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Conserved domains on  [gi|1046903405|ref|XP_017451760|]
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UDP-glucuronic acid decarboxylase 1 isoform X10 [Rattus norvegicus]

Protein Classification

UDP-glucuronic acid decarboxylase 1( domain architecture ID 10570463)

UDP-glucuronic acid decarboxylase 1 catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
76-379 0e+00

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: 626.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNY 155
Cdd:cd05230     1 KRILITGGAGFLGSHLCDRLLEDGHEVICVDNFFTGRKRNIEHLIGHPNFEFIRHDVTEPLYLEVDQIYHLACPASPVHY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQ 235
Cdd:cd05230    81 QYNPIKTLKTNVLGTLNMLGLAKRVGARVLLASTSEVYGDPEVHPQPESYWGNVNPIGPRSCYDEGKRVAETLCMAYHRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 236 EGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSS-PVNLGNPE 314
Cdd:cd05230   161 HGVDVRIARIFNTYGPRMHPNDGRVVSNFIVQALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLMNSDYFGgPVNLGNPE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903405 315 EHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFR 379
Cdd:cd05230   241 EFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKELLGWEPKVPLEEGLRRTIEYFR 305
UXS1_N pfam11803
UDP-glucuronate decarboxylase N-terminal; The N-terminus of the UDP-glucuronate decarboxylases ...
15-65 3.46e-14

UDP-glucuronate decarboxylase N-terminal; The N-terminus of the UDP-glucuronate decarboxylases may be involved in localization to the perinuclear Golgi membrane.


:

Pssm-ID: 463356  Cd Length: 75  Bit Score: 67.19  E-value: 3.46e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1046903405  15 VWGNFVNMsfllnRSIQENGELKIESKIEEIIEPLREKIRDLEKSFTQKYP 65
Cdd:pfam11803  30 VWGTYVNM-----RSIQENGEQKVEQKIEEVVAPLREKIRDLEKSFTQKYP 75
 
Name Accession Description Interval E-value
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
76-379 0e+00

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: 626.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNY 155
Cdd:cd05230     1 KRILITGGAGFLGSHLCDRLLEDGHEVICVDNFFTGRKRNIEHLIGHPNFEFIRHDVTEPLYLEVDQIYHLACPASPVHY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQ 235
Cdd:cd05230    81 QYNPIKTLKTNVLGTLNMLGLAKRVGARVLLASTSEVYGDPEVHPQPESYWGNVNPIGPRSCYDEGKRVAETLCMAYHRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 236 EGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSS-PVNLGNPE 314
Cdd:cd05230   161 HGVDVRIARIFNTYGPRMHPNDGRVVSNFIVQALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLMNSDYFGgPVNLGNPE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903405 315 EHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFR 379
Cdd:cd05230   241 EFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKELLGWEPKVPLEEGLRRTIEYFR 305
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
73-382 5.24e-164

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 467.57  E-value: 5.24e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  73 KDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASP 152
Cdd:PLN02166  118 RKRLRIVVTGGAGFVGSHLVDKLIGRGDEVIVIDNFFTGRKENLVHLFGNPRFELIRHDVVEPILLEVDQIYHLACPASP 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 153 PNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAY 232
Cdd:PLN02166  198 VHYKYNPVKTIKTNVMGTLNMLGLAKRVGARFLLTSTSEVYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLAMDY 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 233 MKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGN 312
Cdd:PLN02166  278 HRGAGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQTIRKQPMTVYGDGKQTRSFQYVSDLVDGLVALMEGEHVGPFNLGN 357
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 313 PEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKEL 382
Cdd:PLN02166  358 PGEFTMLELAEVVKETIDSSATIEFKPNTADDPHKRKPDISKAKELLNWEPKISLREGLPLMVSDFRNRI 427
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
77-380 1.55e-94

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 285.33  E-value: 1.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEhwigHENFELINHDVVEPLYIE-----VDQIYHLASPAS 151
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAA----LPGVEFVRGDLRDPEALAaalagVDAVVHLAAPAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 PPnyMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTSEVYGDPEvHPQSEDYwghvnPIGPRACYDEGKRVAETMCY 230
Cdd:COG0451    77 VG--EEDPDETLEVNVEGTLNLLEAARAAGvKRFVYASSSSVYGDGE-GPIDEDT-----PLRPVSPYGASKLAAELLAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 231 AYMKQEGVEVRVARIFNTFGPRMHmndgRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSS--PV 308
Cdd:COG0451   149 AYARRYGLPVTILRPGNVYGPGDR----GVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPggVY 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903405 309 NLGNPEEHTILEFAQLIKNLVGSGSEIQFlSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRK 380
Cdd:COG0451   225 NVGGGEPVTLRELAEAIAEALGRPPEIVY-PARPGDVRPRRADNSKARRELGWRPRTSLEEGLRETVAWYRA 295
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
79-371 1.00e-65

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 212.41  E-value: 1.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  79 LITGGAGFVGSHLTDKLMMDGHEVTVVDN----FFTGRKRNVEHWIGHENFELINHDVVEPLYIE-------VDQIYHLA 147
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVRrsssFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVrllaevqPDEIYNLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 148 SPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG----ARLLLASTSEVYGDPEVHPQSEDywghvNPIGPRACYDEGKR 223
Cdd:pfam16363  81 AQSHVDVSFEQPEYTADTNVLGTLRLLEAIRSLGlekkVRFYQASTSEVYGKVQEVPQTET-----TPFYPRSPYAAAKL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 224 VAETMCYAYMKQEGVEVRVARIFNTFGPRMHMN-DGRVVSNFILQALQG-EPLTVYGSGSQTRAFQYVSDLVNGLVALMN 301
Cdd:pfam16363 156 YADWIVVNYRESYGLFACNGILFNHESPRRGERfVTRKITRGVARIKLGkQEKLYLGNLDAKRDWGHARDYVEAMWLMLQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 302 SNVSSPVNLGNPEEHTILEF-----AQLIKNLVGSGSEIQFLSEAQD------DPQKRKP--------DIKKAKLMLGWE 362
Cdd:pfam16363 236 QDKPDDYVIATGETHTVREFvekafLELGLTITWEGKGEIGYFKASGkvhvliDPRYFRPgevdrllgDPSKAKEELGWK 315

                  ....*....
gi 1046903405 363 PVVPLEEGL 371
Cdd:pfam16363 316 PKVSFEELV 324
heptose_epim TIGR02197
ADP-L-glycero-D-manno-heptose-6-epimerase; This family consists of examples of ...
78-372 7.52e-22

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


Pssm-ID: 274028 [Multi-domain]  Cd Length: 314  Bit Score: 95.04  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGH-EVTVVDNFFTG------RKRNVEHWIGHENF-ELINHDVveplYIEVDQIYHLASP 149
Cdd:TIGR02197   1 IIVTGGAGFIGSNLVKALNERGItDILVVDNLRDGhkflnlADLVIADYIDKEDFlDRLEKGA----FGKIEAIFHQGAC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 150 ASppNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVhPQSEDywghVNPIGPRACYDEGKRVAETMC 229
Cdd:TIGR02197  77 SD--TTETDGEYMMENNYQYSKRLLDWCAEKGIPFIYASSAATYGDGEA-GFREG----RELERPLNVYGYSKFLFDQYV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 230 YAYMKQEGVEVRVA--RIFNTFGPR-MHMND-GRVVSNFILQALQGEPLTVYGS------GSQTRAFQYVSDLVNGLVAL 299
Cdd:TIGR02197 150 RRRVLPEALSAQVVglRYFNVYGPReYHKGKmASVAFHLFNQIKAGGNVKLFKSsegfkdGEQLRDFVYVKDVVDVNLWL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 300 MNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLseaqDDPQKRKP--------DIKKAKLMLGWEPVVPLEEGL 371
Cdd:TIGR02197 230 LENGVSGIFNLGTGRARSFNDLADAVFKALGKDEKIEYI----PMPEALRGryqyftqaDITKLRAAGYYGPFTTLEEGV 305

                  .
gi 1046903405 372 N 372
Cdd:TIGR02197 306 K 306
UXS1_N pfam11803
UDP-glucuronate decarboxylase N-terminal; The N-terminus of the UDP-glucuronate decarboxylases ...
15-65 3.46e-14

UDP-glucuronate decarboxylase N-terminal; The N-terminus of the UDP-glucuronate decarboxylases may be involved in localization to the perinuclear Golgi membrane.


Pssm-ID: 463356  Cd Length: 75  Bit Score: 67.19  E-value: 3.46e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1046903405  15 VWGNFVNMsfllnRSIQENGELKIESKIEEIIEPLREKIRDLEKSFTQKYP 65
Cdd:pfam11803  30 VWGTYVNM-----RSIQENGEQKVEQKIEEVVAPLREKIRDLEKSFTQKYP 75
 
Name Accession Description Interval E-value
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
76-379 0e+00

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: 626.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNY 155
Cdd:cd05230     1 KRILITGGAGFLGSHLCDRLLEDGHEVICVDNFFTGRKRNIEHLIGHPNFEFIRHDVTEPLYLEVDQIYHLACPASPVHY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQ 235
Cdd:cd05230    81 QYNPIKTLKTNVLGTLNMLGLAKRVGARVLLASTSEVYGDPEVHPQPESYWGNVNPIGPRSCYDEGKRVAETLCMAYHRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 236 EGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSS-PVNLGNPE 314
Cdd:cd05230   161 HGVDVRIARIFNTYGPRMHPNDGRVVSNFIVQALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLMNSDYFGgPVNLGNPE 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903405 315 EHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFR 379
Cdd:cd05230   241 EFTILELAELVKKLTGSKSEIVFLPLPEDDPKRRRPDISKAKELLGWEPKVPLEEGLRRTIEYFR 305
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
73-382 5.24e-164

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 467.57  E-value: 5.24e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  73 KDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASP 152
Cdd:PLN02166  118 RKRLRIVVTGGAGFVGSHLVDKLIGRGDEVIVIDNFFTGRKENLVHLFGNPRFELIRHDVVEPILLEVDQIYHLACPASP 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 153 PNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAY 232
Cdd:PLN02166  198 VHYKYNPVKTIKTNVMGTLNMLGLAKRVGARFLLTSTSEVYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLAMDY 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 233 MKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGN 312
Cdd:PLN02166  278 HRGAGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQTIRKQPMTVYGDGKQTRSFQYVSDLVDGLVALMEGEHVGPFNLGN 357
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 313 PEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKEL 382
Cdd:PLN02166  358 PGEFTMLELAEVVKETIDSSATIEFKPNTADDPHKRKPDISKAKELLNWEPKISLREGLPLMVSDFRNRI 427
PLN02206 PLN02206
UDP-glucuronate decarboxylase
77-382 1.04e-162

