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Conserved domains on  [gi|568981792|ref|XP_006516719|]
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GDP-mannose 4,6 dehydratase isoform X1 [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
34-285 7.58e-175

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


The actual alignment was detected with superfamily member TIGR01472:

Pssm-ID: 451247 [Multi-domain]  Cd Length: 343  Bit Score: 486.27  E-value: 7.58e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792   34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFR 113
Cdd:TIGR01472  92 KVSFEIPEYTADVDGIGTLRLLEAVRTLGLIKSVKFYQASTSELYGKVQEIPQNETTPFYPRSPYAAAKLYAHWITVNYR 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  114 EAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIA 193
Cdd:TIGR01472 172 EAYGLFAVNGILFNHESPRRGENFVTRKITRAAAKIKLGLQEKLYLGNLDAKRDWGHAKDYVEAMWLMLQQDKPDDYVIA 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  194 TGEVHSVREFVEKSFMHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDEL 273
Cdd:TIGR01472 252 TGETHSVREFVEVSFEYIGKTLNWKDKGINEVGRCKETGKVHVEIDPRYFRPTEVDLLLGDATKAKEKLGWKPEVSFEKL 331
                         250
                  ....*....|..
gi 568981792  274 VREMVQADVELM 285
Cdd:TIGR01472 332 VKEMVEEDLELA 343
 
Name Accession Description Interval E-value
gmd TIGR01472
GDP-mannose 4,6-dehydratase; Alternate name: GDP-D-mannose dehydratase. This enzyme converts ...
34-285 7.58e-175

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: 486.27  E-value: 7.58e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792   34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFR 113
Cdd:TIGR01472  92 KVSFEIPEYTADVDGIGTLRLLEAVRTLGLIKSVKFYQASTSELYGKVQEIPQNETTPFYPRSPYAAAKLYAHWITVNYR 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  114 EAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIA 193
Cdd:TIGR01472 172 EAYGLFAVNGILFNHESPRRGENFVTRKITRAAAKIKLGLQEKLYLGNLDAKRDWGHAKDYVEAMWLMLQQDKPDDYVIA 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  194 TGEVHSVREFVEKSFMHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDEL 273
Cdd:TIGR01472 252 TGETHSVREFVEVSFEYIGKTLNWKDKGINEVGRCKETGKVHVEIDPRYFRPTEVDLLLGDATKAKEKLGWKPEVSFEKL 331
                         250
                  ....*....|..
gi 568981792  274 VREMVQADVELM 285
Cdd:TIGR01472 332 VKEMVEEDLELA 343
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
36-277 2.03e-162

GDP-mannose 4,6 dehydratase;


Pssm-ID: 435301 [Multi-domain]  Cd Length: 327  Bit Score: 454.31  E-value: 2.03e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792   36 SFDLAEYTADVDGVGTLRLLDAIKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREA 115
Cdd:pfam16363  88 SFEQPEYTADTNVLGTLRLLEAIRSLGLEKKVRFYQASTSEVYGKVQEVPQTETTPFYPRSPYAAAKLYADWIVVNYRES 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  116 YNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATG 195
Cdd:pfam16363 168 YGLFACNGILFNHESPRRGERFVTRKITRGVARIKLGKQEKLYLGNLDAKRDWGHARDYVEAMWLMLQQDKPDDYVIATG 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  196 EVHSVREFVEKSFMHIGKTIVWEGKNENevGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDELVR 275
Cdd:pfam16363 248 ETHTVREFVEKAFLELGLTITWEGKGEI--GYFKASGKVHVLIDPRYFRPGEVDRLLGDPSKAKEELGWKPKVSFEELVR 325

                  ..
gi 568981792  276 EM 277
Cdd:pfam16363 326 EM 327
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
34-286 2.70e-158

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


Pssm-ID: 224014 [Multi-domain]  Cd Length: 345  Bit Score: 444.49  E-value: 2.70e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLInSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFR 113
Cdd:COG1089   92 GVSFEQPEYTADVDAIGTLRLLEAIRILGEK-KTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAYWITVNYR 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 114 EAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIA 193
Cdd:COG1089  171 ESYGLFACNGILFNHESPLRGETFVTRKITRAVARIKLGLQDKLYLGNLDAKRDWGHAKDYVEAMWLMLQQEEPDDYVIA 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 194 TGEVHSVREFVEKSFMHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDEL 273
Cdd:COG1089  251 TGETHSVREFVELAFEMVGIDLEWEGTGVDEKGVDAKTGKIIVEIDPRYFRPAEVDLLLGDPTKAKEKLGWRPEVSLEEL 330
                        250
                 ....*....|...
gi 568981792 274 VREMVQADVELMR 286
Cdd:COG1089  331 VREMVEADLEAAR 343
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
35-283 4.97e-145

