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Conserved domains on  [gi|445970335|ref|WP_000048190|]
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MULTISPECIES: GDP-mannose 4,6-dehydratase [Enterobacteriaceae]

Protein Classification

GDP-mannose 4,6-dehydratase( domain architecture ID 10787214)

GDP-mannose 4,6-dehydratase catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
3-355 0e+00

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


:

Pssm-ID: 440706 [Multi-domain]  Cd Length: 321  Bit Score: 702.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQdphtcNPKFHLHYGDLSDTSNLTRILREVQPDE 82
Cdd:COG1089    1 KTALITGITGQDGSYLAELLLEKGYEVHGIVRRSSTFNTERIDHLGI-----DDRLFLHYGDLTDSSSLIRIIQEVQPDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGleKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKL 162
Cdd:COG1089   76 IYNLAAQSHVGVSFEQPEYTADVTALGTLRLLEAIRILG--PKTRFYQASSSEMFGLVQEVPQSETTPFYPRSPYAVAKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 YAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQ 242
Cdd:COG1089  154 YAHWITVNYREAYGLFACNGILFNHESPRRGETFVTRKITRAVARIKLGLQDKLYLGNLDAKRDWGHAPDYVEAMWLMLQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 243 QEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFegtgveekgivvsvtghdapgvkpgDVIIAVDPRYFRPAEVETLLG 322
Cdd:COG1089  234 QDKPDDYVIATGETHSVREFVELAFAEVGLDWEW-------------------------KVYVEIDPRYFRPAEVDLLLG 288
                        330       340       350
                 ....*....|....*....|....*....|...
gi 445970335 323 DPTKAHEKLGWKPEITLREMVSEMVANDLEAAK 355
Cdd:COG1089  289 DPSKAKKKLGWKPKTSFEELVREMVEADLELLK 321
 
Name Accession Description Interval E-value
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
3-355 0e+00

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


Pssm-ID: 440706 [Multi-domain]  Cd Length: 321  Bit Score: 702.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQdphtcNPKFHLHYGDLSDTSNLTRILREVQPDE 82
Cdd:COG1089    1 KTALITGITGQDGSYLAELLLEKGYEVHGIVRRSSTFNTERIDHLGI-----DDRLFLHYGDLTDSSSLIRIIQEVQPDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGleKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKL 162
Cdd:COG1089   76 IYNLAAQSHVGVSFEQPEYTADVTALGTLRLLEAIRILG--PKTRFYQASSSEMFGLVQEVPQSETTPFYPRSPYAVAKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 YAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQ 242
Cdd:COG1089  154 YAHWITVNYREAYGLFACNGILFNHESPRRGETFVTRKITRAVARIKLGLQDKLYLGNLDAKRDWGHAPDYVEAMWLMLQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 243 QEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFegtgveekgivvsvtghdapgvkpgDVIIAVDPRYFRPAEVETLLG 322
Cdd:COG1089  234 QDKPDDYVIATGETHSVREFVELAFAEVGLDWEW-------------------------KVYVEIDPRYFRPAEVDLLLG 288
                        330       340       350
                 ....*....|....*....|....*....|...
gi 445970335 323 DPTKAHEKLGWKPEITLREMVSEMVANDLEAAK 355
Cdd:COG1089  289 DPSKAKKKLGWKPKTSFEELVREMVEADLELLK 321
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
6-346 0e+00

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 599.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335    6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHtcNPKFHLHYGDLSDTSNLTRILREVQPDEVYN 85
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVRRSSSFNTGRLEHLYDDHL--NGNLVLHYGDLTDSSNLVRLLAEVQPDEIYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAY 165
Cdd:pfam16363  79 LAAQSHVDVSFEQPEYTADTNVLGTLRLLEAIRSLGLEKKVRFYQASTSEVYGKVQEVPQTETTPFYPRSPYAAAKLYAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  166 WITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQEQ 245
Cdd:pfam16363 159 WIVVNYRESYGLFACNGILFNHESPRRGERFVTRKITRGVARIKLGKQEKLYLGNLDAKRDWGHARDYVEAMWLMLQQDK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  246 PEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVeekgivvsvtghDAPGVKPGDVIIAVDPRYFRPAEVETLLGDPT 325
Cdd:pfam16363 239 PDDYVIATGETHTVREFVEKAFLELGLTITWEGKGE------------IGYFKASGKVHVLIDPRYFRPGEVDRLLGDPS 306
                         330       340
                  ....*....|....*....|.
gi 445970335  326 KAHEKLGWKPEITLREMVSEM 346
Cdd:pfam16363 307 KAKEELGWKPKVSFEELVREM 327
gmd TIGR01472
GDP-mannose 4,6-dehydratase; Alternate name: GDP-D-mannose dehydratase. This enzyme converts ...
3-354 0e+00

GDP-mannose 4,6-dehydratase; Alternate name: GDP-D-mannose dehydratase. This enzyme converts GDP-mannose to GDP-4-dehydro-6-deoxy-D-mannose, the first of three steps for the conversion of GDP-mannose to GDP-fucose in animals, plants, and bacteria. In bacteria, GDP-L-fucose acts as a precursor of surface antigens such as the extracellular polysaccharide colanic acid of E. coli. Excluded from this model are members of the clade that score poorly because of highly dervied (phylogenetically long-branch) sequences, e.g. Aneurinibacillus thermoaerophilus Gmd, described as a bifunctional GDP-mannose 4,6-dehydratase/GDP-6-deoxy-D-lyxo-4-hexulose reductase (PUBMED:11096116). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273644 [Multi-domain]  Cd Length: 343  Bit Score: 578.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335    3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNP-KFHLHYGDLSDTSNLTRILREVQPD 81
Cdd:TIGR01472   1 KIALITGITGQDGSYLAEFLLEKGYEVHGLIRRSSSFNTQRIEHIYEDPHNVNKaRMKLHYGDLTDSSNLRRIIDEIKPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   82 EVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAK 161
Cdd:TIGR01472  81 EIYNLAAQSHVKVSFEIPEYTADVDGIGTLRLLEAVRTLGLIKSVKFYQASTSELYGKVQEIPQNETTPFYPRSPYAAAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  162 LYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMML 241
Cdd:TIGR01472 161 LYAHWITVNYREAYGLFAVNGILFNHESPRRGENFVTRKITRAAAKIKLGLQEKLYLGNLDAKRDWGHAKDYVEAMWLML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  242 QQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKGIvvsvtghdapGVKPGDVIIAVDPRYFRPAEVETLL 321
Cdd:TIGR01472 241 QQDKPDDYVIATGETHSVREFVEVSFEYIGKTLNWKDKGINEVGR----------CKETGKVHVEIDPRYFRPTEVDLLL 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 445970335  322 GDPTKAHEKLGWKPEITLREMVSEMVANDLEAA 354
Cdd:TIGR01472 311 GDATKAKEKLGWKPEVSFEKLVKEMVEEDLELA 343
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
4-352 0e+00

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: 554.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   4 VALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDphtcNPKFHLHYGDLSDTSNLTRILREVQPDEV 83
Cdd:cd05260    1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHLYIN----KDRITLHYGDLTDSSSLRRAIEKVRPDEI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  84 YNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLekKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLY 163
Cdd:cd05260   77 YHLAAQSHVKVSFDDPEYTAEVNAVGTLNLLEAIRILGL--DARFYQASSSEEYGKVQELPQSETTPFRPRSPYAVSKLY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 164 AYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQ 243
Cdd:cd05260  155 ADWITRNYREAYGLFAVNGRLFNHEGPRRGETFVTRKITRQVARIKAGLQPVLKLGNLDAKRDWGDARDYVEAYWLLLQQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 244 EQPEDFVIATGVQYSVRQFVEMAAAQLGiklrfeGTGVEEKGIvvsvtghdapgvkpgdviiavDPRYFRPAEVETLLGD 323
Cdd:cd05260  235 GEPDDYVIATGETHSVREFVELAFEESG------LTGDIEVEI---------------------DPRYFRPTEVDLLLGD 287
                        330       340
                 ....*....|....*....|....*....
gi 445970335 324 PTKAHEKLGWKPEITLREMVSEMVANDLE 352
Cdd:cd05260  288 PSKAREELGWKPEVSFEELVREMLDADLE 316
PLN02653 PLN02653
GDP-mannose 4,6-dehydratase
3-360 0e+00