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 464.45  E-value: 1.04e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYM 156
Cdd:PLN02206  121 RVVVTGGAGFVGSHLVDRLMARGDSVIVVDNFFTGRKENVMHHFSNPNFELIRHDVVEPILLEVDQIYHLACPASPVHYK 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 157 YNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQE 236
Cdd:PLN02206  201 FNPVKTIKTNVVGTLNMLGLAKRVGARFLLTSTSEVYGDPLQHPQVETYWGNVNPIGVRSCYDEGKRTAETLTMDYHRGA 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 237 GVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEH 316
Cdd:PLN02206  281 NVEVRIARIFNTYGPRMCIDDGRVVSNFVAQALRKEPLTVYGDGKQTRSFQFVSDLVEGLMRLMEGEHVGPFNLGNPGEF 360
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903405 317 TILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKEL 382
Cdd:PLN02206  361 TMLELAKVVQETIDPNAKIEFRPNTEDDPHKRKPDITKAKELLGWEPKVSLRQGLPLMVKDFRQRV 426
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
77-380 1.55e-94

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 285.33  E-value: 1.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEhwigHENFELINHDVVEPLYIE-----VDQIYHLASPAS 151
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAA----LPGVEFVRGDLRDPEALAaalagVDAVVHLAAPAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 PPnyMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTSEVYGDPEvHPQSEDYwghvnPIGPRACYDEGKRVAETMCY 230
Cdd:COG0451    77 VG--EEDPDETLEVNVEGTLNLLEAARAAGvKRFVYASSSSVYGDGE-GPIDEDT-----PLRPVSPYGASKLAAELLAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 231 AYMKQEGVEVRVARIFNTFGPRMHmndgRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSS--PV 308
Cdd:COG0451   149 AYARRYGLPVTILRPGNVYGPGDR----GVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPggVY 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903405 309 NLGNPEEHTILEFAQLIKNLVGSGSEIQFlSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRK 380
Cdd:COG0451   225 NVGGGEPVTLRELAEAIAEALGRPPEIVY-PARPGDVRPRRADNSKARRELGWRPRTSLEEGLRETVAWYRA 295
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
77-378 9.85e-87

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: 265.62  E-value: 9.85e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHwiGHENFELINHDV-----VEPLYIEVDQIYHLASPAS 151
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLLERGHEVIVLDNLSTGKKENLPE--VKPNVKFIEGDIrddelVEFAFEGVDYVFHQAAQAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 PPNYMYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVHPQSEDYWGhvNPIGPracYDEGKRVAETMCY 230
Cdd:cd05256    79 VPRSIEDPIKDHEVNVLGTLNLLEAARKAGVkRFVYASSSSVYGDPPYLPKDEDHPP--NPLSP---YAVSKYAGELYCQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 231 AYMKQEGVEVRVARIFNTFGPRMHMNDGR--VVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPV 308
Cdd:cd05256   154 VFARLYGLPTVSLRYFNVYGPRQDPNGGYaaVIPIFIERALKGEPPTIYGDGEQTRDFTYVEDVVEANLLAATAGAGGEV 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903405 309 -NLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYF 378
Cdd:cd05256   234 yNIGTGKRTSVNELAELIREILGKELEPVYAPPRPGDVRHSLADISKAKKLLGWEPKVSFEEGLRLTVEWF 304
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
77-380 3.77e-71

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: 226.03  E-value: 3.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIE-----VDQIYHLASPAS 151
Cdd:cd05257     1 NVLVTGADGFIGSHLTERLLREGHEVRALDIYNSFNSWGLLDNAVHDRFHFISGDVRDASEVEylvkkCDVVFHLAALIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 PPNYMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTSEVYGD------PEVHPQSEDywghvnpIGPRACYDEGKRV 224
Cdd:cd05257    81 IPYSYTAPLSYVETNVFGTLNVLEAACVLYrKRVVHTSTSEVYGTaqdvpiDEDHPLLYI-------NKPRSPYSASKQG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 225 AETMCYAYMKQEGVEVRVARIFNTFGPRmhMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSN- 303
Cdd:cd05257   154 ADRLAYSYGRSFGLPVTIIRPFNTYGPR--QSARAVIPTIISQRAIGQRLINLGDGSPTRDFNFVKDTARGFIDILDAIe 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 304 -VSSPVNLGNPEEHTILEFAQLIknLVGSGSEI--------QFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKA 374
Cdd:cd05257   232 aVGEIINNGSGEEISIGNPAVEL--IVEELGEMvlivyddhREYRPGYSEVERRIPDIRKAKRLLGWEPKYSLRDGLRET 309

                  ....*.
gi 1046903405 375 IHYFRK 380
Cdd:cd05257   310 IEWFKD 315
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
79-371 1.00e-65

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 212.41  E-value: 1.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  79 LITGGAGFVGSHLTDKLMMDGHEVTVVDN----FFTGRKRNVEHWIGHENFELINHDVVEPLYIE-------VDQIYHLA 147
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVRrsssFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVrllaevqPDEIYNLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 148 SPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG----ARLLLASTSEVYGDPEVHPQSEDywghvNPIGPRACYDEGKR 223
Cdd:pfam16363  81 AQSHVDVSFEQPEYTADTNVLGTLRLLEAIRSLGlekkVRFYQASTSEVYGKVQEVPQTET-----TPFYPRSPYAAAKL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 224 VAETMCYAYMKQEGVEVRVARIFNTFGPRMHMN-DGRVVSNFILQALQG-EPLTVYGSGSQTRAFQYVSDLVNGLVALMN 301
Cdd:pfam16363 156 YADWIVVNYRESYGLFACNGILFNHESPRRGERfVTRKITRGVARIKLGkQEKLYLGNLDAKRDWGHARDYVEAMWLMLQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 302 SNVSSPVNLGNPEEHTILEF-----AQLIKNLVGSGSEIQFLSEAQD------DPQKRKP--------DIKKAKLMLGWE 362
Cdd:pfam16363 236 QDKPDDYVIATGETHTVREFvekafLELGLTITWEGKGEIGYFKASGkvhvliDPRYFRPgevdrllgDPSKAKEELGWK 315

                  ....*....
gi 1046903405 363 PVVPLEEGL 371
Cdd:pfam16363 316 PKVSFEELV 324
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
78-311 3.66e-60

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


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 193.67  E-value: 3.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVVDNFftgrkrnvehwighenfelinhdvveplyievDQIYHLASPASPPNYMY 157
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLERGHEVVVIDRL--------------------------------DVVVHLAALVGVPASWD 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 158 NPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTSEVYGDPEVHPQSEDYwghvnPIGPRACYDEGKRVAETMCYAYMKQE 236
Cdd:cd08946    49 NPDEDFETNVVGTLNLLEAARKAGvKRFVYASSASVYGSPEGLPEEEET-----PPRPLSPYGVSKLAAEHLLRSYGESY 123
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903405 237 GVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSN--VSSPVNLG 311
Cdd:cd08946   124 GLPVVILRLANVYGPGQRPRLDGVVNDFIRRALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALENPleGGGVYNIG 200
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
78-311 4.39e-59

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: 192.51  E-value: 4.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPL--YIEVDQIYHLASPASPPNY 155
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVEGDLTDRDALEKLlaDVRPDAVIHLAAVGGVGAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVHPQSEDYwgHVNPIGPRACYDEGKRVAETMCYAYMK 234
Cdd:pfam01370  81 IEDPEDFIEANVLGTLNLLEAARKAGVkRFLFASSSEVYGDGAEIPQEETT--LTGPLAPNSPYAAAKLAGEWLVLAYAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 235 QEGVEVRVARIFNTFGPRMHMN-DGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSP--VNLG 311
Cdd:pfam01370 159 AYGLRAVILRLFNVYGPGDNEGfVSRVIPALIRRILEGKPILLWGDGTQRRDFLYVDDVARAILLALEHGAVKGeiYNIG 238
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
77-377 7.34e-58

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: 191.36  E-value: 7.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYI----EVDQIYHLASPASP 152
Cdd:cd05234     1 RILVTGGAGFIGSHLVDRLLEEGNEVVVVDNLSSGRRENIEPEFENKAFRFVKRDLLDTADKvakkDGDTVFHLAANPDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 153 PNYMYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVHPQSEDYwghvnPIGPRACYDEGKRVAETMCYA 231
Cdd:cd05234    81 RLGATDPDIDLEENVLATYNVLEAMRANGVkRIVFASSSTVYGEAKVIPTPEDY-----PPLPISVYGASKLAAEALISA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 232 YMKQEGVEVRVARIFNTFGPRMHmndGRVVSNFILQALQG-EPLTVYGSGSQTRAFQYVSDLVNGLVaLMNSNVSSPV-- 308
Cdd:cd05234   156 YAHLFGFQAWIFRFANIVGPRST---HGVIYDFINKLKRNpNELEVLGDGRQRKSYLYVSDCVDAML-LAWEKSTEGVni 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903405 309 -NLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQ----DDPQKRKpDIKKAKlMLGWEPVVPLEEGLNKAIHY 377
Cdd:cd05234   232 fNLGNDDTISVNEIAEIVIEELGLKPRFKYSGGDRgwkgDVPYMRL-DIEKLK-ALGWKPRYNSEEAVRKTVRE 303
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
76-379 1.84e-56

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


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 188.37  E-value: 1.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLM--MDGHEVTVVDNFF-TGRKRNVEHWIGHENFELINHDV-----VEPL--YIEVDQIYH 145
Cdd:COG1088     2 MRILVTGGAGFIGSNFVRYLLakYPGAEVVVLDKLTyAGNLENLADLEDDPRYRFVKGDIrdrelVDELfaEHGPDAVVH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 146 LAspASP--PNYMYNPIKTLKTNTIGTLNMLGLAKRVG---ARLLLASTSEVYGD-PEVHPQSEDYwghvnPIGPRACYD 219
Cdd:COG1088    82 FA--AEShvDRSIDDPAAFVETNVVGTFNLLEAARKYWvegFRFHHVSTDEVYGSlGEDGPFTETT-----PLDPSSPYS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 220 EGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNdgRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVAL 299
Cdd:COG1088   155 ASKAASDHLVRAYHRTYGLPVVITRCSNNYGPYQFPE--KLIPLFITNALEGKPLPVYGDGKQVRDWLYVEDHCRAIDLV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 300 MNSNVSSPV-NLGNPEEHTILEFAQLIKNLVG-SGSEIQFLseaQDDP--QKR-KPDIKKAKLMLGWEPVVPLEEGLNKA 374
Cdd:COG1088   233 LEKGRPGETyNIGGGNELSNLEVVELICDLLGkPESLITFV---KDRPghDRRyAIDASKIRRELGWKPKVTFEEGLRKT 309

                  ....*
gi 1046903405 375 IHYFR 379
Cdd:COG1088   310 VDWYL 314
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
76-383 1.78e-55