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: 409.68  E-value: 4.97e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  35 ISFDLAEYTADVDGVGTLRLLDAIKTCGLinSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFRE 114
Cdd:cd05260   87 VSFDDPEYTAEVNAVGTLNLLEAIRILGL--DARFYQASSSEEYGKVQELPQSETTPFRPRSPYAVSKLYADWITRNYRE 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 115 AYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIAT 194
Cdd:cd05260  165 AYGLFAVNGRLFNHEGPRRGETFVTRKITRQVARIKAGLQPVLKLGNLDAKRDWGDARDYVEAYWLLLQQGEPDDYVIAT 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 195 GEVHSVREFVEKSFMHIGktivwegknenevgrckETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDELV 274
Cdd:cd05260  245 GETHSVREFVELAFEESG-----------------LTGDIEVEIDPRYFRPTEVDLLLGDPSKAREELGWKPEVSFEELV 307

                 ....*....
gi 568981792 275 REMVQADVE 283
Cdd:cd05260  308 REMLDADLE 316
PLN02653 PLN02653
GDP-mannose 4,6-dehydratase
34-286 1.02e-132

GDP-mannose 4,6-dehydratase


Pssm-ID: 178259 [Multi-domain]  Cd Length: 340  Bit Score: 379.50  E-value: 1.02e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLINS--VKFYQASTSELYGKVQEiPQKETTPFYPRSPYGAAKLYAYWIVVN 111
Cdd:PLN02653  97 AVSFEMPDYTADVVATGALRLLEAVRLHGQETGrqIKYYQAGSSEMYGSTPP-PQSETTPFHPRSPYAVAKVAAHWYTVN 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 112 FREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFV 191
Cdd:PLN02653 176 YREAYGLFACNGILFNHESPRRGENFVTRKITRAVGRIKVGLQKKLFLGNLDASRDWGFAGDYVEAMWLMLQQEKPDDYV 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 192 IATGEVHSVREFVEKSFMHIGKtivwegknenevgrckeTGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFD 271
Cdd:PLN02653 256 VATEESHTVEEFLEEAFGYVGL-----------------NWKDHVEIDPRYFRPAEVDNLKGDASKAREVLGWKPKVGFE 318
                        250
                 ....*....|....*
gi 568981792 272 ELVREMVQADVELMR 286
Cdd:PLN02653 319 QLVKMMVDEDLELAK 333
 
Name Accession Description Interval E-value
gmd TIGR01472
GDP-mannose 4,6-dehydratase; Alternate name: GDP-D-mannose dehydratase. This enzyme converts ...
34-285 7.58e-175

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: 486.27  E-value: 7.58e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792   34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFR 113
Cdd:TIGR01472  92 KVSFEIPEYTADVDGIGTLRLLEAVRTLGLIKSVKFYQASTSELYGKVQEIPQNETTPFYPRSPYAAAKLYAHWITVNYR 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  114 EAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIA 193
Cdd:TIGR01472 172 EAYGLFAVNGILFNHESPRRGENFVTRKITRAAAKIKLGLQEKLYLGNLDAKRDWGHAKDYVEAMWLMLQQDKPDDYVIA 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  194 TGEVHSVREFVEKSFMHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDEL 273
Cdd:TIGR01472 252 TGETHSVREFVEVSFEYIGKTLNWKDKGINEVGRCKETGKVHVEIDPRYFRPTEVDLLLGDATKAKEKLGWKPEVSFEKL 331
                         250
                  ....*....|..
gi 568981792  274 VREMVQADVELM 285
Cdd:TIGR01472 332 VKEMVEEDLELA 343
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
36-277 2.03e-162

GDP-mannose 4,6 dehydratase;


Pssm-ID: 435301 [Multi-domain]  Cd Length: 327  Bit Score: 454.31  E-value: 2.03e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792   36 SFDLAEYTADVDGVGTLRLLDAIKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREA 115
Cdd:pfam16363  88 SFEQPEYTADTNVLGTLRLLEAIRSLGLEKKVRFYQASTSEVYGKVQEVPQTETTPFYPRSPYAAAKLYADWIVVNYRES 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  116 YNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATG 195
Cdd:pfam16363 168 YGLFACNGILFNHESPRRGERFVTRKITRGVARIKLGKQEKLYLGNLDAKRDWGHARDYVEAMWLMLQQDKPDDYVIATG 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  196 EVHSVREFVEKSFMHIGKTIVWEGKNENevGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDELVR 275
Cdd:pfam16363 248 ETHTVREFVEKAFLELGLTITWEGKGEI--GYFKASGKVHVLIDPRYFRPGEVDRLLGDPSKAKEELGWKPKVSFEELVR 325