GDP-mannose 4,6-dehydratase


Pssm-ID: 178259 [Multi-domain]  Cd Length: 340  Bit Score: 550.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDE 82
Cdd:PLN02653   7 KVALITGITGQDGSYLTEFLLSKGYEVHGIIRRSSNFNTQRLDHIYIDPHPNKARMKLHYGDLSDASSLRRWLDDIKPDE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEK--KTRFYQASTSELYGLVQEiPQKETTPFYPRSPYAVA 160
Cdd:PLN02653  87 VYNLAAQSHVAVSFEMPDYTADVVATGALRLLEAVRLHGQETgrQIKYYQAGSSEMYGSTPP-PQSETTPFHPRSPYAVA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 161 KLYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMM 240
Cdd:PLN02653 166 KVAAHWYTVNYREAYGLFACNGILFNHESPRRGENFVTRKITRAVGRIKVGLQKKLFLGNLDASRDWGFAGDYVEAMWLM 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 241 LQQEQPEDFVIATGVQYSVRQFVEMAaaqlgiklrFEGTGVEEKGIVVsvtghdapgvkpgdviiaVDPRYFRPAEVETL 320
Cdd:PLN02653 246 LQQEKPDDYVVATEESHTVEEFLEEA---------FGYVGLNWKDHVE------------------IDPRYFRPAEVDNL 298
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 445970335 321 LGDPTKAHEKLGWKPEITLREMVSEMVANDLEAAKKHSLL 360
Cdd:PLN02653 299 KGDASKAREVLGWKPKVGFEQLVKMMVDEDLELAKREKVL 338
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
263-308 7.66e-03

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 35.43  E-value: 7.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 445970335   263 VEMAAAQLGIKLRfeGTGVEEKGIVVSVTGHDAP----GVKPGDVIIAVD 308
Cdd:smart00228   7 LEKGGGGLGFSLV--GGKDEGGGVVVSSVVPGSPaakaGLRVGDVILEVN 54
 
Name Accession Description Interval E-value
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
3-355 0e+00

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


Pssm-ID: 440706 [Multi-domain]  Cd Length: 321  Bit Score: 702.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQdphtcNPKFHLHYGDLSDTSNLTRILREVQPDE 82
Cdd:COG1089    1 KTALITGITGQDGSYLAELLLEKGYEVHGIVRRSSTFNTERIDHLGI-----DDRLFLHYGDLTDSSSLIRIIQEVQPDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGleKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKL 162
Cdd:COG1089   76 IYNLAAQSHVGVSFEQPEYTADVTALGTLRLLEAIRILG--PKTRFYQASSSEMFGLVQEVPQSETTPFYPRSPYAVAKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 YAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQ 242
Cdd:COG1089  154 YAHWITVNYREAYGLFACNGILFNHESPRRGETFVTRKITRAVARIKLGLQDKLYLGNLDAKRDWGHAPDYVEAMWLMLQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 243 QEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFegtgveekgivvsvtghdapgvkpgDVIIAVDPRYFRPAEVETLLG 322
Cdd:COG1089  234 QDKPDDYVIATGETHSVREFVELAFAEVGLDWEW-------------------------KVYVEIDPRYFRPAEVDLLLG 288
                        330       340       350
                 ....*....|....*....|....*....|...
gi 445970335 323 DPTKAHEKLGWKPEITLREMVSEMVANDLEAAK 355
Cdd:COG1089  289 DPSKAKKKLGWKPKTSFEELVREMVEADLELLK 321
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
6-346 0e+00

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 599.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335    6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHtcNPKFHLHYGDLSDTSNLTRILREVQPDEVYN 85
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVRRSSSFNTGRLEHLYDDHL--NGNLVLHYGDLTDSSNLVRLLAEVQPDEIYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAY 165
Cdd:pfam16363  79 LAAQSHVDVSFEQPEYTADTNVLGTLRLLEAIRSLGLEKKVRFYQASTSEVYGKVQEVPQTETTPFYPRSPYAAAKLYAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  166 WITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQEQ 245
Cdd:pfam16363 159 WIVVNYRESYGLFACNGILFNHESPRRGERFVTRKITRGVARIKLGKQEKLYLGNLDAKRDWGHARDYVEAMWLMLQQDK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  246 PEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVeekgivvsvtghDAPGVKPGDVIIAVDPRYFRPAEVETLLGDPT 325
Cdd:pfam16363 239 PDDYVIATGETHTVREFVEKAFLELGLTITWEGKGE------------IGYFKASGKVHVLIDPRYFRPGEVDRLLGDPS 306
                         330       340
                  ....*....|....*....|.
gi 445970335  326 KAHEKLGWKPEITLREMVSEM 346
Cdd:pfam16363 307 KAKEELGWKPKVSFEELVREM 327
gmd TIGR01472
GDP-mannose 4,6-dehydratase; Alternate name: GDP-D-mannose dehydratase. This enzyme converts ...
3-354 0e+00

GDP-mannose 4,6-dehydratase; Alternate name: GDP-D-mannose dehydratase. This enzyme converts GDP-mannose to GDP-4-dehydro-6-deoxy-D-mannose, the first of three steps for the conversion of GDP-mannose to GDP-fucose in animals, plants, and bacteria. In bacteria, GDP-L-fucose acts as a precursor of surface antigens such as the extracellular polysaccharide colanic acid of E. coli. Excluded from this model are members of the clade that score poorly because of highly dervied (phylogenetically long-branch) sequences, e.g. Aneurinibacillus thermoaerophilus Gmd, described as a bifunctional GDP-mannose 4,6-dehydratase/GDP-6-deoxy-D-lyxo-4-hexulose reductase (PUBMED:11096116). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273644 [Multi-domain]  Cd Length: 343  Bit Score: 578.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335    3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNP-KFHLHYGDLSDTSNLTRILREVQPD 81
Cdd:TIGR01472   1 KIALITGITGQDGSYLAEFLLEKGYEVHGLIRRSSSFNTQRIEHIYEDPHNVNKaRMKLHYGDLTDSSNLRRIIDEIKPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   82 EVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAK 161
Cdd:TIGR01472  81 EIYNLAAQSHVKVSFEIPEYTADVDGIGTLRLLEAVRTLGLIKSVKFYQASTSELYGKVQEIPQNETTPFYPRSPYAAAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  162 LYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMML 241
Cdd:TIGR01472 161 LYAHWITVNYREAYGLFAVNGILFNHESPRRGENFVTRKITRAAAKIKLGLQEKLYLGNLDAKRDWGHAKDYVEAMWLML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  242 QQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKGIvvsvtghdapGVKPGDVIIAVDPRYFRPAEVETLL 321
Cdd:TIGR01472 241 QQDKPDDYVIATGETHSVREFVEVSFEYIGKTLNWKDKGINEVGR----------CKETGKVHVEIDPRYFRPTEVDLLL 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 445970335  322 GDPTKAHEKLGWKPEITLREMVSEMVANDLEAA 354
Cdd:TIGR01472 311 GDATKAKEKLGWKPEVSFEKLVKEMVEEDLELA 343
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
4-352 0e+00

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: 554.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   4 VALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDphtcNPKFHLHYGDLSDTSNLTRILREVQPDEV 83
Cdd:cd05260    1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHLYIN----KDRITLHYGDLTDSSSLRRAIEKVRPDEI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  84 YNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLekKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLY 163
Cdd:cd05260   77 YHLAAQSHVKVSFDDPEYTAEVNAVGTLNLLEAIRILGL--DARFYQASSSEEYGKVQELPQSETTPFRPRSPYAVSKLY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 164 AYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQ 243
Cdd:cd05260  155 ADWITRNYREAYGLFAVNGRLFNHEGPRRGETFVTRKITRQVARIKAGLQPVLKLGNLDAKRDWGDARDYVEAYWLLLQQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 244 EQPEDFVIATGVQYSVRQFVEMAAAQLGiklrfeGTGVEEKGIvvsvtghdapgvkpgdviiavDPRYFRPAEVETLLGD 323
Cdd:cd05260  235 GEPDDYVIATGETHSVREFVELAFEESG------LTGDIEVEI---------------------DPRYFRPTEVDLLLGD 287
                        330       340
                 ....*....|....*....|....*....
gi 445970335 324 PTKAHEKLGWKPEITLREMVSEMVANDLE 352
Cdd:cd05260  288 PSKAREELGWKPEVSFEELVREMLDADLE 316
PLN02653 PLN02653
GDP-mannose 4,6-dehydratase
3-360 0e+00

