKVL----ISASAIgyYGD--RGDEVLTEDS 130
                         170       180
                  ....*....|....*....|..
gi 1929626784 153 PyaPSSPYSAskassdHLVRAW 174
Cdd:COG1090   131 P--PGDGFLA------EVCRAW 144
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
3-254 2.19e-03

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 39.62  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKltyagNLMSLAPVAQSERFAfekVDICDRAELARVftEHQPDCVMHLA 82
Cdd:cd05229     1 TAHVLGASGPIGREVARELRRRGWD-VRLVSR-----SGSKLAWLPGVEIVA---ADAMDASSVIAA--ARGADVIYHCA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  83 AESHVDRSIDGPAafIETNIVgtytllEAARAYwNAltedkksafrfHHISTDEVYGDLHSTDDFFTETTPYAPSSPYSA 162
Cdd:cd05229    70 NPAYTRWEELFPP--LMENVV------AAAEAN-GA-----------KLVLPGNVYMYGPQAGSPITEDTPFQPTTRKGR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 163 SKASSDHLVRAWLRTYGLPTLITNCSNNYGPyhfpEKLIPLM---ILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCV 239
Cdd:cd05229   130 IRAEMEERLLAAHAKGDIRALIVRAPDFYGP----GAINSWLgaaLFAILQGKTAVFPGNLDTPHEWTYLPDVARALVTL 205
                         250
                  ....*....|....*.
gi 1929626784 240 ATT-GKVGETYNIGGH 254
Cdd:cd05229   206 AEEpDAFGEAWHLPGA 221
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
3-253 3.29e-03

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 38.29  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784   3 KILITGGAGFIGSALVRYIINETSDAVVVV------DKLTYAGnlmslAPVAQserfafekVDICDRAELARVFTEHqpD 76
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVRALVrdpekaAALAAAG-----VEVVQ--------GDLDDPESLAAALAGV--D 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784  77 CVMHLAAeshvdrsiDGPAAFIETNIVGTYTLLEAARAywnaltedkKSAFRFHHISTdevygdLHSTDDfftettpyaP 156
Cdd:COG0702    66 AVFLLVP--------SGPGGDFAVDVEGARNLADAAKA---------AGVKRIVYLSA------LGADRD---------S 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626784 157 SSPYSASKASSDHLVRA----W--LRtyglPTLITncsNNYgpyhfpeklipLMILNALAGKSLPVYGNGQQIRDWLYVE 230
Cdd:COG0702   114 PSPYLRAKAAVEEALRAsglpYtiLR----PGWFM---GNL-----------LGFFERLRERGVLPLPAGDGRVQPIAVR 175
                         250       260
                  ....*....|....*....|....
gi 1929626784 231 DHARALYCVATT-GKVGETYNIGG 253
Cdd:COG0702   176 DVAEAAAAALTDpGHAGRTYELGG 199
 
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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