                  ..
gi 568981792  276 EM 277
Cdd:pfam16363 326 EM 327
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
34-286 2.70e-158

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


Pssm-ID: 224014 [Multi-domain]  Cd Length: 345  Bit Score: 444.49  E-value: 2.70e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLInSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFR 113
Cdd:COG1089   92 GVSFEQPEYTADVDAIGTLRLLEAIRILGEK-KTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAYWITVNYR 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 114 EAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIA 193
Cdd:COG1089  171 ESYGLFACNGILFNHESPLRGETFVTRKITRAVARIKLGLQDKLYLGNLDAKRDWGHAKDYVEAMWLMLQQEEPDDYVIA 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 194 TGEVHSVREFVEKSFMHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDEL 273
Cdd:COG1089  251 TGETHSVREFVELAFEMVGIDLEWEGTGVDEKGVDAKTGKIIVEIDPRYFRPAEVDLLLGDPTKAKEKLGWRPEVSLEEL 330
                        250
                 ....*....|...
gi 568981792 274 VREMVQADVELMR 286
Cdd:COG1089  331 VREMVEADLEAAR 343
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
35-283 4.97e-145

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: 409.68  E-value: 4.97e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  35 ISFDLAEYTADVDGVGTLRLLDAIKTCGLinSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFRE 114
Cdd:cd05260   87 VSFDDPEYTAEVNAVGTLNLLEAIRILGL--DARFYQASSSEEYGKVQELPQSETTPFRPRSPYAVSKLYADWITRNYRE 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 115 AYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIAT 194
Cdd:cd05260  165 AYGLFAVNGRLFNHEGPRRGETFVTRKITRQVARIKAGLQPVLKLGNLDAKRDWGDARDYVEAYWLLLQQGEPDDYVIAT 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 195 GEVHSVREFVEKSFMHIGktivwegknenevgrckETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDELV 274
Cdd:cd05260  245 GETHSVREFVELAFEESG-----------------LTGDIEVEIDPRYFRPTEVDLLLGDPSKAREELGWKPEVSFEELV 307

                 ....*....
gi 568981792 275 REMVQADVE 283
Cdd:cd05260  308 REMLDADLE 316
PLN02653 PLN02653
GDP-mannose 4,6-dehydratase
34-286 1.02e-132

GDP-mannose 4,6-dehydratase


Pssm-ID: 178259 [Multi-domain]  Cd Length: 340  Bit Score: 379.50  E-value: 1.02e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLINS--VKFYQASTSELYGKVQEiPQKETTPFYPRSPYGAAKLYAYWIVVN 111
Cdd:PLN02653  97 AVSFEMPDYTADVVATGALRLLEAVRLHGQETGrqIKYYQAGSSEMYGSTPP-PQSETTPFHPRSPYAVAKVAAHWYTVN 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 112 FREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFV 191
Cdd:PLN02653 176 YREAYGLFACNGILFNHESPRRGENFVTRKITRAVGRIKVGLQKKLFLGNLDASRDWGFAGDYVEAMWLMLQQEKPDDYV 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 192 IATGEVHSVREFVEKSFMHIGKtivwegknenevgrckeTGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFD 271
Cdd:PLN02653 256 VATEESHTVEEFLEEAFGYVGL-----------------NWKDHVEIDPRYFRPAEVDNLKGDASKAREVLGWKPKVGFE 318
                        250
                 ....*....|....*
gi 568981792 272 ELVREMVQADVELMR 286
Cdd:PLN02653 319 QLVKMMVDEDLELAK 333
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
36-193 8.55e-61

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: 192.90  E-value: 8.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792   36 SFDLAEYTADVDGVGTLRLLDAIKTCGLinsVKFYQASTSELYGKVQEIPQKETT---PFYPRSPYGAAKLYAYWIVVNF 112
Cdd:pfam01370  80 SIEDPEDFIEANVLGTLNLLEAARKAGV---KRFLFASSSEVYGDGAEIPQEETTltgPLAPNSPYAAAKLAGEWLVLAY 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  113 REAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQlECFSLGNLDAKRDWGHAKDYVEAMWLMLQN--DEPEDF 190
Cdd:pfam01370 157 AAAYGLRAVILRLFNVYGPGDNEGFVSRVIPALIRRILEGK-PILLWGDGTQRRDFLYVDDVARAILLALEHgaVKGEIY 235