GDP-mannose 4,6-dehydratase


Pssm-ID: 178259 [Multi-domain]  Cd Length: 340  Bit Score: 550.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDE 82
Cdd:PLN02653   7 KVALITGITGQDGSYLTEFLLSKGYEVHGIIRRSSNFNTQRLDHIYIDPHPNKARMKLHYGDLSDASSLRRWLDDIKPDE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEK--KTRFYQASTSELYGLVQEiPQKETTPFYPRSPYAVA 160
Cdd:PLN02653  87 VYNLAAQSHVAVSFEMPDYTADVVATGALRLLEAVRLHGQETgrQIKYYQAGSSEMYGSTPP-PQSETTPFHPRSPYAVA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 161 KLYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMM 240
Cdd:PLN02653 166 KVAAHWYTVNYREAYGLFACNGILFNHESPRRGENFVTRKITRAVGRIKVGLQKKLFLGNLDASRDWGFAGDYVEAMWLM 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 241 LQQEQPEDFVIATGVQYSVRQFVEMAaaqlgiklrFEGTGVEEKGIVVsvtghdapgvkpgdviiaVDPRYFRPAEVETL 320
Cdd:PLN02653 246 LQQEKPDDYVVATEESHTVEEFLEEA---------FGYVGLNWKDHVE------------------IDPRYFRPAEVDNL 298
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 445970335 321 LGDPTKAHEKLGWKPEITLREMVSEMVANDLEAAKKHSLL 360
Cdd:PLN02653 299 KGDASKAREVLGWKPKVGFEQLVKMMVDEDLELAKREKVL 338
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
5-252 7.80e-95

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: 282.65  E-value: 7.80e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335    5 ALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIyqdphtcnpkfHLHYGDLSDTSNLTRILREVQPDEVY 84
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADL-----------RFVEGDLTDRDALEKLLADVRPDAVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   85 NLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQKETT---PFYPRSPYAVAK 161
Cdd:pfam01370  70 HLAAVGGVGASIEDPEDFIEANVLGTLNLLEAARKAGVK---RFLFASSSEVYGDGAEIPQEETTltgPLAPNSPYAAAK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  162 LYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGlESCLYLGNMDSLRDWGHAKDYVKMQWMML 241
Cdd:pfam01370 147 LAGEWLVLAYAAAYGLRAVILRLFNVYGPGDNEGFVSRVIPALIRRILEG-KPILLWGDGTQRRDFLYVDDVARAILLAL 225
                         250
                  ....*....|...
gi 445970335  242 QQ--EQPEDFVIA 252
Cdd:pfam01370 226 EHgaVKGEIYNIG 238
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
6-348 3.40e-44

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 154.37  E-value: 3.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFntERVDHIyqdphtcnPKFHLHYGDLSDTSNLTRILRevQPDEVYN 85
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGA--ANLAAL--------PGVEFVRGDLRDPEALAAALA--GVDAVVH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVsfESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLvQEIPQKETTPFYPRSPYAVAKLYAY 165
Cdd:COG0451   71 LAAPAGVGE--EDPDETLEVNVEGTLNLLEAARAAGVK---RFVYASSSSVYGD-GEGPIDEDTPLRPVSPYGASKLAAE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 166 WITVNYRESYGMYACNGILFNHESPRRgetfvTRKITRAIANIAQGlESCLYLGNMDSLRDWGHAKDYVK-MQWMMLQQE 244
Cdd:COG0451  145 LLARAYARRYGLPVTILRPGNVYGPGD-----RGVLPRLIRRALAG-EPVPVFGDGDQRRDFIHVDDVARaIVLALEAPA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 245 QP-EDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTgveekgivvsvtghdapgvkpgdviiavdpryFRPAEVETLLGD 323
Cdd:COG0451  219 APgGVYNVGGGEPVTLRELAEAIAEALGRPPEIVYP--------------------------------ARPGDVRPRRAD 266
                        330       340
                 ....*....|....*....|....*
gi 445970335 324 PTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:COG0451  267 NSKARRELGWRPRTSLEEGLRETVA 291
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-247 3.07e-43

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: 148.99  E-value: 3.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRassfntervdhiyqdphtcnpkfhlhygdlsdtsnltrilrevqpDEVYN 85
Cdd:cd08946    2 LVTGGAGFIGSHLVRRLLERGHEVVVIDRL---------------------------------------------DVVVH 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAY 165
Cdd:cd08946   37 LAALVGVPASWDNPDEDFETNVVGTLNLLEAARKAGVK---RFVYASSASVYGSPEGLPEEEETPPRPLSPYGVSKLAAE 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 166 WITVNYRESYGMYACNGILFNHESPRRGETF--VTRKITRAIANIaqgleSCLYL-GNMDSLRDWGHAKDYVKMQWMMLQ 242
Cdd:cd08946  114 HLLRSYGESYGLPVVILRLANVYGPGQRPRLdgVVNDFIRRALEG-----KPLTVfGGGNQTRDFIHVDDVVRAILHALE 188

                 ....*
gi 445970335 243 QEQPE 247
Cdd:cd08946  189 NPLEG 193
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
6-347 5.54e-37

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: 135.43  E-value: 5.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRrASSFNTERVDHIyqdphtcNPKFHLHYGDLSDTSNLTRILREVqpDEVYN 85
Cdd:cd05256    3 LVTGGAGFIGSHLVERLLERGHEVIVLDN-LSTGKKENLPEV-------KPNVKFIEGDIRDDELVEFAFEGV--DYVFH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAY 165
Cdd:cd05256   73 QAAQASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVK---RFVYASSSSVYGDPPYLPKDEDHPPNPLSPYAVSKYAGE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 166 WITVNYRESYGMYACNGILFNHESPRRGETFVTRK-ITRAIANIAQGLESCLYlGNMDSLRDWGHAKDYVKMQWMMLQQE 244
Cdd:cd05256  150 LYCQVFARLYGLPTVSLRYFNVYGPRQDPNGGYAAvIPIFIERALKGEPPTIY-GDGEQTRDFTYVEDVVEANLLAATAG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 245 QPED-FVIATGVQYSVRQFVEmaaaqlgiKLRfEGTGVEekgivvsvtghdapgvkpgdviIAVDPRYFRPAEVETLLGD 323
Cdd:cd05256  229 AGGEvYNIGTGKRTSVNELAE--------LIR-EILGKE----------------------LEPVYAPPRPGDVRHSLAD 277
                        330       340
                 ....*....|....*....|....
gi 445970335 324 PTKAHEKLGWKPEITLREMVSEMV 347
Cdd:cd05256  278 ISKAKKLLGWEPKVSFEEGLRLTV 301
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
1-348 2.73e-36

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


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 134.44  E-value: 2.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   1 MSKVaLITGVTGQDGSYLAEFLLEK--GYEVHGI-K-RRASsfNTERVDHIYQDPHtcnpkFHLHYGDLSDTSNLTRILR 76
Cdd:COG1088    1 MMRI-LVTGGAGFIGSNFVRYLLAKypGAEVVVLdKlTYAG--NLENLADLEDDPR-----YRFVKGDIRDRELVDELFA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  77 EVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKtRFYQASTSELYG-LVQEIPQKETTPFYPRS 155
Cdd:COG1088   73 EHGPDAVVHFAAESHVDRSIDDPAAFVETNVVGTFNLLEAARKYWVEGF-RFHHVSTDEVYGsLGEDGPFTETTPLDPSS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 156 PYAVAKL------YAYWITvnyresYGMYAcngILFNHeS----PRR-GETFVTRKITRAIANIAQGlescLYlGNMDSL 224
Cdd:COG1088  152 PYSASKAasdhlvRAYHRT------YGLPV---VITRC-SnnygPYQfPEKLIPLFITNALEGKPLP----VY-GDGKQV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 225 RDWGHAKDYVKMQWMMLQQEQP-EDFVIATGVQYSVRQFVEMAAAQLGiklrfegtgvEEKGIVVSVTGHdapgvkPGDv 303
Cdd:COG1088  217 RDWLYVEDHCRAIDLVLEKGRPgETYNIGGGNELSNLEVVELICDLLG----------KPESLITFVKDR------PGH- 279
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 445970335 304 iiavDPRYfrpaevetlLGDPTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:COG1088  280 ----DRRY---------AIDASKIRRELGWKPKVTFEEGLRKTVD 311
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
6-341 1.58e-29