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: 185.76  E-value: 1.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNY 155
Cdd:cd05273     1 QRALVTGAGGFIGSHLAERLKAEGHYVRGADWKSPEHMTQPTDDDEFHLVDLREMENCLKATEGVDHVFHLAADMGGMGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MY-NPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYgdPEVHPQS--------EDYWghvnPIGPRACYDEGKRVA 225
Cdd:cd05273    81 IQsNHAVIMYNNTLINFNMLEAARINGVeRFLFASSACVY--PEFKQLEttvvrlreEDAW----PAEPQDAYGWEKLAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 226 ETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGR-----VVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALM 300
Cdd:cd05273   155 ERLCQHYNEDYGIETRIVRFHNIYGPRGTWDGGRekapaAMCRKVATAKDGDRFEIWGDGLQTRSFTYIDDCVEGLRRLM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 301 NSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRK 380
Cdd:cd05273   235 ESDFGEPVNLGSDEMVSMNELAEMVLSFSGKPLEIIHHTPGPQGVRGRNSDNTLLKEELGWEPNTPLEEGLRITYFWIKE 314

                  ...
gi 1046903405 381 ELE 383
Cdd:cd05273   315 QIE 317
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
77-373 9.81e-46

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: 159.41  E-value: 9.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFF------TGRKRNVEhwighENFELInHDVVEPLyIEVDQIYHLASPA 150
Cdd:cd05264     1 RVLIVGGNGFIGSHLVDALLEEGPQVRVFDRSIppyelpLGGVDYIK-----GDYENR-ADLESAL-VGIDTVIHLASTT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 151 SPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLAST-SEVYGDPEVHPQSEDywghvNPIGPRACYDEGKRVAETM 228
Cdd:cd05264    74 NPATSNKNPILDIQTNVAPTVQLLEACAAAGiGKIIFASSgGTVYGVPEQLPISES-----DPTLPISSYGISKLAIEKY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 229 CYAYMKQEGVEVRVARIFNTFGPRMHMNDGR-VVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSP 307
Cdd:cd05264   149 LRLYQYLYGLDYTVLRISNPYGPGQRPDGKQgVIPIALNKILRGEPIEIWGDGESIRDYIYIDDLVEALMALLRSKGLEE 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903405 308 V-NLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNK 373
Cdd:cd05264   229 VfNIGSGIGYSLAELIAEIEKVTGRSVQVIYTPARTTDVPKIVLDISRARAELGWSPKISLEDGLEK 295
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
76-379 2.45e-45

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: 159.42  E-value: 2.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHW----IGHENFE------LINHDVVEPLYIEV--DQI 143
Cdd:cd05253     1 MKILVTGAAGFIGFHVAKRLLERGDEVVGIDNLNDYYDVRLKEArlelLGKSGGFkfvkgdLEDREALRRLFKDHefDAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 144 YHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGAR-LLLASTSEVYGDPEVHPQSEDywGHVN-PIGPracYDEG 221
Cdd:cd05253    81 IHLAAQAGVRYSLENPHAYVDSNIVGFLNLLELCRHFGVKhLVYASSSSVYGLNTKMPFSED--DRVDhPISL---YAAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 222 KRVAETMCYAYMKQEGVEVRVARIFNTFGP--RMHMndgrVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVAL 299
Cdd:cd05253   156 KKANELMAHTYSHLYGIPTTGLRFFTVYGPwgRPDM----ALFLFTKAILEGKPIDVFNDGNMSRDFTYIDDIVEGVVRA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 300 MNSNVSSP-------------------VNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLG 360
Cdd:cd05253   232 LDTPAKPNpnwdaeapdpstssapyrvYNIGNNSPVKLMDFIEALEKALGKKAKKNYLPMQKGDVPETYADISKLQRLLG 311
                         330
                  ....*....|....*....
gi 1046903405 361 WEPVVPLEEGLNKAIHYFR 379
Cdd:cd05253   312 YKPKTSLEEGVKRFVEWYK 330
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
76-380 5.70e-45

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: 158.10  E-value: 5.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMM--DGHEVTVVDNF-FTGRKRNVEHWIGHENFELINHDVVEPLYI-------EVDQIYH 145
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLNkyPDYKIINLDKLtYAGNLENLEDVSSSPRYRFVKGDICDAELVdrlfeeeKIDAVIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 146 LASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEvhpqSEDYWGHVNPIGPRACYDEGKRV 224
Cdd:cd05246    81 FAAESHVDRSISDPEPFIRTNVLGTYTLLEAARKYGVkRFVHISTDEVYGDLL----DDGEFTETSPLAPTSPYSASKAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 225 AETMCYAYMKQEGVEVRVARIFNTFGPRMHmnDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNV 304
Cdd:cd05246   157 ADLLVRAYHRTYGLPVVITRCSNNYGPYQF--PEKLIPLFILNALDGKPLPIYGDGLNVRDWLYVEDHARAIELVLEKGR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 305 SSPV-NLGNPEEHTILEFAQLIKNLVG-SGSEIQFLSeaqDDP-QKRKPDIKKAKLM--LGWEPVVPLEEGLNKAIHYFR 379
Cdd:cd05246   235 VGEIyNIGGGNELTNLELVKLILELLGkDESLITYVK---DRPgHDRRYAIDSSKIRreLGWRPKVSFEEGLRKTVRWYL 311

                  .
gi 1046903405 380 K 380
Cdd:cd05246   312 E 312
PRK11908 PRK11908
bifunctional UDP-4-keto-pentose/UDP-xylose synthase;
76-385 3.29e-37

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


Pssm-ID: 183375 [Multi-domain]  Cd Length: 347  Bit Score: 138.31  E-value: 3.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDK-LMMDGHEVTVVDNfftgRKRNVEHWIGHENFEL------INHDVVEPLYIEVDQIYHLAS 148
Cdd:PRK11908    2 KKVLILGVNGFIGHHLSKRiLETTDWEVYGMDM----QTDRLGDLVNHPRMHFfegditINKEWIEYHVKKCDVILPLVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 149 PASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYG---DPEVHPQ-SEDYWGHVNPigPRACYDEGKRV 224
Cdd:PRK11908   78 IATPATYVKQPLRVFELDFEANLPIVRSAVKYGKHLVFPSTSEVYGmcpDEEFDPEaSPLVYGPINK--PRWIYACSKQL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 225 AETMCYAYMKQEGVEVRVARIFNTFGPRM------HMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVA 298
Cdd:PRK11908  156 MDRVIWAYGMEEGLNFTLFRPFNWIGPGLdsiytpKEGSSRVVTQFLGHIVRGEPISLVDGGSQKRAFTDIDDGIDALMK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 299 LM-NSN---VSSPVNLGNP-EEHTILEFAQLIKNLVGSGSEI---------------QFLSEAQDDPQKRKPDIKKAKLM 358
Cdd:PRK11908  236 IIeNKDgvaSGKIYNIGNPkNNHSVRELANKMLELAAEYPEYaesakkvklvettsgAYYGKGYQDVQNRVPKIDNTMQE 315
                         330       340
                  ....*....|....*....|....*..
gi 1046903405 359 LGWEPVVPLEEGLNKAIHYFRKELEYQ 385
Cdd:PRK11908  316 LGWAPKTTMDDALRRIFEAYRGHVAEA 342
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
76-377 3.90e-36

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: 135.11  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFF-TGRKRNvEHWI----GHENFELINHDV-----VEPLYIEVDQIYH 145
Cdd:cd05258     1 MRVLITGGAGFIGSNLARFFLKQGWEVIGFDNLMrRGSFGN-LAWLkanrEDGGVRFVHGDIrnrndLEDLFEDIDLIIH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 146 LASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG--ARLLLASTSEVYGDpevHPQSEDY------WgHVNPIGPRAC 217
Cdd:cd05258    80 TAAQPSVTTSASSPRLDFETNALGTLNVLEAARQHApnAPFIFTSTNKVYGD---LPNYLPLeeletrY-ELAPEGWSPA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 218 -YDEG-------------KRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMN-DGRVVSNFILQALQGEPLTVYGSG-S 281
Cdd:cd05258   156 gISESfpldfshslygasKGAADQYVQEYGRIFGLKTVVFRCGCLTGPRQFGTeDQGWVAYFLKCAVTGKPLTIFGYGgK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 282 QTRAFQYVSDLVNGLVALMNSNVSSP---VNLGNPEEH--TILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAK 356
Cdd:cd05258   236 QVRDVLHSADLVNLYLRQFQNPDRRKgevFNIGGGRENsvSLLELIALCEEITGRKMESYKDENRPGDQIWYISDIRKIK 315
                         330       340
                  ....*....|....*....|.
gi 1046903405 357 LMLGWEPVVPLEEGLNKAIHY 377
Cdd:cd05258   316 EKPGWKPERDPREILAEIYAW 336
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
77-369 5.07e-36

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: 134.26  E-value: 5.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHEN--FELINHDV------------VEPlyievDQ 142
Cdd:cd05260     1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHLYINKdrITLHYGDLtdssslrraiekVRP-----DE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 143 IYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAK--RVGARLLLASTSEVYGDPEVHPQSEDywghvNPIGPRACYDE 220
Cdd:cd05260    76 IYHLAAQSHVKVSFDDPEYTAEVNAVGTLNLLEAIRilGLDARFYQASSSEEYGKVQELPQSET-----TPFRPRSPYAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 221 GKRVAETMCYAYMKQEGVEVRVARIFNTFGPRmhMNDGRVVSNFILQAL-----QGEPLTVyGSGSQTRAFQYVSDLVNG 295
Cdd:cd05260   151 SKLYADWITRNYREAYGLFAVNGRLFNHEGPR--RGETFVTRKITRQVArikagLQPVLKL-GNLDAKRDWGDARDYVEA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 296 LVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIqflsEAQDDPQKRKP--------DIKKAKLMLGWEPVVPL 367
Cdd:cd05260   228 YWLLLQQGEPDDYVIATGETHSVREFVELAFEESGLTGDI----EVEIDPRYFRPtevdlllgDPSKAREELGWKPEVSF 303

                  ..
gi 1046903405 368 EE 369
Cdd:cd05260   304 EE 305
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
61-383 8.59e-36