                  ...
gi 568981792  191 VIA 193
Cdd:pfam01370 236 NIG 238
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
36-188 7.79e-28

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: 106.23  E-value: 7.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  36 SFDLAEYTADVDGVGTLRLLDAIKTCGLInsvKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREA 115
Cdd:cd08946   46 SWDNPDEDFETNVVGTLNLLEAARKAGVK---RFVYASSASVYGSPEGLPEEEETPPRPLSPYGVSKLAAEHLLRSYGES 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981792 116 YNLFAVNGILFNHESPRRGANFvTRKISRSVAKIYLGQ-LECFslGNLDAKRDWGHAKDYVEAMWLMLQNDEPE 188
Cdd:cd08946  123 YGLPVVILRLANVYGPGQRPRL-DGVVNDFIRRALEGKpLTVF--GGGNQTRDFIHVDDVVRAILHALENPLEG 193
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
34-278 1.42e-22

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: 94.59  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  34 QISFDLAEYTADVDGVGTLRLLDAIKTCGLinsVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFR 113
Cdd:cd05256   80 PRSIEDPIKDHEVNVLGTLNLLEAARKAGV---KRFVYASSSSVYGDPPYLPKDEDHPPNPLSPYAVSKYAGELYCQVFA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 114 EAYNLFAVNGILFNHESPRRG---------ANFVTRKISRSVAKIYlgqlecfslGNLDAKRDWGHAKDYVEAMWLMLQN 184
Cdd:cd05256  157 RLYGLPTVSLRYFNVYGPRQDpnggyaaviPIFIERALKGEPPTIY---------GDGEQTRDFTYVEDVVEANLLAATA 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 185 DEPED-FVIATGEVHSVREFVEKsfmhigktivwegknenevgrCKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLN 263
Cdd:cd05256  228 GAGGEvYNIGTGKRTSVNELAEL---------------------IREILGKELEPVYAPPRPGDVRHSLADISKAKKLLG 286
                        250
                 ....*....|....*
gi 568981792 264 WKPRVAFDELVREMV 278
Cdd:cd05256  287 WEPKVSFEEGLRLTV 301
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
40-279 2.46e-21

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


Pssm-ID: 223528 [Multi-domain]  Cd Length: 314  Bit Score: 91.54  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  40 AEYTADVDGVGTLRLLDAIKTCGLInsvKFYQAST-SELYGKVQEIPQKET-TPFYPRSPYGAAKLYAYWIVVNFREAYN 117
Cdd:COG0451   85 PAEFLDVNVDGTLNLLEAARAAGVK---RFVFASSvSVVYGDPPPLPIDEDlGPPRPLNPYGVSKLAAEQLLRAYARLYG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 118 LFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEV 197
Cdd:COG0451  162 LPVVILRPFNVYGPGDKPDLSSGVVSAFIRQLLKGEPIIVIGGDGSQTRDFVYVDDVADALLLALENPDGGVFNIGSGTA 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 198 H-SVREFVEKSFMHIGKTIvwegknenevgrcketgkVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAFDELVRE 276
Cdd:COG0451  242 EiTVRELAEAVAEAVGSKA------------------PLIVYIPLGRRGDLREGKLLDISKARAALGWEPKVSLEEGLAD 303

                 ...
gi 568981792 277 MVQ 279
Cdd:COG0451  304 TLE 306
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
36-279 2.65e-15

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: 74.51  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  36 SFDLAEYTADVDGVGTLRLLDAIKTCGLInsvKFYQASTSELYGKVQEIPQ-KETTPFYPRSPYGAAKLYAYWIVVNFRE 114
Cdd:cd05246   90 SISDPEPFIRTNVLGTYTLLEAARKYGVK---RFVHISTDEVYGDLLDDGEfTETSPLAPTSPYSASKAAADLLVRAYHR 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 115 AYNLFAVngILfnhesprRGAN------FVTRKISRSVAKIYLGQlECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEP- 187
Cdd:cd05246  167 TYGLPVV--IT-------RCSNnygpyqFPEKLIPLFILNALDGK-PLPIYGDGLNVRDWLYVEDHARAIELVLEKGRVg 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 188 EDFVIATGEVHSVREFVeksfmhigKTIvwegknenevgrCKETGKVHVTV---------DLKYYRptevdflqgDCSKA 258
Cdd:cd05246  237 EIYNIGGGNELTNLELV--------KLI------------LELLGKDESLItyvkdrpghDRRYAI---------DSSKI 287
                        250       260
                 ....*....|....*....|.
gi 568981792 259 QQKLNWKPRVAFDELVREMVQ 279
Cdd:cd05246  288 RRELGWRPKVSFEEGLRKTVR 308
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
39-267 1.20e-13