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: 115.72  E-value: 1.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSF--NTERVDHIYQdphtcNPKFHLHYGDLSDTSNLTRILREVQPDEV 83
Cdd:cd05246    4 LVTGGAGFIGSNFVRYLLNKYPDYKIINLDKLTYagNLENLEDVSS-----SPRYRFVKGDICDAELVDRLFEEEKIDAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  84 YNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQ-KETTPFYPRSPYAVAKL 162
Cdd:cd05246   79 IHFAAESHVDRSISDPEPFIRTNVLGTYTLLEAARKYGVK---RFVHISTDEVYGDLLDDGEfTETSPLAPTSPYSASKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 YAYWITVNYRESYGMYA----CNgilfNHESPRRgetFVTRKITRAIANIAQGLESCLYlGNMDSLRDWGHAKDYVKMQW 238
Cdd:cd05246  156 AADLLVRAYHRTYGLPVvitrCS----NNYGPYQ---FPEKLIPLFILNALDGKPLPIY-GDGLNVRDWLYVEDHARAIE 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 239 MMLQQEQP-EDFVIATGVQYSVRQFVEMAAAQLGiklrfegtgvEEKGIVVSVT---GHDApgvkpgdviiavdpRYFRp 314
Cdd:cd05246  228 LVLEKGRVgEIYNIGGGNELTNLELVKLILELLG----------KDESLITYVKdrpGHDR--------------RYAI- 282
                        330       340
                 ....*....|....*....|....*..
gi 445970335 315 aevetllgDPTKAHEKLGWKPEITLRE 341
Cdd:cd05246  283 --------DSSKIRRELGWRPKVSFEE 301
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
6-347 5.86e-29

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: 114.32  E-value: 5.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASsfnteRVDHIYQDPHtCNPKFHLHYGDLSDTSNLTRILREVqpDEVYN 85
Cdd:cd05257    3 LVTGADGFIGSHLTERLLREGHEVRALDIYNS-----FNSWGLLDNA-VHDRFHFISGDVRDASEVEYLVKKC--DVVFH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQKETTPFY----PRSPYAVAK 161
Cdd:cd05257   75 LAALIAIPYSYTAPLSYVETNVFGTLNVLEAACVLYRK---RVVHTSTSEVYGTAQDVPIDEDHPLLyinkPRSPYSASK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 162 LYAYWITVNYRESYGM-YAcngIL--FNHESPRRGETFVTRKItraIANIAQGLEScLYLGNMDSLRDWGHAKDyvkmqw 238
Cdd:cd05257  152 QGADRLAYSYGRSFGLpVT---IIrpFNTYGPRQSARAVIPTI---ISQRAIGQRL-INLGDGSPTRDFNFVKD------ 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 239 mmlqqeqpedfviatgvqySVRQFVemaAAQLGIKLRFE----GTGVEekgIVVSVTGHDApGVKPGDVIIAV---DPRY 311
Cdd:cd05257  219 -------------------TARGFI---DILDAIEAVGEiinnGSGEE---ISIGNPAVEL-IVEELGEMVLIvydDHRE 272
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 445970335 312 FRPA--EVETLLGDPTKAHEKLGWKPEITLREMVSEMV 347
Cdd:cd05257  273 YRPGysEVERRIPDIRKAKRLLGWEPKYSLRDGLRETI 310
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
6-344 2.71e-28

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: 112.63  E-value: 2.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIkrraSSFNTERVDHIyqdPHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVYN 85
Cdd:cd05247    3 LVTGGAGYIGSHTVVELLEAGYDVVVL----DNLSNGHREAL---PRIEKIRIEFYEGDIRDRAALDKVFAEHKIDAVIH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGlekKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAY 165
Cdd:cd05247   76 FAALKAVGESVQKPLKYYDNNVVGTLNLLEAMRAHG---VKNFVFSSSAAVYGEPETVPITEEAPLNPTNPYGRTKLMVE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 166 WITVNYRESYGMyacNGIL---FN----HESPRRGEtfVTRKITRAIANIAQGLesclyLGNMDSL-------------- 224
Cdd:cd05247  153 QILRDLAKAPGL---NYVIlryFNpagaHPSGLIGE--DPQIPNNLIPYVLQVA-----LGRREKLaifgddyptpdgtc 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 225 -RDWGHAKDYVKMQWMMLQQEQPED----FVIATGVQYSVRQFVEMAaaqlgiklrfegtgveEKgivvsVTGHDAPgvk 299
Cdd:cd05247  223 vRDYIHVVDLADAHVLALEKLENGGgseiYNLGTGRGYSVLEVVEAF----------------EK-----VSGKPIP--- 278
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 445970335 300 pgdVIIAvdPRyfRPAEVETLLGDPTKAHEKLGWKPEITLREMVS 344
Cdd:cd05247  279 ---YEIA--PR--RAGDPASLVADPSKAREELGWKPKRDLEDMCE 316
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
3-348 2.67e-25

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: 103.87  E-value: 2.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIkrraSSFNTERVDHIYQdpHTCNPKFHLHYGDLSDTsnltrILREVqpDE 82
Cdd:cd05230    1 KRILITGGAGFLGSHLCDRLLEDGHEVICV----DNFFTGRKRNIEH--LIGHPNFEFIRHDVTEP-----LYLEV--DQ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEairfLGLEKKTRFYQASTSELYGLVQEIPQKET-----TPFYPRSPY 157
Cdd:cd05230   68 IYHLACPASPVHYQYNPIKTLKTNVLGTLNMLG----LAKRVGARVLLASTSEVYGDPEVHPQPESywgnvNPIGPRSCY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 158 AVAKLYAYWITVNYRESYGMYACNGILFNHESPRRGETFvtrkiTRAIAN-IAQGL--ESCLYLGNMDSLRDWGHAKDYV 234
Cdd:cd05230  144 DEGKRVAETLCMAYHRQHGVDVRIARIFNTYGPRMHPND-----GRVVSNfIVQALrgEPITVYGDGTQTRSFQYVSDLV 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 235 K-MQWMMLQQEQPEDFVIATGVQYSVRQFVEMaaaqlgiklrfegtgveekgiVVSVTGHDAPGV---KPGDviiavDPR 310
Cdd:cd05230  219 EgLIRLMNSDYFGGPVNLGNPEEFTILELAEL---------------------VKKLTGSKSEIVflpLPED-----DPK 272
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 445970335 311 YFRPaevetllgDPTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:cd05230  273 RRRP--------DISKAKELLGWEPKVPLEEGLRRTIE 302
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
3-348 5.14e-21

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: 92.76  E-value: 5.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASS----FNTERVDHIYQDphtcnpkfhlHYGDLSDTSNLTRILREV 78
Cdd:cd05252    5 KRVLVTGHTGFKGSWLSLWLQELGAKVIGYSLDPPTnpnlFELANLDNKISS----------TRGDIRDLNALREAIREY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  79 QPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKtrFYQASTSELYGLVQEI-PQKETTPFYPRSPY 157
Cdd:cd05252   75 EPEIVFHLAAQPLVRLSYKDPVETFETNVMGTVNLLEAIRETGSVKA--VVNVTSDKCYENKEWGwGYRENDPLGGHDPY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 158 AVAKLYAYWITVNYRESYgmyacngilFNHESPRRGETFVTrkITRA--------------IANIAQGLES--CLYLGNM 221
Cdd:cd05252  153 SSSKGCAELIISSYRNSF---------FNPENYGKHGIAIA--SARAgnvigggdwaedriVPDCIRAFEAgeRVIIRNP 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 222 DSLRDWGHAKDYVKMqWMMLQQEQPED---------FVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEekgivvsvtg 292
Cdd:cd05252  222 NAIRPWQHVLEPLSG-YLLLAEKLYERgeeyaeawnFGPDDEDAVTVLELVEAMARYWGEDARWDLDGNS---------- 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445970335 293 hdapgvkpgdviiavdpryfRPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:cd05252  291 --------------------HPHEANLLKLDCSKAKTMLGWRPRWNLEETLEFTVA 326
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
3-350 3.55e-20