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


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 134.94  E-value: 8.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  61 TQKYPPvkflSEKdrKRILITGGAGFVGSHLTDKLMMDGHEVTVVDnfftgRKRNvEHW----IGHEnFELINHDVVE-- 134
Cdd:PLN02695   13 REPYWP----SEK--LRICITGAGGFIASHIARRLKAEGHYIIASD-----WKKN-EHMsedmFCHE-FHLVDLRVMEnc 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 135 -PLYIEVDQIYHLASPASPPNY--------MYNpiktlktNTIGTLNMLGLAKRVGA-RLLLASTSEVYG-----DPEVH 199
Cdd:PLN02695   80 lKVTKGVDHVFNLAADMGGMGFiqsnhsviMYN-------NTMISFNMLEAARINGVkRFFYASSACIYPefkqlETNVS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 200 PQSEDYWghvnPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGR--VVSNFILQALQG-EPLTV 276
Cdd:PLN02695  153 LKESDAW----PAEPQDAYGLEKLATEELCKHYTKDFGIECRIGRFHNIYGPFGTWKGGRekAPAAFCRKALTStDEFEM 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 277 YGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLsEAQDDPQKRKPDIKKAK 356
Cdd:PLN02695  229 WGDGKQTRSFTFIDECVEGVLRLTKSDFREPVNIGSDEMVSMNEMAEIALSFENKKLPIKHI-PGPEGVRGRNSDNTLIK 307
                         330       340
                  ....*....|....*....|....*..
gi 1046903405 357 LMLGWEPVVPLEEGLNKAIHYFRKELE 383
Cdd:PLN02695  308 EKLGWAPTMRLKDGLRITYFWIKEQIE 334
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
77-379 4.94e-34

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


Pssm-ID: 187550 [Multi-domain]  Cd Length: 300  Bit Score: 128.47  E-value: 4.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLM-MDGHEVTVvdnfftgrkrnvehwIGHENFELINHDVVEPLYIEV--DQIYHLASPASPP 153
Cdd:cd05239     1 KILVTGHRGLVGSAIVRVLArRGYENVVF---------------RTSKELDLTDQEAVRAFFEKEkpDYVIHLAAKVGGI 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 154 --NyMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTSEVYGDPEVHPQSEDYWgHVNPIGP-RACYDEGKRVAETMC 229
Cdd:cd05239    66 vaN-MTYPADFLRDNLLINDNVIHAAHRFGvKKLVFLGSSCIYPDLAPQPIDESDL-LTGPPEPtNEGYAIAKRAGLKLC 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 230 YAYMKQEGVEVRVARIFNTFGPR--MHMNDGRVV----SNFILQALQG-EPLTVYGSGSQTRAFQYVSDLVNGLVALMNs 302
Cdd:cd05239   144 EAYRKQYGCDYISVMPTNLYGPHdnFDPENSHVIpaliRKFHEAKLRGgKEVTVWGSGTPRREFLYSDDLARAIVFLLE- 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903405 303 NVSSP--VNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKlMLGWEPVVPLEEGLNKAIHYFR 379
Cdd:cd05239   223 NYDEPiiVNVGSGVEISIRELAEAIAEVVGFKGEIVFDTSKPDGQPRKLLDVSKLR-ALGWFPFTPLEQGIRETYEWYL 300
PLN02427 PLN02427
UDP-apiose/xylose synthase
77-397 2.21e-33

UDP-apiose/xylose synthase


Pssm-ID: 178047 [Multi-domain]  Cd Length: 386  Bit Score: 128.82  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDG-HEVTVVDNFFTGRKRNVE----HWIGHENFELIN--HDV-VEPLYIEVDQIYHLAS 148
Cdd:PLN02427   16 TICMIGAGGFIGSHLCEKLMTETpHKVLALDVYNDKIKHLLEpdtvPWSGRIQFHRINikHDSrLEGLIKMADLTINLAA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 149 PASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGD------PEVHPQSEDYWGHV-----NP--IGP- 214
Cdd:PLN02427   96 ICTPADYNTRPLDTIYSNFIDALPVVKYCSENNKRLIHFSTCEVYGKtigsflPKDHPLRQDPAFYVlkedeSPciFGSi 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 215 ---RACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDG---------RVVSNFILQALQGEPLTVYGSGSQ 282
Cdd:PLN02427  176 ekqRWSYACAKQLIERLIYAEGAENGLEFTIVRPFNWIGPRMDFIPGidgpsegvpRVLACFSNNLLRREPLKLVDGGQS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 283 TRAFQYVSDLVNGlVALMNSNVSSP----VNLGNPE-EHTILEFAQLIKNLVG--SG-----------SEIQFLSEAQDD 344
Cdd:PLN02427  256 QRTFVYIKDAIEA-VLLMIENPARAnghiFNVGNPNnEVTVRQLAEMMTEVYAkvSGepaleeptvdvSSKEFYGEGYDD 334
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046903405 345 PQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEyQANNQYIPKPKPA 397
Cdd:PLN02427  335 SDKRIPDMTIINKQLGWNPKTSLWDLLESTLTYQHKTYA-EAIKKAMSKPTAS 386
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
77-369 2.17e-31

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: 121.87  E-value: 2.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEhWIGHENFELINHDVVEPLYIE-------VDQIYHLASP 149
Cdd:cd05247     1 KVLVTGGAGYIGSHTVVELLEAGYDVVVLDNLSNGHREALP-RIEKIRIEFYEGDIRDRAALDkvfaehkIDAVIHFAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 150 ASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVHPQSEDYwghvnPIGPRACYDEGKRVAETM 228
Cdd:cd05247    80 KAVGESVQKPLKYYDNNVVGTLNLLEAMRAHGVkNFVFSSSAAVYGEPETVPITEEA-----PLNPTNPYGRTKLMVEQI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 229 CYAYMKQEGVEVRVARIFNTFGPrmHMN-----DGRVVSN---FILQALQG--EPLTVYGS------GSQTRAFQYVSDL 292
Cdd:cd05247   155 LRDLAKAPGLNYVILRYFNPAGA--HPSgligeDPQIPNNlipYVLQVALGrrEKLAIFGDdyptpdGTCVRDYIHVVDL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 293 VNG----LVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLvgSGSEIQ--FLSEAQDDPQKRKPDIKKAKLMLGWEPVVP 366
Cdd:cd05247   233 ADAhvlaLEKLENGGGSEIYNLGTGRGYSVLEVVEAFEKV--SGKPIPyeIAPRRAGDPASLVADPSKAREELGWKPKRD 310

                  ...
gi 1046903405 367 LEE 369
Cdd:cd05247   311 LED 313
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
73-383 1.45e-28

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 117.78  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  73 KDRKRILITGGAGFVGSHLTDKLMMDGH-EVTVVDnffTGRKRnVEHWIGHENFELINHDV-VEPLYIE-----VDQIYH 145
Cdd:PRK08125  313 KRRTRVLILGVNGFIGNHLTERLLRDDNyEVYGLD---IGSDA-ISRFLGHPRFHFVEGDIsIHSEWIEyhikkCDVVLP 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 146 LASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYG---DPEVhpqSEDywgHVNPI-GP----RAC 217
Cdd:PRK08125  389 LVAIATPIEYTRNPLRVFELDFEENLKIIRYCVKYNKRIIFPSTSEVYGmctDKYF---DED---TSNLIvGPinkqRWI 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 218 YDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRM------HMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFqyvSD 291
Cdd:PRK08125  463 YSVSKQLLDRVIWAYGEKEGLRFTLFRPFNWMGPRLdnlnaaRIGSSRAITQLILNLVEGSPIKLVDGGKQKRCF---TD 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 292 LVNGLVALM----NSNVSSP---VNLGNPE-EHTILEFAQLIK------------------NLVGSGSeiqFLSEAQDDP 345
Cdd:PRK08125  540 IRDGIEALFriieNKDNRCDgqiINIGNPDnEASIRELAEMLLasfekhplrdhfppfagfRVVESSS---YYGKGYQDV 616
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1046903405 346 QKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELE 383
Cdd:PRK08125  617 EHRKPSIRNARRLLDWEPKIDMQETIDETLDFFLRTVD 654
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
76-384 4.74e-28

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 116.38  E-value: 4.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMD--GHEVTVVDNF-FTGRKRNVEHWIGHENFELINHDV-----VEPLYI--EVDQIYH 145
Cdd:PLN02260    7 KNILITGAAGFIASHVANRLIRNypDYKIVVLDKLdYCSNLKNLNPSKSSPNFKFVKGDIasadlVNYLLIteGIDTIMH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 146 LASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGA--RLLLASTSEVYGDPEV------HPQSEdywghVNPIGPrac 217
Cdd:PLN02260   87 FAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQirRFIHVSTDEVYGETDEdadvgnHEASQ-----LLPTNP--- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 218 YDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPrmHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGL- 296
Cdd:PLN02260  159 YSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGP--NQFPEKLIPKFILLAMQGKPLPIHGDGSNVRSYLYCEDVAEAFe 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 297 VALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSE--IQFLSEAQDDPQKRKPDIKKAKlMLGWEPVVPLEEGLNKA 374
Cdd:PLN02260  237 VVLHKGEVGHVYNIGTKKERRVIDVAKDICKLFGLDPEksIKFVENRPFNDQRYFLDDQKLK-KLGWQERTSWEEGLKKT 315
                         330
                  ....*....|
gi 1046903405 375 IHYFRKELEY 384
Cdd:PLN02260  316 MEWYTSNPDW 325
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
76-378 1.61e-27

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 112.05  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHE-VTVVDNF-FTGRKRNVEHWIGHENFELINHDVVEPLYIE-------VDQIYHL 146
Cdd:PRK10217    2 RKILITGGAGFIGSALVRYIINETSDaVVVVDKLtYAGNLMSLAPVAQSERFAFEKVDICDRAELArvftehqPDCVMHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 147 ASPASPPNYMYNPIKTLKTNTIGTLNMLGLA----------KRVGARLLLASTSEVYGDpeVHpQSEDYWGHVNPIGPRA 216
Cdd:PRK10217   82 AAESHVDRSIDGPAAFIETNIVGTYTLLEAAraywnaltedKKSAFRFHHISTDEVYGD--LH-STDDFFTETTPYAPSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 217 CYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPrMHMNDgRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGL 296
Cdd:PRK10217  159 PYSASKASSDHLVRAWLRTYGLPTLITNCSNNYGP-YHFPE-KLIPLMILNALAGKPLPVYGNGQQIRDWLYVEDHARAL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 297 -VALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGS------------GSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEP 363
Cdd:PRK10217  237 yCVATTGKVGETYNIGGHNERKNLDVVETICELLEElapnkpqgvahyRDLITFVADRPGHDLRYAIDASKIARELGWLP 316
                         330
                  ....*....|....*
gi 1046903405 364 VVPLEEGLNKAIHYF 378
Cdd:PRK10217  317 QETFESGMRKTVQWY 331
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
76-369 2.01e-27