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


Pssm-ID: 224012 [Multi-domain]  Cd Length: 329  Bit Score: 69.90  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  39 LAEYTADVdgVGTLRLLDAIKTCGLINSVkFyqASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNL 118
Cdd:COG1087   88 LKYYDNNV--VGTLNLIEAMLQTGVKKFI-F--SSTAAVYGEPTTSPISETSPLAPINPYGRSKLMSEEILRDAAKANPF 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 119 FAVngIL--FN----HESPRRG--ANFVTRKISRsVAKIYLGQLECFSL--GNLDAK-----RDWGHAKDYVEAMWLMLQ 183
Cdd:COG1087  163 KVV--ILryFNvagaCPDGTLGqrYPGATLLIPV-AAEAALGKRDKLFIfgDDYDTKdgtciRDYIHVDDLADAHVLALK 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 184 ----NDEPEDFVIATGEVHSVREFVEKSfmhigktivwegknenevgrCKETGKvHVTVDLKYYRPTEVDFLQGDCSKAQ 259
Cdd:COG1087  240 ylkeGGSNNIFNLGSGNGFSVLEVIEAA--------------------KKVTGR-DIPVEIAPRRAGDPAILVADSSKAR 298

                 ....*...
gi 568981792 260 QKLNWKPR 267
Cdd:COG1087  299 QILGWQPT 306
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
49-275 1.64e-13

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


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 69.49  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  49 VGTLRLLDAIKTCGLINSVkFyqASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVngIL--F 126
Cdd:cd05247   98 VGTLNLLEAMRAHGVKNFV-F--SSSAAVYGEPETVPITEEAPLNPTNPYGRTKLMVEQILRDLAKAPGLNYV--ILryF 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 127 N----HESPRRGAN-FVTRKISRSVAKIYLGQLECFSL-GNlDAK-------RDWGHAKDYVEAMWLMLQ----NDEPED 189
Cdd:cd05247  173 NpagaHPSGLIGEDpQIPNNLIPYVLQVALGRREKLAIfGD-DYPtpdgtcvRDYIHVVDLADAHVLALEklenGGGSEI 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 190 FVIATGEVHSVREFVEKSFMHIGKTIvwegkNENEVGRcketgkvhvtvdlkyyRPTEVDFLQGDCSKAQQKLNWKPRVA 269
Cdd:cd05247  252 YNLGTGRGYSVLEVVEAFEKVSGKPI-----PYEIAPR----------------RAGDPASLVADPSKAREELGWKPKRD 310

                 ....*.
gi 568981792 270 FDELVR 275
Cdd:cd05247  311 LEDMCE 316
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
42-278 1.46e-12

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: 66.51  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  42 YTADVDGVGTLRLLDAIKTCGlinsVKFYQASTSELYGKVQEIPQKET-----TPFYPRSPYGAAKLYAYWIVVNFREAY 116
Cdd:cd05230   86 KTLKTNVLGTLNMLGLAKRVG----ARVLLASTSEVYGDPEVHPQPESywgnvNPIGPRSCYDEGKRVAETLCMAYHRQH 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 117 NLFAVNGILFNHESPRRGANF---VTRKISRSVA----KIYlgqlecfslGNLDAKRDWGHAKDYVEAMWLMLQNDEPED 189
Cdd:cd05230  162 GVDVRIARIFNTYGPRMHPNDgrvVSNFIVQALRgepiTVY---------GDGTQTRSFQYVSDLVEGLIRLMNSDYFGG 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 190 FV-IATGEVHSVREFVEKsfmhigktIVwegknenevgrcKETGKvhvTVDLKYYRPTEVDFLQ--GDCSKAQQKLNWKP 266
Cdd:cd05230  233 PVnLGNPEEFTILELAEL--------VK------------KLTGS---KSEIVFLPLPEDDPKRrrPDISKAKELLGWEP 289
                        250
                 ....*....|..
gi 568981792 267 RVAFDELVREMV 278
Cdd:cd05230  290 KVPLEEGLRRTI 301
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
50-278 1.81e-12