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 90.48  E-value: 3.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLL-EKGYEVHGIKRRASSFNTERVDHIYQDPHtcnpkFHLHYGDLSDTSNLTRILREVQPD 81
Cdd:PRK10217   2 RKILITGGAGFIGSALVRYIInETSDAVVVVDKLTYAGNLMSLAPVAQSER-----FAFEKVDICDRAELARVFTEHQPD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  82 EVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIR----FLGLEKKT--RFYQASTSELYGLVQEIPQ--KETTPFYP 153
Cdd:PRK10217  77 CVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARaywnALTEDKKSafRFHHISTDEVYGDLHSTDDffTETTPYAP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 154 RSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRRgetFVTRKITRAIANIAQGLESCLYlGNMDSLRDWGHAKDY 233
Cdd:PRK10217 157 SSPYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYH---FPEKLIPLMILNALAGKPLPVY-GNGQQIRDWLYVEDH 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 234 VKMQWMMLQQEQPedfviatGVQYSVrqfvemaaaqlgiklrfeGTGVEEKGIVVSVTGHD-----APGVKPG-----DV 303
Cdd:PRK10217 233 ARALYCVATTGKV-------GETYNI------------------GGHNERKNLDVVETICElleelAPNKPQGvahyrDL 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445970335 304 IIAVDPryfRPAEVETLLGDPTKAHEKLGWKPEIT----LREMVSEMVAND 350
Cdd:PRK10217 288 ITFVAD---RPGHDLRYAIDASKIARELGWLPQETfesgMRKTVQWYLANE 335
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
6-348 1.12e-19

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: 88.55  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIkrraSSFNTervdhiYQDPH---------TCNPKFHLHYGDLSDTSNLTRILR 76
Cdd:cd05253    4 LVTGAAGFIGFHVAKRLLERGDEVVGI----DNLND------YYDVRlkearlellGKSGGFKFVKGDLEDREALRRLFK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  77 EVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKktrFYQASTSELYGLVQEIPQKETTPF-YPRS 155
Cdd:cd05253   74 DHEFDAVIHLAAQAGVRYSLENPHAYVDSNIVGFLNLLELCRHFGVKH---LVYASSSSVYGLNTKMPFSEDDRVdHPIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 156 PYAVAK------------LYAYWITV-NYRESYGMYA---------CNGIL-------FNHESPRRGETFV---TRKITR 203
Cdd:cd05253  151 LYAATKkanelmahtyshLYGIPTTGlRFFTVYGPWGrpdmalflfTKAILegkpidvFNDGNMSRDFTYIddiVEGVVR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 204 AIANIAQGlESCLYLGNMDSLRdwGHAkDYvkmqwmmlqqeqpEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEgtgvee 283
Cdd:cd05253  231 ALDTPAKP-NPNWDAEAPDPST--SSA-PY-------------RVYNIGNNSPVKLMDFIEALEKALGKKAKKN------ 287
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445970335 284 kgivvsvtghdapgVKPgdviiavdpryFRPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:cd05253  288 --------------YLP-----------MQKGDVPETYADISKLQRLLGYKPKTSLEEGVKRFVE 327
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
3-348 1.95e-19

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: 88.12  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGI---KRRASSFNTERVDHIYQDPhtcNPKFhLHyGDLSDTSNLTRILRevQ 79
Cdd:cd05258    1 MRVLITGGAGFIGSNLARFFLKQGWEVIGFdnlMRRGSFGNLAWLKANREDG---GVRF-VH-GDIRNRNDLEDLFE--D 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  80 PDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGleKKTRFYQASTSELYG-LVQEIPQKETTPFY------ 152
Cdd:cd05258   74 IDLIIHTAAQPSVTTSASSPRLDFETNALGTLNVLEAARQHA--PNAPFIFTSTNKVYGdLPNYLPLEELETRYelapeg 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 153 --------------PRSPYAVAKLYAYWITVNYRESYGMYA----CNGILFNHESPRRGETFVTRKITRAIANiaqglES 214
Cdd:cd05258  152 wspagisesfpldfSHSLYGASKGAADQYVQEYGRIFGLKTvvfrCGCLTGPRQFGTEDQGWVAYFLKCAVTG-----KP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 215 CLYLGN-MDSLRDWGHAKDYVKMQWMMLQQEQ---PEDFVIATGVQYSV--RQFVEMAAAQLGIKLRfegtgveekgivv 288
Cdd:cd05258  227 LTIFGYgGKQVRDVLHSADLVNLYLRQFQNPDrrkGEVFNIGGGRENSVslLELIALCEEITGRKME------------- 293
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 289 sVTGHDApgvKPGDVIIAVdpryfrpaevetllGDPTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:cd05258  294 -SYKDEN---RPGDQIWYI--------------SDIRKIKEKPGWKPERDPREILAEIYA 335
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
6-349 5.67e-17

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 81.98  E-value: 5.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIkrraSSFNTERVDHIYQdpHTCNPKFHLHYGDLSDTsnltrILREVqpDEVYN 85
Cdd:PLN02166 124 VVTGGAGFVGSHLVDKLIGRGDEVIVI----DNFFTGRKENLVH--LFGNPRFELIRHDVVEP-----ILLEV--DQIYH 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLeairflGLEKK--TRFYQASTSELYGLVQEIPQKET-----TPFYPRSPYA 158
Cdd:PLN02166 191 LACPASPVHYKYNPVKTIKTNVMGTLNML------GLAKRvgARFLLTSTSEVYGDPLEHPQKETywgnvNPIGERSCYD 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 159 VAKLYAYWITVNYRESYGMYACNGILFNHESPRrgetfVTRKITRAIAN-IAQGL--ESCLYLGNMDSLRDWGHAKDYVK 235
Cdd:PLN02166 265 EGKRTAETLAMDYHRGAGVEVRIARIFNTYGPR-----MCLDDGRVVSNfVAQTIrkQPMTVYGDGKQTRSFQYVSDLVD 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 236 MQWMMLQQEQPEDFVIATGVQYSVRQFVEmaaaqlgiklrfegtgVEEKGIVVSVTGHDAPGVkpgdviiAVDPRYFRPa 315
Cdd:PLN02166 340 GLVALMEGEHVGPFNLGNPGEFTMLELAE----------------VVKETIDSSATIEFKPNT-------ADDPHKRKP- 395
                        330       340       350
                 ....*....|....*....|....*....|....
gi 445970335 316 evetllgDPTKAHEKLGWKPEITLREMVSEMVAN 349
Cdd:PLN02166 396 -------DISKAKELLNWEPKISLREGLPLMVSD 422
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
5-346 6.48e-17

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: 80.44  E-value: 6.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   5 ALITGVTGQDGSYLAEFLLEKGYEVHGIKRR--ASSFNTERVDhiyqdphtcnpkfhLHYGDLSDTSNLTRILREVqpDE 82
Cdd:cd05264    2 VLIVGGNGFIGSHLVDALLEEGPQVRVFDRSipPYELPLGGVD--------------YIKGDYENRADLESALVGI--DT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKktRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKL 162
Cdd:cd05264   66 VIHLASTTNPATSNKNPILDIQTNVAPTVQLLEACAAAGIGK--IIFASSGGTVYGVPEQLPISESDPTLPISSYGISKL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 ----YAYWITVNY-------RES--YGMYacngilfnhESPRRGETFVTRKITRAIANiaqglESCLYLGNMDSLRDWGH 229
Cdd:cd05264  144 aiekYLRLYQYLYgldytvlRISnpYGPG---------QRPDGKQGVIPIALNKILRG-----EPIEIWGDGESIRDYIY 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 230 AKDYVKMQWMMLQQEQPED-FVIATGVQYSVRQFvemaaaqlgIKLRFEGTGVEEKGIVvsvtgHDAPGVKPGDVIIAVD 308
Cdd:cd05264  210 IDDLVEALMALLRSKGLEEvFNIGSGIGYSLAEL---------IAEIEKVTGRSVQVIY-----TPARTTDVPKIVLDIS 275
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 445970335 309 pryfrpaevetllgdptKAHEKLGWKPEITLREMVSEM 346
Cdd:cd05264  276 -----------------RARAELGWSPKISLEDGLEKT 296
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
55-235 1.61e-15