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


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 110.88  E-value: 2.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIE--VDQIYHLASPASPP 153
Cdd:COG1087     1 MKILVTGGAGYIGSHTVVALLEAGHEVVVLDNLSNGHREAVPKGVPFVEGDLRDRAALDRVFAEhdIDAVIHFAALKAVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 154 NYMYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVHPQSEDYwgHVNPIGPracYDEGKRVAETM---- 228
Cdd:COG1087    81 ESVEKPLKYYRNNVVGTLNLLEAMREAGVkRFVFSSSAAVYGEPESVPITEDA--PTNPTNP---YGRSKLMVEQIlrdl 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 229 CYAYmkqegvEVRVA--RIFNTFG--PRMHM-NDGRVVSN---FILQALQG--EPLTVYGS------GSQTRAFQYVSDL 292
Cdd:COG1087   156 ARAY------GLRYValRYFNPAGahPSGRIgEDHGPPTHlipLVLQVALGkrEKLSVFGDdyptpdGTCVRDYIHVVDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 293 VNGLVA----LMNSNVSSPVNLGNPEEHTILE----FAQLiknlvgSGSEIqflsEAQDDPqkRKP--------DIKKAK 356
Cdd:COG1087   230 ADAHVLaleyLLAGGGSEVFNLGTGRGYSVLEvidaFERV------TGRPI----PYEIAP--RRPgdpaalvaDSEKAR 297
                         330
                  ....*....|...
gi 1046903405 357 LMLGWEPVVPLEE 369
Cdd:COG1087   298 RELGWKPKYDLED 310
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
76-380 9.93e-27

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: 108.74  E-value: 9.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKrnvEHWIGHENFELI-----NHDVVEPLY--IEVDQIYHLAS 148
Cdd:cd08957     1 MKVLITGGAGQIGSHLIEHLLERGHQVVVIDNFATGRR---EHLPDHPNLTVVegsiaDKALVDKLFgdFKPDAVVHTAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 149 PASPPNYMYNpikTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYG-DPEVHPQSEDYwghvnpigPRACYDEGKRVAE 226
Cdd:cd08957    78 AYKDPDDWYE---DTLTNVVGGANVVQAAKKAGVkRLIYFQTALCYGlKPMQQPIRLDH--------PRAPPGSSYAISK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 227 TMCYAYMKQEGVEVRVARIFNTFGPRmhmNDGRVVSNFILQALQGEPLTVygsgSQT-RAFQYVSDLVNglVALMNSNVS 305
Cdd:cd08957   147 TAGEYYLELSGVDFVTFRLANVTGPR---NVIGPLPTFYQRLKAGKKCFV----TDTrRDFVFVKDLAR--VVDKALDGI 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 306 SP---VNLGNPEEHTILEFAQLIKNLVG--SGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRK 380
Cdd:cd08957   218 RGhgaYHFSSGEDVSIKELFDAVVEALDlpLRPEVEVVELGPDDVPSILLDPSRTFQDFGWKEFTPLSETVSAALAWYDK 297
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
76-378 6.14e-26

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


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 107.49  E-value: 6.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNV---------EHWighENFELINHDV-----VEPLYIEVD 141
Cdd:PRK15181   16 KRWLITGVAGFIGSGLLEELLFLNQTVIGLDNFSTGYQHNLddvrtsvseEQW---SRFIFIQGDIrkftdCQKACKNVD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 142 QIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTSEVYGDPEVHPQSEDYWGHvnPIGPracYDE 220
Cdd:PRK15181   93 YVLHQAALGSVPRSLKDPIATNSANIDGFLNMLTAARDAHvSSFTYAASSSTYGDHPDLPKIEERIGR--PLSP---YAV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 221 GKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDG--RVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNG-LV 297
Cdd:PRK15181  168 TKYVNELYADVFARSYEFNAIGLRYFNVFGRRQNPNGAysAVIPRWILSLLKDEPIYINGDGSTSRDFCYIENVIQAnLL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 298 ALMNSNVSSP---VNLGNPEEHTILEFAQLIKNLVG------SGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLE 368
Cdd:PRK15181  248 SATTNDLASKnkvYNVAVGDRTSLNELYYLIRDGLNlwrneqSRAEPIYKDFRDGDVKHSQADITKIKTFLSYEPEFDIK 327
                         330
                  ....*....|
gi 1046903405 369 EGLNKAIHYF 378
Cdd:PRK15181  328 EGLKQTLKWY 337
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
78-370 6.75e-22

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


Pssm-ID: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 95.45  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDG-HEVTVVDNFFTGRK------RNVEHWIGHENF-ELINHDVVEPlyiEVDQIYHLASP 149
Cdd:cd05248     2 IIVTGGAGFIGSNLVKALNERGiTDILVVDNLSNGEKfknlvgLKIADYIDKDDFkDWVRKGDENF---KIEAIFHQGAC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 150 ASPP----NYMynpiktLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRA----CYDeg 221
Cdd:cd05248    79 SDTTetdgKYM------MDNNYQYTKELLHYCLEKKIRFIYASSAAVYGNGSLGFAEDIETPNLRPLNVYGysklLFD-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 222 krvaetmCYAYMKQEGVEVRVA--RIFNTFGPRmHMNDGR---VVSNFILQALQGEPLTV------YGSGSQTRAFQYVS 290
Cdd:cd05248   151 -------QWARRHGKEVLSQVVglRYFNVYGPR-EYHKGRmasVVFHLFNQIKAGEKVKLfkssdgYADGEQLRDFVYVK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 291 DLVNGLVALM-NSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFL---SEAQDDPQK-RKPDIKKaKLMLGW-EPV 364
Cdd:cd05248   223 DVVKVNLFFLeNPSVSGIFNVGTGRARSFNDLASATFKALGKEVKIEYIdfpEDLRGKYQSfTEADISK-LRAAGYtKEF 301

                  ....*.
gi 1046903405 365 VPLEEG 370
Cdd:cd05248   302 HSLEEG 307
heptose_epim TIGR02197
ADP-L-glycero-D-manno-heptose-6-epimerase; This family consists of examples of ...
78-372 7.52e-22

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


Pssm-ID: 274028 [Multi-domain]  Cd Length: 314  Bit Score: 95.04  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGH-EVTVVDNFFTG------RKRNVEHWIGHENF-ELINHDVveplYIEVDQIYHLASP 149
Cdd:TIGR02197   1 IIVTGGAGFIGSNLVKALNERGItDILVVDNLRDGhkflnlADLVIADYIDKEDFlDRLEKGA----FGKIEAIFHQGAC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 150 ASppNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVhPQSEDywghVNPIGPRACYDEGKRVAETMC 229
Cdd:TIGR02197  77 SD--TTETDGEYMMENNYQYSKRLLDWCAEKGIPFIYASSAATYGDGEA-GFREG----RELERPLNVYGYSKFLFDQYV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 230 YAYMKQEGVEVRVA--RIFNTFGPR-MHMND-GRVVSNFILQALQGEPLTVYGS------GSQTRAFQYVSDLVNGLVAL 299
Cdd:TIGR02197 150 RRRVLPEALSAQVVglRYFNVYGPReYHKGKmASVAFHLFNQIKAGGNVKLFKSsegfkdGEQLRDFVYVKDVVDVNLWL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 300 MNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLseaqDDPQKRKP--------DIKKAKLMLGWEPVVPLEEGL 371
Cdd:TIGR02197 230 LENGVSGIFNLGTGRARSFNDLADAVFKALGKDEKIEYI----PMPEALRGryqyftqaDITKLRAAGYYGPFTTLEEGV 305

                  .
gi 1046903405 372 N 372
Cdd:TIGR02197 306 K 306
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
79-378 6.31e-20

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


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 89.37  E-value: 6.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  79 LITGGAGFVGSHLTDKLMMDGHEVTVVDNfftgrkrnvehwigHENFELINHDVVEPLYIEVDQIY--HLASP-----AS 151
Cdd:PLN02725    1 FVAGHRGLVGSAIVRKLEALGFTNLVLRT--------------HKELDLTRQADVEAFFAKEKPTYviLAAAKvggihAN 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 ppnyMYNPIKTLKTNTIGTLNMLGLAKRVGAR-LLLASTSEVYgdPEVHPQsedywghvnPI-------GPRACYDEG-- 221
Cdd:PLN02725   67 ----MTYPADFIRENLQIQTNVIDAAYRHGVKkLLFLGSSCIY--PKFAPQ---------PIpetalltGPPEPTNEWya 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 222 --KRVAETMCYAYMKQEGVEVRVARIFNTFGPR--MHMNDGRVVSNFI----LQALQGEPLT-VYGSGSQTRAFQYVSDL 292
Cdd:PLN02725  132 iaKIAGIKMCQAYRIQYGWDAISGMPTNLYGPHdnFHPENSHVIPALIrrfhEAKANGAPEVvVWGSGSPLREFLHVDDL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 293 VNGLVALMNS-NVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAkLMLGWEPVVPLEEGL 371
Cdd:PLN02725  212 ADAVVFLMRRySGAEHVNVGSGDEVTIKELAELVKEVVGFEGELVWDTSKPDGTPRKLMDSSKL-RSLGWDPKFSLKDGL 290

                  ....*..
gi 1046903405 372 NKAIHYF 378
Cdd:PLN02725  291 QETYKWY 297
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
77-378 1.38e-19

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


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 89.03  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLM-MDGHEVTVVDNFFTGRKrnveHW-IGHENFELINHDVVEPLYIE-----VDQIYHLASP 149
Cdd:cd05241     1 SVLVTGGSGFFGERLVKQLLeRGGTYVRSFDIAPPGEA----LSaWQHPNIEFLKGDITDRNDVEqalsgADCVFHTAAI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 150 ASP--PNYMYNpiktlKTNTIGTLNMLGLAKRVGA-RLLLASTSEVY--GDPeVHPQSEDYwghvnPIGPRA--CYDEGK 222
Cdd:cd05241    77 VPLagPRDLYW-----EVNVGGTQNVLDACQRCGVqKFVYTSSSSVIfgGQN-IHNGDETL-----PYPPLDsdMYAETK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 223 RVAETMCYAYMKQEGVEVRVARIFNTFGPRmhmnDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNS 302
Cdd:cd05241   146 AIAEIIVLEANGRDDLLTCALRPAGIFGPG----DQGLVPILFEWAEKGLVKFVFGRGNNLVDFTYVHNLAHAHILAAAA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 303 NVS------SPVNLGNPEEHTILEFAQLIKNLVGSGSEIQ------------FLSEAQDDPQKRKP-------------- 350
Cdd:cd05241   222 LVKgktisgQTYFITDAEPHNMFELLRPVWKALGFGSRPKirlsgplaycaaLLSELVSFMLGPYFvfspfyvralvtpm 301
                         330       340       350
                  ....*....|....*....|....*....|
gi 1046903405 351 --DIKKAKLMLGWEPVVPLEEGLNKAIHYF 378
Cdd:cd05241   302 yfSIAKAQKDLGYAPRYSNEEGLIETLNWY 331
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
76-386 2.42e-18