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


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 66.55  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  50 GTLRLLDAikTCGLINSvKFYQASTSELYGKVQEIPQKETTPFY----PRSPYGAAKLYAYwivvnfREAYNLFAVNG-- 123
Cdd:cd05257   98 GTLNVLEA--ACVLYRK-RVVHTSTSEVYGTAQDVPIDEDHPLLyinkPRSPYSASKQGAD------RLAYSYGRSFGlp 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 124 --IL--FNHESPRRGANFVTRKISRSVAkiyLGQLEcFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEP--EDFVIATGEV 197
Cdd:cd05257  169 vtIIrpFNTYGPRQSARAVIPTIISQRA---IGQRL-INLGDGSPTRDFNFVKDTARGFIDILDAIEAvgEIINNGSGEE 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 198 HSVREFVEKsfmhigkTIVWEGKNENEVgrcketgkvhVTVDLKYYRP--TEVDFLQGDCSKAQQKLNWKPRVAFDELVR 275
Cdd:cd05257  245 ISIGNPAVE-------LIVEELGEMVLI----------VYDDHREYRPgySEVERRIPDIRKAKRLLGWEPKYSLRDGLR 307

                 ...
gi 568981792 276 EMV 278
Cdd:cd05257  308 ETI 310
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
49-279 6.21e-12

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


Pssm-ID: 224013 [Multi-domain]  Cd Length: 340  Bit Score: 64.94  E-value: 6.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  49 VGTLRLLDAIKTCGLInsVKFYQASTSELYGKVQEIPQK--ETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVNGILF 126
Cdd:COG1088  103 VGTYTLLEAARKYWGK--FRFHHISTDEVYGDLGLDDDAftETTPYNPSSPYSASKAASDLLVRAYVRTYGLPATITRCS 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 127 NHESPRRGA-NFVTRKISRSVA----KIYlgqlecfslGNLDAKRDWGHAKDYVEAMWLMLQNDEPedfviatGEVHSVR 201
Cdd:COG1088  181 NNYGPYQFPeKLIPLMIINALLgkplPVY---------GDGLQIRDWLYVEDHCRAIDLVLTKGKI-------GETYNIG 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 202 EFVEKSFMHIGKTIvwegknenevgrCKETGKvhvtvDLKYYRPTeVDFLQG----------DCSKAQQKLNWKPRVAFD 271
Cdd:COG1088  245 GGNERTNLEVVKTI------------CELLGK-----DKPDYRDL-ITFVEDrpghdrryaiDASKIKRELGWRPQETFE 306

                 ....*...
gi 568981792 272 ELVREMVQ 279
Cdd:COG1088  307 TGLRKTVD 314
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
33-280 3.18e-11

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: 62.72  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  33 GQISFDLAEytadvDGVGTLRLLDAiktCGLINSVKFYQASTS-ELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVN 111
Cdd:cd05264   80 KNPILDIQT-----NVAPTVQLLEA---CAAAGIGKIIFASSGgTVYGVPEQLPISESDPTLPISSYGISKLAIEKYLRL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 112 FREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQ-LECFslGNLDAKRDWGHAKDYVEAMWLMLQNDEPED- 189
Cdd:cd05264  152 YQYLYGLDYTVLRISNPYGPGQRPDGKQGVIPIALNKILRGEpIEIW--GDGESIRDYIYIDDLVEALMALLRSKGLEEv 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 190 FVIATGEVHSVREFVEKSFmhigktivwegknenevgrcKETGKvhvTVDLKYY--RPTEVDFLQGDCSKAQQKLNWKPR 267
Cdd:cd05264  230 FNIGSGIGYSLAELIAEIE--------------------KVTGR---SVQVIYTpaRTTDVPKIVLDISRARAELGWSPK 286
                        250
                 ....*....|...
gi 568981792 268 VAFDELVREMVQA 280
Cdd:cd05264  287 ISLEDGLEKTWQW 299
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
43-278 3.91e-11