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 76.75  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  55 NPKFHLHYGDLSDTSNLTRILREVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRF----LGLEKKT--RF 128
Cdd:PRK10084  49 SERYVFEHADICDRAELDRIFAQHQPDAVMHLAAESHVDRSITGPAAFIETNIVGTYVLLEAARNywsaLDEDKKNafRF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 129 YQASTSELYG---------LVQEIPQ-KETTPFYPRSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRRgetFVT 198
Cdd:PRK10084 129 HHISTDEVYGdlphpdeveNSEELPLfTETTAYAPSSPYSASKASSDHLVRAWLRTYGLPTIVTNCSNNYGPYH---FPE 205
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 445970335 199 RKITRAIANIAQGLESCLYlGNMDSLRDWGHAKDYVK 235
Cdd:PRK10084 206 KLIPLVILNALEGKPLPIY-GKGDQIRDWLYVEDHAR 241
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
5-347 2.05e-15

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: 75.80  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   5 ALITGVTGQDGSYLAEFLLEKGYEVHGIKRrASSFNTErvdhiYQDPHTCNPKFHLHYGDLSDTSNLtRILREVqpDEVY 84
Cdd:cd05234    2 ILVTGGAGFIGSHLVDRLLEEGNEVVVVDN-LSSGRRE-----NIEPEFENKAFRFVKRDLLDTADK-VAKKDG--DTVF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  85 NLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYA 164
Cdd:cd05234   73 HLAANPDVRLGATDPDIDLEENVLATYNVLEAMRANGVK---RIVFASSSTVYGEAKVIPTPEDYPPLPISVYGASKLAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 165 YWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANiaqgLESCLYLGNMDSLRDWGHAKDYVKMqwMMLQQE 244
Cdd:cd05234  150 EALISAYAHLFGFQAWIFRFANIVGPRSTHGVIYDFINKLKRN----PNELEVLGDGRQRKSYLYVSDCVDA--MLLAWE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 245 QPED----FVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGveekgivvsvtghdapGVK--PGDViiavdPRYFRpaeve 318
Cdd:cd05234  224 KSTEgvniFNLGNDDTISVNEIAEIVIEELGLKPRFKYSG----------------GDRgwKGDV-----PYMRL----- 277
                        330       340
                 ....*....|....*....|....*....
gi 445970335 319 tllgDPTKAHeKLGWKPEITLREMVSEMV 347
Cdd:cd05234  278 ----DIEKLK-ALGWKPRYNSEEAVRKTV 301
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
6-348 5.50e-15

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: 74.85  E-value: 5.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIkrraSSFNTERVDHIyqDPHtcnPKFHLHYGDLSDTSNLTRILREVQPDEVYn 85
Cdd:cd08957    4 LITGGAGQIGSHLIEHLLERGHQVVVI----DNFATGRREHL--PDH---PNLTVVEGSIADKALVDKLFGDFKPDAVV- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 lgamsHVAVSFESP---EYTADVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGL---VQEIPQKETTpFYPRSPYAV 159
Cdd:cd08957   74 -----HTAAAYKDPddwYEDTLTNVVGGANVVQAAKKAGVK---RLIYFQTALCYGLkpmQQPIRLDHPR-APPGSSYAI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 160 AKlyaywiTVNyrESYGMYAcngilfnhesprrGETFVTRKITRAIA--NIAQGL----------ESCLYlgnMDSLRDW 227
Cdd:cd08957  145 SK------TAG--EYYLELS-------------GVDFVTFRLANVTGprNVIGPLptfyqrlkagKKCFV---TDTRRDF 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 228 GHAKDYVKMQWMMLQQEQPED-FVIATGVQYSVRQFVEMAAAQLGIKLRfegtgveekgivvsvtgHDAPGVKPGdviia 306
Cdd:cd08957  201 VFVKDLARVVDKALDGIRGHGaYHFSSGEDVSIKELFDAVVEALDLPLR-----------------PEVEVVELG----- 258
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 445970335 307 vdpryfrPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMVA 348
Cdd:cd08957  259 -------PDDVPSILLDPSRTFQDFGWKEFTPLSETVSAALA 293
PLN02206 PLN02206
UDP-glucuronate decarboxylase
6-349 9.13e-13

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 69.24  E-value: 9.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIkrraSSFNTERVDHIYQdpHTCNPKFHLHYGDLSDTsnltrILREVqpDEVYN 85
Cdd:PLN02206 123 VVTGGAGFVGSHLVDRLMARGDSVIVV----DNFFTGRKENVMH--HFSNPNFELIRHDVVEP-----ILLEV--DQIYH 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGA-MSHVAVSFeSPEYTADVDAMGTLRLLeairflGLEKKT--RFYQASTSELYGLVQEIPQKET-----TPFYPRSPY 157
Cdd:PLN02206 190 LACpASPVHYKF-NPVKTIKTNVVGTLNML------GLAKRVgaRFLLTSTSEVYGDPLQHPQVETywgnvNPIGVRSCY 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 158 AVAKLYAYWITVNYRESYGMYACNGILFNHESPRrgetfVTRKITRAIAN-IAQGL--ESCLYLGNMDSLRDWGHAKDYV 234
Cdd:PLN02206 263 DEGKRTAETLTMDYHRGANVEVRIARIFNTYGPR-----MCIDDGRVVSNfVAQALrkEPLTVYGDGKQTRSFQFVSDLV 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 235 KMQWMMLQQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKgivvsvtghdapgvkpgdviiavDPRYFRP 314
Cdd:PLN02206 338 EGLMRLMEGEHVGPFNLGNPGEFTMLELAKVVQETIDPNAKIEFRPNTED-----------------------DPHKRKP 394
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 445970335 315 aevetllgDPTKAHEKLGWKPEITLREMVSEMVAN 349
Cdd:PLN02206 395 --------DITKAKELLGWEPKVSLRQGLPLMVKD 421
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
3-355 2.90e-12

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: 66.73  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIyqdphtcnpKFHLhyGDLSDTSNLTRILREVqpDE 82
Cdd:cd05273    1 QRALVTGAGGFIGSHLAERLKAEGHYVRGADWKSPEHMTQPTDDD---------EFHL--VDLREMENCLKATEGV--DH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGAmSHVAVSFESPEYTADV--DAMGTLRLLEAIRFLGLEkktRFYQASTSELY-------GLVQEIPQKETTPFYP 153
Cdd:cd05273   68 VFHLAA-DMGGMGYIQSNHAVIMynNTLINFNMLEAARINGVE---RFLFASSACVYpefkqleTTVVRLREEDAWPAEP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 154 RSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRR----GETFVTRKITRAIAnIAQGLESCLYLGNMDSLRDWGH 229
Cdd:cd05273  144 QDAYGWEKLATERLCQHYNEDYGIETRIVRFHNIYGPRGtwdgGREKAPAAMCRKVA-TAKDGDRFEIWGDGLQTRSFTY 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 230 AKDYVKMQWMMLQQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEgtgveekgivvsvtgHDAPGvkpgdviiavdp 309
Cdd:cd05273  223 IDDCVEGLRRLMESDFGEPVNLGSDEMVSMNELAEMVLSFSGKPLEII---------------HHTPG------------ 275
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 445970335 310 ryfrPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMV---ANDLEAAK 355
Cdd:cd05273  276 ----PQGVRGRNSDNTLLKEELGWEPNTPLEEGLRITYfwiKEQIEAEK 320
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
5-162 3.47e-11

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 61.26  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   5 ALITGVTGQDGSYLAEFLLEKGYEVHGIKRrassfNTERVDHIYQDPhtcnpkFHLHYGDLSDTSNLTRILRevQPDEVY 84
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVR-----NTKRLSKEDQEP------VAVVEGDLRDLDSLSDAVQ--GVDVVI 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445970335  85 NLGAMSHVAVSFEspeytaDVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGlvqeiPQKETTPFYPRSPYAVAKL 162
Cdd:cd05226   68 HLAGAPRDTRDFC------EVDVEGTRNVLEAAKEAGVK---HFIFISSLGAYG-----DLHEETEPSPSSPYLAVKA 131
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
6-345 5.68e-11