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: 85.45  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVT-------VVDNFFtgRKRNVEHWIGHENFELINHDVVEPLYIEV--DQIYHL 146
Cdd:cd05252     5 KRVLVTGHTGFKGSWLSLWLQELGAKVIgysldppTNPNLF--ELANLDNKISSTRGDIRDLNALREAIREYepEIVFHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 147 AspASP-PNYMY-NPIKTLKTNTIGTLNMLGLAKRVGA--RLLLASTSEVYGDPE-VHPQSEDywghvNPIGPRACYDEG 221
Cdd:cd05252    83 A--AQPlVRLSYkDPVETFETNVMGTVNLLEAIRETGSvkAVVNVTSDKCYENKEwGWGYREN-----DPLGGHDPYSSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 222 KRVAE----TMCYAYMKQE-----GVEVRVARIFNTFGPRmHMNDGRVVSNFILQALQGEPLTVYGSGSqTRAFQYVSDL 292
Cdd:cd05252   156 KGCAEliisSYRNSFFNPEnygkhGIAIASARAGNVIGGG-DWAEDRIVPDCIRAFEAGERVIIRNPNA-IRPWQHVLEP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 293 VNGLVAL---MNSN---VSSPVNLGNPEEH--TILEFAQLIKNLVGSGSEIQFLSEAQDDPQKR-KPDIKKAKLMLGWEP 363
Cdd:cd05252   234 LSGYLLLaekLYERgeeYAEAWNFGPDDEDavTVLELVEAMARYWGEDARWDLDGNSHPHEANLlKLDCSKAKTMLGWRP 313
                         330       340
                  ....*....|....*....|...
gi 1046903405 364 VVPLEEGLNKAIHYFRKELEYQA 386
Cdd:cd05252   314 RWNLEETLEFTVAWYKEWLSGED 336
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
77-390 2.50e-18

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 85.61  E-value: 2.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTV-VDNF-FTGRKRNVEHWIGHE--NFELIN------HDVVEPLYiEVDQIYHL 146
Cdd:PRK10084    2 KILVTGGAGFIGSAVVRHIINNTQDSVVnVDKLtYAGNLESLADVSDSEryVFEHADicdraeLDRIFAQH-QPDAVMHL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 147 ASPASPPNYMYNPIKTLKTNTIGTLNMLGLA----------KRVGARLLLASTSEVYGD----PEVHPQSE-DYWGHVNP 211
Cdd:PRK10084   81 AAESHVDRSITGPAAFIETNIVGTYVLLEAArnywsaldedKKNAFRFHHISTDEVYGDlphpDEVENSEElPLFTETTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 212 IGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPrMHMNDgRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSD 291
Cdd:PRK10084  161 YAPSSPYSASKASSDHLVRAWLRTYGLPTIVTNCSNNYGP-YHFPE-KLIPLVILNALEGKPLPIYGKGDQIRDWLYVED 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 292 LVNGLVALMNSN-VSSPVNLGNPEEHTILEFAQLIKNLVGS-----GSEIQFLSEAQDDP-QKRKPDIKKAKLM--LGWE 362
Cdd:PRK10084  239 HARALYKVVTEGkAGETYNIGGHNEKKNLDVVLTICDLLDEivpkaTSYREQITYVADRPgHDRRYAIDASKISreLGWK 318
                         330       340
                  ....*....|....*....|....*...
gi 1046903405 363 PVVPLEEGLNKAIHYfrkeleYQANNQY 390
Cdd:PRK10084  319 PQETFESGIRKTVEW------YLANTEW 340
SQD1_like_SDR_e cd05255
UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) ...
77-393 7.30e-18

UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) SDRs; Arabidopsis thaliana UDP-sulfoquinovose-synthase ( SQD1), an extended SDR, catalyzes the transfer of SO(3)(-) to UDP-glucose in the biosynthesis of plant sulfolipids. Members of this subgroup share the conserved SDR catalytic residues, and a partial match to the characteristic extended-SDR NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187565 [Multi-domain]  Cd Length: 382  Bit Score: 84.36  E-value: 7.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTgRKRNVE------------------------HWIGHENFELINHDV 132
Cdd:cd05255     2 KVLILGGDGYCGWPTALHLSKRGHEVCIVDNLVR-RRIDVElglesltpiasiherlrawkeltgKTIEFYVGDACDYEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 133 VEPLY--IEVDQIYHLASPASPPNYMYN---PIKTLKTNTIGTLNMLGLAKRVG--ARLLLASTSEVYGDPEVhPQSEDY 205
Cdd:cd05255    81 LAELLasHEPDAVVHFAEQRSAPYSMIDrehANYTQHNNVIGTLNLLFAIKEFDpdCHLVKLGTMGEYGTPNI-DIPEGY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 206 WGHVN---------PIGPRACYDEGKRVAETMCYAYMKQEGV---EVRVARIFNTFGPRMHMND------------GRVV 261
Cdd:cd05255   160 ITIEHngrrdtlpyPKQAGSWYHLSKVHDSHNIMFACKAWGIritDLNQGVVYGTKTEETEADErlinrfdydgvfGTVL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 262 SNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGL-VALMNSNVSSPVNLGN--PEEHTILEFAQLIK---NLVGSGSEI 335
Cdd:cd05255   240 NRFCVQAAIGHPLTVYGKGGQTRGFISIRDTVQCLeLALENPAKAGEYRVFNqfTEQFSVGELAEMVAeagSKLGLDVKV 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903405 336 QFLSEAQDDPQKRKPDIKKAKLM-LGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPK 393
Cdd:cd05255   320 EHLPNPRVEAEEHYYNAKNTKLLdLGLEPHYLSESLLDSILNFAVKYADRVDEKRILPK 378
PLN02240 PLN02240
UDP-glucose 4-epimerase
75-362 4.00e-17

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 81.93  E-value: 4.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  75 RKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEH---WIGHENFELINHDV-------VEPLYIE--VDQ 142
Cdd:PLN02240    5 GRTILVTGGAGYIGSHTVLQLLLAGYKVVVIDNLDNSSEEALRRvkeLAGDLGDNLVFHKVdlrdkeaLEKVFAStrFDA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 143 IYHLA-------SPASPPNYMYNpiktlktNTIGTLNMLGLAKRVGARLLLASTS-EVYGDPEVHPQSEDYwghvnPIGP 214
Cdd:PLN02240   85 VIHFAglkavgeSVAKPLLYYDN-------NLVGTINLLEVMAKHGCKKLVFSSSaTVYGQPEEVPCTEEF-----PLSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 215 RACYDEGKRVAETMCYAYMKQEGvEVRVA--RIFNTFG--PRMHM-NDGRVVSN----FILQALQG--EPLTVYGS---- 279
Cdd:PLN02240  153 TNPYGRTKLFIEEICRDIHASDP-EWKIIllRYFNPVGahPSGRIgEDPKGIPNnlmpYVQQVAVGrrPELTVFGNdypt 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 280 --GSQTRAFQYVSDLVNGLVALMNSNVSSP------VNLGNPEEHTILEFAQLIKNlvGSGSEIqflseaqddPQK---R 348
Cdd:PLN02240  232 kdGTGVRDYIHVMDLADGHIAALRKLFTDPdigceaYNLGTGKGTSVLEMVAAFEK--ASGKKI---------PLKlapR 300
                         330       340
                  ....*....|....*....|..
gi 1046903405 349 KP--------DIKKAKLMLGWE 362
Cdd:PLN02240  301 RPgdaeevyaSTEKAEKELGWK 322
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
76-335 2.52e-16

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


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 78.10  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVvdnFFTGRKRN-----VEHWIG-----HENFELINH---DVVeplyieVDQ 142
Cdd:cd05265     1 MKILIIGGTRFIGKALVEELLAAGHDVTV---FNRGRTKPdlpegVEHIVGdrndrDALEELLGGedfDVV------VDT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 143 I-YHLASpasppnymynpiktlktntigTLNMLGLAKRVGARLLLASTSEVYGDP-----EVHPQSEDYWGHVNPIGPra 216
Cdd:cd05265    72 IaYTPRQ---------------------VERALDAFKGRVKQYIFISSASVYLKPgrvitESTPLREPDAVGLSDPWD-- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 217 cYDEGKRVAETMcyaYMKQEGVEVRVARIFNTFGPRmhmNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGL 296
Cdd:cd05265   129 -YGRGKRAAEDV---LIEAAAFPYTIVRPPYIYGPG---DYTGRLAYFFDRLARGRPILVPGDGHSLVQFIHVKDLARAL 201
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1046903405 297 VALM--NSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEI 335
Cdd:cd05265   202 LGAAgnPKAIGGIFNITGDEAVTWDELLEACAKALGKEAEI 242
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
77-369 5.95e-15

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 75.24  E-value: 5.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVDNfFTGRKRNV----EHWIGHENfELINHDVV-EPLYIE------VDQIYH 145
Cdd:PRK10675    2 RVLVTGGSGYIGSHTCVQLLQNGHDVVILDN-LCNSKRSVlpviERLGGKHP-TFVEGDIRnEALLTEilhdhaIDTVIH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 146 LASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGAR-LLLASTSEVYGDPEVHPQSEDYwghvnPIG-PRACYDEGKR 223
Cdd:PRK10675   80 FAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANVKnLIFSSSATVYGDQPKIPYVESF-----PTGtPQSPYGKSKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 224 VAETMCYAYMK-QEGVEVRVARIFNTFG--PRMHM-NDGRVVSN----FILQALQG--EPLTVYGS------GSQTRAFQ 287
Cdd:PRK10675  155 MVEQILTDLQKaQPDWSIALLRYFNPVGahPSGDMgEDPQGIPNnlmpYIAQVAVGrrDSLAIFGNdyptedGTGVRDYI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 288 YVSDLVNGLVALMNSNVSSP----VNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEP 363
Cdd:PRK10675  235 HVMDLADGHVAAMEKLANKPgvhiYNLGAGVGSSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYWADASKADRELNWRV 314

                  ....*.
gi 1046903405 364 VVPLEE 369
Cdd:PRK10675  315 TRTLDE 320
Gmd COG1089
GDP-D-mannose dehydratase [Cell wall/membrane/envelope biogenesis];
76-218 9.06e-15

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


Pssm-ID: 440706 [Multi-domain]  Cd Length: 321  Bit Score: 74.73  E-value: 9.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTvvdnfftGRKR--------NVEHWIGHENFELINHDV------------VEP 135
Cdd:COG1089     1 KTALITGITGQDGSYLAELLLEKGYEVH-------GIVRrsstfnteRIDHLGIDDRLFLHYGDLtdsssliriiqeVQP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 136 lyievDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG--ARLLLASTSEVYGDPEVHPQSEDywghvNPIG 213
Cdd:COG1089    74 -----DEIYNLAAQSHVGVSFEQPEYTADVTALGTLRLLEAIRILGpkTRFYQASSSEMFGLVQEVPQSET-----TPFY 143

                  ....*
gi 1046903405 214 PRACY 218
Cdd:COG1089   144 PRSPY 148
UXS1_N pfam11803
UDP-glucuronate decarboxylase N-terminal; The N-terminus of the UDP-glucuronate decarboxylases ...
15-65 3.46e-14

UDP-glucuronate decarboxylase N-terminal; The N-terminus of the UDP-glucuronate decarboxylases may be involved in localization to the perinuclear Golgi membrane.