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 63.11  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  43 TADVDGVGTLRLLDAIKTCGlinsVKFYQASTSELYGKVQEIPQKET-----TPFYPRSPYGAAKLYAYWIVVNFREAYN 117
Cdd:PLN02166 207 TIKTNVMGTLNMLGLAKRVG----ARFLLTSTSEVYGDPLEHPQKETywgnvNPIGERSCYDEGKRTAETLAMDYHRGAG 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 118 LFAVNGILFNHESPRRG-------ANFVTRKISRSVAKIYlgqlecfslGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDF 190
Cdd:PLN02166 283 VEVRIARIFNTYGPRMClddgrvvSNFVAQTIRKQPMTVY---------GDGKQTRSFQYVSDLVDGLVALMEGEHVGPF 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 191 VIATGEVHSVREFVEksfmhigktIVwegknenevgrcKETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKLNWKPRVAF 270
Cdd:PLN02166 354 NLGNPGEFTMLELAE---------VV------------KETIDSSATIEFKPNTADDPHKRKPDISKAKELLNWEPKISL 412

                 ....*...
gi 568981792 271 DELVREMV 278
Cdd:PLN02166 413 REGLPLMV 420
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
48-278 1.30e-10

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: 60.78  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  48 GVGTLRLLDAIKTCGlINSVKFyqASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAywivvnfrEAY-----NLFAVN 122
Cdd:cd05234   95 VLATYNVLEAMRANG-VKRIVF--ASSSTVYGEAKVIPTPEDYPPLPISVYGASKLAA--------EALisayaHLFGFQ 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 123 GILFnhesprRGANFVTRKISRSVAKIYLGQL-----ECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEP--EDFVIATG 195
Cdd:cd05234  164 AWIF------RFANIVGPRSTHGVIYDFINKLkrnpnELEVLGDGRQRKSYLYVSDCVDAMLLAWEKSTEgvNIFNLGND 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 196 EVHSVREFVEksfmhigktIVwegknenevgrCKETGkvhVTVDLKY---YR--PTEVDFLQGDCSKAqQKLNWKPRVAF 270
Cdd:cd05234  238 DTISVNEIAE---------IV-----------IEELG---LKPRFKYsggDRgwKGDVPYMRLDIEKL-KALGWKPRYNS 293

                 ....*...
gi 568981792 271 DELVREMV 278
Cdd:cd05234  294 EEAVRKTV 301
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
49-279 1.69e-10

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 60.82  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  49 VGTLRLLDAIKT------CGLINSVKFYQASTSELYGKVQEIPQ--KETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFA 120
Cdd:PRK10217 103 VGTYTLLEAARAywnaltEDKKSAFRFHHISTDEVYGDLHSTDDffTETTPYAPSSPYSASKASSDHLVRAWLRTYGLPT 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 121 VNGILFNHESPRrgaNFVTRKISRSVAKIYLGQ-LECFslGNLDAKRDWGHAKDYVEAMWLMLQNDEPedfviatGEVHS 199
Cdd:PRK10217 183 LITNCSNNYGPY---HFPEKLIPLMILNALAGKpLPVY--GNGQQIRDWLYVEDHARALYCVATTGKV-------GETYN 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 200 VREFVEKSFMHIGKTIVwegKNENEVGRCKETGKVHVTvDLKYY---RPTEVDFLQGDCSKAQQKLNWKPRVAFDELVRE 276
Cdd:PRK10217 251 IGGHNERKNLDVVETIC---ELLEELAPNKPQGVAHYR-DLITFvadRPGHDLRYAIDASKIARELGWLPQETFESGMRK 326

                 ...
gi 568981792 277 MVQ 279
Cdd:PRK10217 327 TVQ 329
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
42-279 3.93e-06

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


Pssm-ID: 187562 [Multi-domain]  Cd Length: 336  Bit Score: 47.31  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  42 YTADVDGVGTLRLLDAIKTCGLINSVkfYQASTSELYGKVQEI-PQKETTPFYPRSPYGAAKLYAYWIVVNFREAY---N 117
Cdd:cd05252   97 ETFETNVMGTVNLLEAIRETGSVKAV--VNVTSDKCYENKEWGwGYRENDPLGGHDPYSSSKGCAELIISSYRNSFfnpE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 118 LFAVNGILFnheSPRRGANFV-------TRKISRSVAKIYLGqlECFSLGNLDAKRDWGHAKDYVeAMWLML---QNDEP 187
Cdd:cd05252  175 NYGKHGIAI---ASARAGNVIgggdwaeDRIVPDCIRAFEAG--ERVIIRNPNAIRPWQHVLEPL-SGYLLLaekLYERG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 188 EDFVIA------TGEVHSVREFVEKSFMHIGKTIVWEGKNENevgrcketgkvhvtvdlkyyRPTEVDFLQGDCSKAQQK 261
Cdd:cd05252  249 EEYAEAwnfgpdDEDAVTVLELVEAMARYWGEDARWDLDGNS--------------------HPHEANLLKLDCSKAKTM 308
                        250
                 ....*....|....*...
gi 568981792 262 LNWKPRVAFDELVREMVQ 279
Cdd:cd05252  309 LGWRPRWNLEETLEFTVA 326
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
50-276 1.27e-05