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 62.91  E-value: 5.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNT--ERVDHIYQDphtcNPKFHlhYGDLSDTSNLTRILREVQPDEV 83
Cdd:PRK10675   4 LVTGGSGYIGSHTCVQLLQNGHDVVILDNLCNSKRSvlPVIERLGGK----HPTFV--EGDIRNEALLTEILHDHAIDTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  84 YNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLekkTRFYQASTSELYGLVQEIPQKETTPF-YPRSPYAVAKL 162
Cdd:PRK10675  78 IHFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANV---KNLIFSSSATVYGDQPKIPYVESFPTgTPQSPYGKSKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 YAYWITVNYRESYGMYACNGI-LFN----HESPRRGE--TFVTRKITRAIANIAQG-LESCLYLGN------MDSLRDWG 228
Cdd:PRK10675 155 MVEQILTDLQKAQPDWSIALLrYFNpvgaHPSGDMGEdpQGIPNNLMPYIAQVAVGrRDSLAIFGNdyptedGTGVRDYI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 229 HAKDYVKMQWMMLQQEQPEDFV----IATGVQYSVRQFVEMAAAQLGIKLRFegtgveekgivvsvtgHDAPGvKPGDVi 304
Cdd:PRK10675 235 HVMDLADGHVAAMEKLANKPGVhiynLGAGVGSSVLDVVNAFSKACGKPVNY----------------HFAPR-REGDL- 296
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 445970335 305 iavdPRYFrpaevetllGDPTKAHEKLGWKPEITLREMVSE 345
Cdd:PRK10675 297 ----PAYW---------ADASKADRELNWRVTRTLDEMAQD 324
PLN02240 PLN02240
UDP-glucose 4-epimerase
1-342 1.17e-10

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 62.29  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   1 MSKVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFnTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQP 80
Cdd:PLN02240   4 MGRTILVTGGAGYIGSHTVLQLLLAGYKVVVIDNLDNSS-EEALRRVKELAGDLGDNLVFHKVDLRDKEALEKVFASTRF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  81 DEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLeKKTRFyqASTSELYGLVQEIPQKETTPFYPRSPYAVA 160
Cdd:PLN02240  83 DAVIHFAGLKAVGESVAKPLLYYDNNLVGTINLLEVMAKHGC-KKLVF--SSSATVYGQPEEVPCTEEFPLSATNPYGRT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 161 KLYAYWITVNYRESYGMYACngIL---FN----HESPRRGETfvtrkiTRAIAN--------IAQG-LESCLYLGN---- 220
Cdd:PLN02240 160 KLFIEEICRDIHASDPEWKI--ILlryFNpvgaHPSGRIGED------PKGIPNnlmpyvqqVAVGrRPELTVFGNdypt 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 221 MD--SLRDW--------GHAKDYVKMqwmmlqQEQP----EDFVIATGVQYSVrqfVEMAAAqlgiklrFEgtgveekgi 286
Cdd:PLN02240 232 KDgtGVRDYihvmdladGHIAALRKL------FTDPdigcEAYNLGTGKGTSV---LEMVAA-------FE--------- 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445970335 287 vvSVTGHDAPgvkpgdviIAVDPRyfRPAEVETLLGDPTKAHEKLGWKPEITLREM 342
Cdd:PLN02240 287 --KASGKKIP--------LKLAPR--RPGDAEEVYASTEKAEKELGWKAKYGIDEM 330
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
5-164 3.85e-09

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: 57.30  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   5 ALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASsfNTERVDHiyqdphtcnPKFHLHYGDLSDTSNLTRILREVqpDEVY 84
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGS--DAVLLDG---------LPVEVVEGDLTDAASLAAAMKGC--DRVF 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  85 NLGAMshvaVSFESPEYTA--DVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYGLVQEIPQKETTPFYPRS---PYAV 159
Cdd:cd05228   68 HLAAF----TSLWAKDRKElyRTNVEGTRNVLDAALEAGVR---RVVHTSSIAALGGPPDGRIDETTPWNERPfpnDYYR 140

                 ....*
gi 445970335 160 AKLYA 164
Cdd:cd05228  141 SKLLA 145
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
6-162 2.51e-08

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: 54.55  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRassfntervdhiyqdpHTCNPKFhlhygDLSDTSNLTRILREVQPDEVYN 85
Cdd:cd05254    3 LITGATGMLGRALVRLLKERGYEVIGTGRS----------------RASLFKL-----DLTDPDAVEEAIRDYKPDVIIN 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGlekkTRFYQASTselyGLV---QEIPQKETTPFYPRSPYAVAKL 162
Cdd:cd05254   62 CAAYTRVDKCESDPELAYRVNVLAPENLARAAKEVG----ARLIHIST----DYVfdgKKGPYKEEDAPNPLNVYGKSKL 133
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
6-341 8.10e-08

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: 53.12  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHiyqdphtcnpkfhlhygDLSDTSNLTRILREVqpDEVYN 85
Cdd:cd05232    3 LVTGANGFIGRALVDKLLSRGEEVRIAVRNAENAEPSVVLA-----------------ELPDIDSFTDLFLGV--DAVVH 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTA--DVDAMGTLRLLEAIRFLGLEkktRFYQASTSELYG-LVQEIPQKETTPFYPRSPYAVAKL 162
Cdd:cd05232   64 LAARVHVMNDQGADPLSDyrKVNTELTRRLARAAARQGVK---RFVFLSSVKVNGeGTVGAPFDETDPPAPQDAYGRSKL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 163 YAYWITVNYRESYGMYACngILfnhESPRRGETFVTRKITRAIANIAQGLEscLYLGNMDSLRDWGHAKDYVkmQWMMLQ 242
Cdd:cd05232  141 EAERALLELGASDGMEVV--IL---RPPMVYGPGVRGNFARLMRLIDRGLP--LPPGAVKNRRSLVSLDNLV--DAIYLC 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335 243 QEQP----EDFVIATGVQYSVRQFVEMAAAQLGIKLR--FEGTGVEEkgIVVSVTGhdapgvkpgdviiavdpryfRPAE 316
Cdd:cd05232  212 ISLPkaanGTFLVSDGPPVSTAELVDEIRRALGKPTRllPVPAGLLR--FAAKLLG--------------------KRAV 269
                        330       340
                 ....*....|....*....|....*....
gi 445970335 317 VETLLG----DPTKAHEKLGWKPEITLRE 341
Cdd:cd05232  270 IQRLFGslqyDPEKTQNELGWRPPISLEE 298
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
51-177 2.87e-07

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 52.44  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  51 PHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVYNLGAMSHVAVSF-ESPEYTADvDAMGTLRLLEAIRFLGLEKktRFY 129
Cdd:PLN02260  52 PSKSSPNFKFVKGDIASADLVNYLLITEGIDTIMHFAAQTHVDNSFgNSFEFTKN-NIYGTHVLLEACKVTGQIR--RFI 128
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445970335 130 QASTSELYGLVQE---IPQKETTPFYPRSPYAVAKLYAYWITVNYRESYGM 177
Cdd:PLN02260 129 HVSTDEVYGETDEdadVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGL 179
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
6-118 7.51e-07

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: 50.35  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASsfNTERVDHIYqDPHTCNPKFHLHYGDLSDTSNltrILREVQPDEVYN 85
Cdd:cd05227    3 LVTGATGFIASHIVEQLLKAGYKVRGTVRSLS--KSAKLKALL-KAAGYNDRLEFVIVDDLTAPN---AWDEALKGVDYV 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 445970335  86 LgamsHVA--VSFESPEYTADVDAM---GTLRLLEAIR 118
Cdd:cd05227   77 I----HVAspFPFTGPDAEDDVIDPaveGTLNVLEAAK 110
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
1-124 8.38e-07

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: 49.92  E-value: 8.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   1 MSKVALITGVTGQDGSYLAEFLLEKG-YEVHGIKRraSSFNTERVDHIYQDpHTCNPKFHLHYGDLSDTSNLTRILREVQ 79
Cdd:cd05237    1 KGKTILVTGGAGSIGSELVRQILKFGpKKLIVFDR--DENKLHELVRELRS-RFPHDKLRFIIGDVRDKERLRRAFKERG 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445970335  80 PDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEK 124
Cdd:cd05237   78 PDIVFHAAALKHVPSMEDNPEEAIKTNVLGTKNVIDAAIENGVEK 122
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
6-118 1.58e-06