Pssm-ID: 463356  Cd Length: 75  Bit Score: 67.19  E-value: 3.46e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1046903405  15 VWGNFVNMsfllnRSIQENGELKIESKIEEIIEPLREKIRDLEKSFTQKYP 65
Cdd:pfam11803  30 VWGTYVNM-----RSIQENGEQKVEQKIEEVVAPLREKIRDLEKSFTQKYP 75
PLN02653 PLN02653
GDP-mannose 4,6-dehydratase
71-369 1.14e-13

GDP-mannose 4,6-dehydratase


Pssm-ID: 178259 [Multi-domain]  Cd Length: 340  Bit Score: 71.34  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  71 SEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVV----DNFFTGRkrnVEHWI--GHENFELIN-H------------- 130
Cdd:PLN02653    2 GDPPRKVALITGITGQDGSYLTEFLLSKGYEVHGIirrsSNFNTQR---LDHIYidPHPNKARMKlHygdlsdasslrrw 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 131 -DVVEPlyievDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNML------GLAKRVGARLLLASTSEVYGD-PEvhPQS 202
Cdd:PLN02653   79 lDDIKP-----DEVYNLAAQSHVAVSFEMPDYTADVVATGALRLLeavrlhGQETGRQIKYYQAGSSEMYGStPP--PQS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 203 EDywghvNPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNdgrVVSNFILQAL----QGEPLTVY- 277
Cdd:PLN02653  152 ET-----TPFHPRSPYAVAKVAAHWYTVNYREAYGLFACNGILFNHESPRRGEN---FVTRKITRAVgrikVGLQKKLFl 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 278 GSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGsgseIQFLSEAQDDPQKRKP------- 350
Cdd:PLN02653  224 GNLDASRDWGFAGDYVEAMWLMLQQEKPDDYVVATEESHTVEEFLEEAFGYVG----LNWKDHVEIDPRYFRPaevdnlk 299
                         330       340
                  ....*....|....*....|
gi 1046903405 351 -DIKKAKLMLGWEPVVPLEE 369
Cdd:PLN02653  300 gDASKAREVLGWKPKVGFEQ 319
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
77-378 1.20e-13

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: 71.24  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGH-EVTVVDNFFTGRKRNVEHwiGHENF---ELINHDVVEPLYIE--VDQIYHLASPA 150
Cdd:cd09813     1 SCLVVGGSGFLGRHLVEQLLRRGNpTVHVFDIRPTFELDPSSS--GRVQFhtgDLTDPQDLEKAFNEkgPNVVFHTASPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 151 SPPNY-MYNpiktlKTNTIGTLNMLGLAKRVGARLLL--ASTSEVYGDPEVHPQSEDyWGHvnPIGPRACYDEGKRVAET 227
Cdd:cd09813    79 HGSNDdLYY-----KVNVQGTRNVIEACRKCGVKKLVytSSASVVFNGQDIINGDES-LPY--PDKHQDAYNETKALAEK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 228 MCYAYMKQEG----VEVRVARIfntFGPRmhmnDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLV----AL 299
Cdd:cd09813   151 LVLKANDPESglltCALRPAGI---FGPG----DRQLVPGLLKAAKNGKTKFQIGDGNNLFDFTYVENVAHAHIlaadAL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 300 MNSNVSSPVN------------------------LGNPEEHTIlEFAQLIKNLVGSGSEIQFL---SEAQDDPQK----- 347
Cdd:cd09813   224 LSSSHAETVAgeaffitndepiyfwdfaraiwegLGYERPPSI-KLPRPVALYLASLLEWTCKvlgKEPTFTPFRvallc 302
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1046903405 348 --RKPDIKKAKLMLGWEPVVPLEEGLNKAIHYF 378
Cdd:cd09813   303 stRYFNIEKAKKRLGYTPVVTLEEGIERTLQWF 335
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
77-372 2.00e-13

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: 69.96  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVtvvdnFFTGRKRNvehwiGHENFELINHDVVEPLYIEV--DQIYHLASPASPPN 154
Cdd:cd05254     1 KILITGATGMLGRALVRLLKERGYEV-----IGTGRSRA-----SLFKLDLTDPDAVEEAIRDYkpDVIINCAAYTRVDK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 155 YMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYgDPEVHPQSEDywGHVNPIGpraCYDEGKRVAETmCYAYMK 234
Cdd:cd05254    71 CESDPELAYRVNVLAPENLARAAKEVGARLIHISTDYVF-DGKKGPYKEE--DAPNPLN---VYGKSKLLGEV-AVLNAN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 235 QEGVEVRVARIFNTFGprmhmNDGRVVSNFILQALQGEPLTVY----GSGSqtrafqYVSDLVNGLVALMNSNVSSPV-N 309
Cdd:cd05254   144 PRYLILRTSWLYGELK-----NGENFVEWMLRLAAERKEVNVVhdqiGSPT------YAADLADAILELIERNSLTGIyH 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903405 310 LGNPEEHTILEFAQLIKNLVGS-GSEIQFLSEAQDDPQKRKP-----DIKKAKLMLGWEPvVPLEEGLN 372
Cdd:cd05254   213 LSNSGPISKYEFAKLIADALGLpDVEIKPITSSEYPLPARRPansslDCSKLEELGGIKP-PDWKEALR 280
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
78-378 2.81e-13

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: 70.01  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVvdnffTGRKRNVEHWIGHENFELINHDVVEPLYI-----EVDQIYHLASPASP 152
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRA-----LVRSGSDAVLLDGLPVEVVEGDLTDAASLaaamkGCDRVFHLAAFTSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 153 ----PNYMYnpiktlKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEvhPQSEDYWGHVNPIGPRACYDEGKRVAET 227
Cdd:cd05228    76 wakdRKELY------RTNVEGTRNVLDAALEAGVrRVVHTSSIAALGGPP--DGRIDETTPWNERPFPNDYYRSKLLAEL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 228 MCYAYMKQ--EGVEVRVARIfntFGPRMHMND--GRVVSNFILQALQGEPltvyGSGSqtrAFQYVSDLVNGLVALMNSn 303
Cdd:cd05228   148 EVLEAAAEglDVVIVNPSAV---FGPGDEGPTstGLDVLDYLNGKLPAYP----PGGT---SFVDVRDVAEGHIAAMEK- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 304 vsspvnlGNPEEHTIL--------EFAQLIKNLVGSGSE-----------IQFLSEAQDDPQKRKP-------------- 350
Cdd:cd05228   217 -------GRRGERYILggenlsfkQLFETLAEITGVKPPrrtippwllkaVAALSELKARLTGKPPlltprtarvlrrny 289
                         330       340       350
                  ....*....|....*....|....*....|
gi 1046903405 351 --DIKKAKLMLGWEPvVPLEEGLNKAIHYF 378
Cdd:cd05228   290 lySSDKARRELGYSP-RPLEEALRDTLAWL 318
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
77-375 5.57e-13

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 68.62  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTvvdnfFTGRKRnvehwighenFELINHDVVEPLYIEV--DQIYHLASpasppn 154
Cdd:COG1091     1 RILVTGANGQLGRALVRLLAERGYEVV-----ALDRSE----------LDITDPEAVAALLEEVrpDVVINAAA------ 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 155 ymY--------NPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVY-GDPEvHPQSEDywGHVNPIGPracYDEGK--- 222
Cdd:COG1091    60 --YtavdkaesEPELAYAVNATGPANLAEACAELGARLIHISTDYVFdGTKG-TPYTED--DPPNPLNV---YGRSKlag 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 223 --RVAETMCYAYMkqegveVRVARIFNTFGprmhmndgrvvSNFILQAL----QGEPLTV----YGSGSqtrafqYVSDL 292
Cdd:COG1091   132 eqAVRAAGPRHLI------LRTSWVYGPHG-----------KNFVKTMLrllkEGEELRVvddqIGSPT------YAADL 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 293 VNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQ-FLSEAQDDPQKRkP-----DIKKAKLMLGWEPvVP 366
Cdd:COG1091   189 ARAILALLEKDLSGIYHLTGSGETSWYEFARAIAELAGLDALVEpITTAEYPTPAKR-PansvlDNSKLEATLGIKP-PD 266

                  ....*....
gi 1046903405 367 LEEGLNKAI 375
Cdd:COG1091   267 WREALAELL 275
PLN02572 PLN02572
UDP-sulfoquinovose synthase
74-377 9.24e-13

UDP-sulfoquinovose synthase


Pssm-ID: 215310 [Multi-domain]  Cd Length: 442  Bit Score: 69.44  E-value: 9.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  74 DRKRILITGGAGFVG----SHLTDKlmmdGHEVTVVDNFFtgrKRNVEHWIG----------HE-----------NFELI 128
Cdd:PLN02572   46 KKKKVMVIGGDGYCGwataLHLSKR----GYEVAIVDNLC---RRLFDHQLGldsltpiasiHErvrrwkevsgkEIELY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 129 NHDVVEPLYI-------EVDQIYHLASPASPPNYMYNPIK---TLKTNTIGTLNMLGLAK--RVGARLLLASTSEVYGDP 196
Cdd:PLN02572  119 VGDICDFEFLseafksfEPDAVVHFGEQRSAPYSMIDRSRavfTQHNNVIGTLNVLFAIKefAPDCHLVKLGTMGEYGTP 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 197 EV----------HPQSEDYWGHvnPIGPRACYDEGKRVAETMCYAYMKQEGV---EVRVARIFNTFGPRMHMND------ 257
Cdd:PLN02572  199 NIdieegyititHNGRTDTLPY--PKQASSFYHLSKVHDSHNIAFTCKAWGIratDLNQGVVYGVRTDETMMDEelinrl 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 258 ------GRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGL-VALMNSNVSSPVNLGN--PEEHTILEFAQLIKNL 328
Cdd:PLN02572  277 dydgvfGTALNRFCVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIeIAIANPAKPGEFRVFNqfTEQFSVNELAKLVTKA 356
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903405 329 ---VGSGSEIQFLSEAQDDPQKRKPDIKKAKLM-LGWEPVVP----LEEGLNKAIHY 377
Cdd:PLN02572  357 gekLGLDVEVISVPNPRVEAEEHYYNAKHTKLCeLGLEPHLLsdslLDSLLNFAVKY 413
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
77-374 1.53e-11