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 45.96  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  50 GTLRLLDAIKTCGLINsvkFYQASTSELYGKVQEIPQKETTPF-YPRSPYGAAKLYAYWIVVNFREAYNLFAVNGI-LFN 127
Cdd:PRK10675 103 GTLRLISAMRAANVKN---LIFSSSATVYGDQPKIPYVESFPTgTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLrYFN 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 128 ----HESPRRGAN--FVTRKISRSVAKIYLGQLECFSL-GNLDAKRDWGHAKDYVEAMWLmlqndepedfviATGEVHSV 200
Cdd:PRK10675 180 pvgaHPSGDMGEDpqGIPNNLMPYIAQVAVGRRDSLAIfGNDYPTEDGTGVRDYIHVMDL------------ADGHVAAM 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 201 REFVEKSFMHIGKTIVWEGKNENEV--GRCKETGKvhvtvDLKYY----RPTEVDFLQGDCSKAQQKLNWKPRVAFDELV 274
Cdd:PRK10675 248 EKLANKPGVHIYNLGAGVGSSVLDVvnAFSKACGK-----PVNYHfaprREGDLPAYWADASKADRELNWRVTRTLDEMA 322

                 ..
gi 568981792 275 RE 276
Cdd:PRK10675 323 QD 324
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
49-279 6.63e-05

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 43.63  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  49 VGTLRLLDAIKT------CGLINSVKFYQASTSELYGKV---------QEIPQ-KETTPFYPRSPYGAAKLYAYWIVVNF 112
Cdd:PRK10084 102 VGTYVLLEAARNywsaldEDKKNAFRFHHISTDEVYGDLphpdevensEELPLfTETTAYAPSSPYSASKASSDHLVRAW 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 113 REAYNLFAVNGILFNHESPRrgaNFVTRKISRsvakIYLGQLECFSL---GNLDAKRDWGHAKDYVEAMWLMLQNDEPed 189
Cdd:PRK10084 182 LRTYGLPTIVTNCSNNYGPY---HFPEKLIPL----VILNALEGKPLpiyGKGDQIRDWLYVEDHARALYKVVTEGKA-- 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 190 fviatGEVHSVREFVEKSFMHIGKTIvwegknenevgrCK-------ETGKVHVTVDLKYYRPTEVDFLQGDCSKAQQKL 262
Cdd:PRK10084 253 -----GETYNIGGHNEKKNLDVVLTI------------CDlldeivpKATSYREQITYVADRPGHDRRYAIDASKISREL 315
                        250
                 ....*....|....*..
gi 568981792 263 NWKPRVAFDELVREMVQ 279
Cdd:PRK10084 316 GWKPQETFESGIRKTVE 332
PLN02206 PLN02206
UDP-glucuronate decarboxylase
49-279 7.35e-05

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 43.82  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792  49 VGTLRLLDAIKTCGlinsVKFYQASTSELYGKVQEIPQKET-----TPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVNG 123
Cdd:PLN02206 212 VGTLNMLGLAKRVG----ARFLLTSTSEVYGDPLQHPQVETywgnvNPIGVRSCYDEGKRTAETLTMDYHRGANVEVRIA 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 124 ILFNHESPRRG-------ANFVTRKISRSVAKIYlgqlecfslGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIAT-G 195
Cdd:PLN02206 288 RIFNTYGPRMCiddgrvvSNFVAQALRKEPLTVY---------GDGKQTRSFQFVSDLVEGLMRLMEGEHVGPFNLGNpG 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981792 196 EVhsvrefvekSFMHIGKTIvwegknenevgrcKETGKVHVTVDlkyYRP-TEVD--FLQGDCSKAQQKLNWKPRVAFDE 272
Cdd:PLN02206 359 EF---------TMLELAKVV-------------QETIDPNAKIE---FRPnTEDDphKRKPDITKAKELLGWEPKVSLRQ 413

                 ....*..
gi 568981792 273 LVREMVQ 279
Cdd:PLN02206 414 GLPLMVK 420
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
50-118 1.13e-03

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 40.11  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568981792  50 GTLRLLDAIKTCGLINsvKFYQASTSELYGKVQE---IPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNL 118
Cdd:PLN02260 110 GTHVLLEACKVTGQIR--RFIHVSTDEVYGETDEdadVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGL 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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