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: 48.30  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVhgikrRASSFNTERVDHIYqdphtcNPKFHLHYGDLSDTSNLTRILREVqpDEVYN 85
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARGHPV-----RALVRDPEKAAALA------AAGVEVVQGDLDDPESLAAALAGV--DAVFL 69
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445970335  86 LGAMSHVAvsfespeyTADVDAMGTLRLLEAIR 118
Cdd:COG0702   70 LVPSGPGG--------DFAVDVEGARNLADAAK 94
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
6-162 2.26e-06

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


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 48.81  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335    6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRAssfntervdhiyqdphtcnpkfhlhyGDLSDTSNLTRILREVQPDEVYN 85
Cdd:pfam04321   2 LITGANGQLGTELRRLLAERGIEVVALTRAE--------------------------LDLTDPEAVARLLREIKPDVVVN 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445970335   86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRflglEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKL 162
Cdd:pfam04321  56 AAAYTAVDKAESEPDLAYAINALAPANLAEACA----AVGAPLIHISTDYVFDGTKPRPYEEDDETNPLNVYGRTKL 128
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
3-83 2.39e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.44  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDhIYqdphtcNPKFHLHYGDLSDTSNLTR----ILREV 78
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAE-QY------NSNLTFHSLDLQDVHELETnfneILSSI 74

                 ....*
gi 445970335  79 QPDEV 83
Cdd:PRK06924  75 QEDNV 79
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
6-162 2.98e-05

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: 45.45  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIkrrassfNTERVDHIY--QDPH-TCnpkfhlHYGDLSDTSNLTRILREVqPDE 82
Cdd:cd05238    4 LITGASGFVGQRLAERLLSDVPNERLI-------LIDVVSPKApsGAPRvTQ------IAGDLAVPALIEALANGR-PDV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  83 VYNLGA-MSHVAVSFESPEYTADVDamGTLRLLEAIRFLGleKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAK 161
Cdd:cd05238   70 VFHLAAiVSGGAEADFDLGYRVNVD--GTRNLLEALRKNG--PKPRFVFTSSLAVYGLPLPNPVTDHTALDPASSYGAQK 145

                 .
gi 445970335 162 L 162
Cdd:cd05238  146 A 146
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
6-164 5.20e-05

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


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 44.70  E-value: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVqpDEVYN 85
Cdd:PRK15181  19 LITGVAGFIGSGLLEELLFLNQTVIGLDNFSTGYQHNLDDVRTSVSEEQWSRFIFIQGDIRKFTDCQKACKNV--DYVLH 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  86 LGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLekkTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAK---- 161
Cdd:PRK15181  97 QAALGSVPRSLKDPIATNSANIDGFLNMLTAARDAHV---SSFTYAASSSTYGDHPDLPKIEERIGRPLSPYAVTKyvne 173

                 ...
gi 445970335 162 LYA 164
Cdd:PRK15181 174 LYA 176
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
5-128 8.35e-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: 43.76  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   5 ALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASsfNTERVDHIYQDPHTCNPkFHLHYGDLSDtsnltrilrEVQPDEVY 84
Cdd:cd05193    1 VLVTGASGFVASHVVEQLLERGYKVRATVRDPS--KVKKVNHLLDLDAKPGR-LELAVADLTD---------EQSFDEVI 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445970335  85 -NLGAMSHVA--VSFESPE----YTADVDamGTLRLLEAIRFLGLEKKTRF 128
Cdd:cd05193   69 kGCAGVFHVAtpVSFSSKDpnevIKPAIG--GTLNALKAAAAAKSVKRFVL 117
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
3-124 1.22e-04

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


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 43.39  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   3 KVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRassfnteRVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVqpDE 82
Cdd:cd05271    1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRC-------EAYARRLLVMGDLGQVLFVEFDLRDDESIRKALEGS--DV 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445970335  83 VYNLgamshVAVSFESPEYT-ADVDAMGTLRLLEAIRFLGLEK 124
Cdd:cd05271   72 VINL-----VGRLYETKNFSfEDVHVEGPERLAKAAKEAGVER 109
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
6-176 1.84e-04

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


Pssm-ID: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 43.07  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKgyevhgikrrassFNTERVdhIYQD------PHTCNPKFhlHYGDLSDTSNLTRILREVQ 79
Cdd:cd05272    3 LITGGLGQIGSELAKLLRKR-------------YGKDNV--IASDirkppaHVVLSGPF--EYLDVLDFKSLEEIVVNHK 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  80 PDEVYNLGA-MShvAVSFESPEYTADVDAMGTLRLLEAIRflglEKKTRFYQASTSELYGlvQEIPqKETTPFY----PR 154
Cdd:cd05272   66 ITWIIHLAAlLS--AVGEKNPPLAWDVNMNGLHNVLELAR----EHNLRIFVPSTIGAFG--PTTP-RNNTPDDtiqrPR 136
                        170       180
                 ....*....|....*....|..
gi 445970335 155 SPYAVAKLYAYWITVNYRESYG 176
Cdd:cd05272  137 TIYGVSKVAAELLGEYYHHKFG 158
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-116 5.38e-04

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 41.01  E-value: 5.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   1 MSKVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRAssfntERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQP 80
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDA-----ERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445970335  81 DE------VYNLGAMSHVAVSFESPE---YTADVDAMGTLRLLEA 116
Cdd:COG0300   79 RFgpidvlVNNAGVGGGGPFEELDLEdlrRVFEVNVFGPVRLTRA 123
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
7-118 2.49e-03

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


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 39.25  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   7 ITGVTGQDGSYLAEFLLEKGYEVHGIKRraSSFNTERVDHIYQDPHTcnpkfhlhyGDLSDTSNLTRilREVQPDEVYNL 86
Cdd:cd05262    5 VTGATGFIGSAVVRELVAAGHEVVGLAR--SDAGAAKLEAAGAQVHR---------GDLEDLDILRK--AAAEADAVIHL 71
                         90       100       110
                 ....*....|....*....|....*....|..
gi 445970335  87 GAmSHvavSFESPEYTADVDAMGTLRLLEAIR 118
Cdd:cd05262   72 AF-TH---DFDNFAQACEVDRRAIEALGEALR 99
PRK11908 PRK11908
bifunctional UDP-4-keto-pentose/UDP-xylose synthase;
1-165 3.62e-03

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


Pssm-ID: 183375 [Multi-domain]  Cd Length: 347  Bit Score: 38.93  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   1 MSKVaLITGVTGQDGSYLAEFLLE-KGYEVHGIkrrasSFNTERVDHIYQdphtcNPKFHLHYGDLsdTSNLTRILREVQ 79
Cdd:PRK11908   1 MKKV-LILGVNGFIGHHLSKRILEtTDWEVYGM-----DMQTDRLGDLVN-----HPRMHFFEGDI--TINKEWIEYHVK 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335  80 P-DEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAirflGLEKKTRFYQASTSELYGLVQ--EIPQKETTPFY---- 152
Cdd:PRK11908  68 KcDVILPLVAIATPATYVKQPLRVFELDFEANLPIVRS----AVKYGKHLVFPSTSEVYGMCPdeEFDPEASPLVYgpin 143
                        170       180
                 ....*....|....*....|
gi 445970335 153 -PRSPYAVAK------LYAY 165
Cdd:PRK11908 144 kPRWIYACSKqlmdrvIWAY 163
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
6-156 4.93e-03

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: 38.49  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970335   6 LITGVTGQDGSYLAEFLLEKG-YEVHGIKRRassfntervdHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVY 84
Cdd:cd09813    3 LVVGGSGFLGRHLVEQLLRRGnPTVHVFDIR----------PTFELDPSSSGRVQFHTGDLTDPQDLEKAFNEKGPNVVF 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445970335  85 NLGAMSHVAvsfeSPEYTADVDAMGTLRLLEAIRFLGLEKktRFYQASTSELYGLVQEIPQKETTPfYPRSP 156
Cdd:cd09813   73 HTASPDHGS----NDDLYYKVNVQGTRNVIEACRKCGVKK--LVYTSSASVVFNGQDIINGDESLP-YPDKH 137
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
263-308 7.66e-03

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 35.43  E-value: 7.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 445970335   263 VEMAAAQLGIKLRfeGTGVEEKGIVVSVTGHDAP----GVKPGDVIIAVD 308
Cdd:smart00228   7 LEKGGGGLGFSLV--GGKDEGGGVVVSSVVPGSPaakaGLRVGDVILEVN 54
 
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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