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: 64.68  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTV-VDNFFTGRKRNVEHwighenfELINHDVVEPLYIEVDQIYHLASPASPPNY 155
Cdd:cd05232     1 KVLVTGANGFIGRALVDKLLSRGEEVRIaVRNAENAEPSVVLA-------ELPDIDSFTDLFLGVDAVVHLAARVHVMND 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPIKTL--KTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVH-PQSEDywghvNPIGPRACYDEGKRVAETMCYA 231
Cdd:cd05232    74 QGADPLSDyrKVNTELTRRLARAAARQGVkRFVFLSSVKVNGEGTVGaPFDET-----DPPAPQDAYGRSKLEAERALLE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 232 YMKQEGVEVRVARIFNTFGPRMHMNDGRVVsnfilQAL-QGEPLtVYGSGSQTRAFQYVSDLVNGLV-ALMNSNVSSPVN 309
Cdd:cd05232   149 LGASDGMEVVILRPPMVYGPGVRGNFARLM-----RLIdRGLPL-PPGAVKNRRSLVSLDNLVDAIYlCISLPKAANGTF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 310 L-GNPEEHTILEFAQLIKNLVGSGS-----EIQFLSEAQDDPQKRKP----------DIKKAKLMLGWEPVVPLEEGLNK 373
Cdd:cd05232   223 LvSDGPPVSTAELVDEIRRALGKPTrllpvPAGLLRFAAKLLGKRAViqrlfgslqyDPEKTQNELGWRPPISLEEGLQE 302

                  .
gi 1046903405 374 A 374
Cdd:cd05232   303 T 303
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
76-309 1.29e-10

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


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 61.22  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLmmdgHEVTVVDNFFTGRKRNVEhwighenfELinhdvvePLYI-EVDQIYHLASPASPPn 154
Cdd:cd05261     1 MKILITGAKGFIGKNLIARL----KEQKDDDIFFYDRESDES--------EL-------DDFLqGADFIFHLAGVNRPK- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 155 ymyNPIKTLKTNTIGTLNMLGLAKRVGAR--LLLASTSEVYGDpevhpqsedywghvNPigpracYDEGKRVAETMCYAY 232
Cdd:cd05261    61 ---DEAEFESGNVGLTERLLDALTRNGKKppILLSSSIQAALD--------------NP------YGKSKLAAEELLQEY 117
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903405 233 MKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRaFQYVSDLVNGLVALMNSNVSSPVN 309
Cdd:cd05261   118 ARETGAPVYIYRLPNVFGKWCRPNYNSAVATFCYNIARDLPIQINDPAAELT-LVYIDDVVDELIQLLEGAPTYSGG 193
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
78-325 1.90e-10

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


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 61.12  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVvdnfFTGRKRNVEH--WIGHENFELINHDVVEPlyieVDQIYHLASpASPPNY 155
Cdd:TIGR01777   1 ILITGGTGFIGRALTQRLTKRGHEVTI----LTRSPPPGANtkWEGYKPWAGEDADSLEG----ADAVINLAG-EPIADK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPI--KTLKTNTIGTLNMLGLA----KRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYD--EGKRVAEt 227
Cdd:TIGR01777  72 RWTEErkQEIRDSRIDTTRLLVEAiaaaEQKPKVFISASAVGYYGPSEDREYTEEDSPAGDDFLAELCRDweEAAQAAE- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 228 mcyaymkQEGVEVRVARIFNTFGPrmhmnDGRVVSNFIL--QALQGEPLtvyGSGSQTRAFQYVSDLVNG-LVALMNSNV 304
Cdd:TIGR01777 151 -------DLGTRVVLLRTGIVLGP-----KGGALAKMLLpfRLGLGGPL---GSGRQWFSWIHIEDLVQLiLFALENASV 215
                         250       260
                  ....*....|....*....|.
gi 1046903405 305 SSPVNLGNPEEHTILEFAQLI 325
Cdd:TIGR01777 216 SGPVNATAPEPVRNKEFAKAL 236
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
76-286 2.85e-10

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: 60.71  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLM-MDGHEVTVVDNFFTGR---KRNVEHWIGHENFELINHDVVEPLYI-------EVDQIY 144
Cdd:cd05237     3 KTILVTGGAGSIGSELVRQILkFGPKKLIVFDRDENKLhelVRELRSRFPHDKLRFIIGDVRDKERLrrafkerGPDIVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 145 HLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVG-ARLLLASTsevygDPEVHPqsedywghVNPIGpracydEGKR 223
Cdd:cd05237    83 HAAALKHVPSMEDNPEEAIKTNVLGTKNVIDAAIENGvEKFVCIST-----DKAVNP--------VNVMG------ATKR 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903405 224 VAETMCYAYMKQEG-VEVRVARIFNTFGPRmhmndGRVVSNFILQALQGEPLTVYGSGsQTRAF 286
Cdd:cd05237   144 VAEKLLLAKNEYSSsTKFSTVRFGNVLGSR-----GSVLPLFKKQIKKGGPLTVTDPD-MTRFF 201
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
78-371 3.05e-10

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


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 60.80  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVVDnfftgrkRNVEHWIGHENFELINHDVVEPLYIE-----VDQIYHLASPAS- 151
Cdd:cd05229     2 AHVLGASGPIGREVARELRRRGWDVRLVS-------RSGSKLAWLPGVEIVAADAMDASSVIaaargADVIYHCANPAYt 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 ------PPnymynpiktLKTNTIGTlnmlglAKRVGARLLLASTSEVYGDPEVHPQSEDYwgHVNPIGpracyDEGK-RV 224
Cdd:cd05229    75 rweelfPP---------LMENVVAA------AEANGAKLVLPGNVYMYGPQAGSPITEDT--PFQPTT-----RKGRiRA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 225 A-ETMCYAYMKQEGVEVRVARIFNTFGPrmhmndgRVVSNF----ILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVAL 299
Cdd:cd05229   133 EmEERLLAAHAKGDIRALIVRAPDFYGP-------GAINSWlgaaLFAILQGKTAVFPGNLDTPHEWTYLPDVARALVTL 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 300 MNSNVSS--PVNLGNPEEHTILEFAQLIKNLVG---------------SGSEIQFLSEAQD-DPQKRKP---DIKKAKLM 358
Cdd:cd05229   206 AEEPDAFgeAWHLPGAGAITTRELIAIAARAAGrppkvrvipkwtlrlAGLFDPLMREIVEmMYLWEEPfilDSSKLEAT 285
                         330
                  ....*....|...
gi 1046903405 359 LGWEPVVPLEEGL 371
Cdd:cd05229   286 FGEIPHTPLDEAI 298
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
78-197 1.86e-09

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


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 58.15  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVVD---NFFTGRKRNVEHWIGHENFELINHDVVEP-----------LYIEVDQI 143
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLENGFKVLVLVrseSLGEAHERIEEAGLEADRVRVLEGDLTQPnlglsaaasreLAGKVDHV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903405 144 YHLA---SPASPPNYMYnpiktlKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPE 197
Cdd:cd05263    81 IHCAasyDFQAPNEDAW------RTNIDGTEHVLELAARLDIqRFHYVSTAYVAGNRE 132
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
77-325 1.37e-08

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. 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: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 55.70  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVVdnfftGRKRNVEHWigheNFELINHDVVEPLYIE---VDQIYHLASpASPP 153
Cdd:cd05242     1 KIVITGGTGFIGRALTRRLTAAGHEVVVL-----SRRPGKAEG----LAEVITWDGLSLGPWElpgADAVINLAG-EPIA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 154 NYMYNPI--KTLKTNTIGTLNMLGLA-KRVGAR---LLLASTSEVYGDPEVHPQSEDYWGhvnpigpracydeGKRVAET 227
Cdd:cd05242    71 CRRWTEAnkKEILSSRIESTRVLVEAiANAPAPpkvLISASAVGYYGHSGDEVLTENSPS-------------GKDFLAE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 228 MCYAYMK------QEGVEVRVARIfntfgprmhmndGRVVSNF--ILQALQ-------GEPLtvyGSGSQTRAFQYVSDL 292
Cdd:cd05242   138 VCKAWEKaaqpasELGTRVVILRT------------GVVLGPDggALPKMLlpfrlglGGPL---GSGRQWMSWIHIDDL 202
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1046903405 293 VNGLV-ALMNSNVSSPVNLGNPEEHTILEFAQLI 325
Cdd:cd05242   203 VRLIEfAIENPDLSGPVNAVAPNPVTNAEFTKAL 236
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
76-244 1.97e-08

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


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 54.83  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGH-EVTVV---DNFFTGRKR---NVEHW-IGHENF----ELINHDVVEP-------- 135
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDaRVYCLvraSDEAAARERleaLLERYgLWLELDasrvVVVAGDLTQPrlglseae 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 136 ---LYIEVDQIYHLASpasppnyMYN---PIKTLK-TNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDPEVHPQSEDYWg 207
Cdd:COG3320    81 fqeLAEEVDAIVHLAA-------LVNlvaPYSELRaVNVLGTREVLRLAATGRLkPFHYVSTIAVAGPADRSGVFEEDD- 152
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1046903405 208 HVNPIGPRACYDEGKRVAETMCYAYMKQeGVEVRVAR 244
Cdd:COG3320   153 LDEGQGFANGYEQSKWVAEKLVREARER-GLPVTIYR 188
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
80-212 4.83e-08

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


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 53.77  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  80 ITGGAGFVGSHLTDKLMMDGHEVTVV------DNFFTGRKRNVEHWIGHENFELINH-----------DVVEP------- 135
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIyllvraKDGESALERLRQELEKYPLFDALLKealerivpvagDLSEPnlglsee 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 136 ----LYIEVDQIYHLASPAsppNYMYnPIKTLK-TNTIGTLNMLGLAKRVGAR--LLLASTSEVYGDPEVHPQSEDYWGH 208
Cdd:pfam07993  81 dfqeLAEEVDVIIHSAATV---NFVE-PYDDARaVNVLGTREVLRLAKQGKQLkpFHHVSTAYVNGERGGLVEEKPYPEG 156

                  ....
gi 1046903405 209 VNPI 212
Cdd:pfam07993 157 EDDM 160
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
78-324 6.67e-08

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


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 53.53  E-value: 6.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKL--MMDGHEVTVVDnfftgRKRNVEHWIGHE--NFELINHDVVEPLYI-EVDQIYHLASPASP 152
Cdd:cd05240     1 ILVTGAAGGLGRLLARRLaaSPRVIGVDGLD-----RRRPPGSPPKVEyvRLDIRDPAAADVFRErEADAVVHLAFILDP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 153 PNymyNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYG----DPEVHpqSEDYWGHVNpigPRACYDEGKRVAET 227
Cdd:cd05240    76 PR---DGAERHRINVDGTQNVLDACAAAGVpRVVVTSSVAVYGahpdNPAPL--TEDAPLRGS---PEFAYSRDKAEVEQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 228 MCYAYMK-QEGVEVRVARIFNTFGPRMhmndgrvvSNFILQALQGEPLTV-YGSGSqtrAFQYV--SDLVNGLVALMNSN 303
Cdd:cd05240   148 LLAEFRRrHPELNVTVLRPATILGPGT--------RNTTRDFLSPRRLPVpGGFDP---PFQFLheDDVARALVLAVRAG 216
                         250       260
                  ....*....|....*....|.
gi 1046903405 304 VSSPVNLGNPEEHTILEFAQL 324
Cdd:cd05240   217 ATGIFNVAGDGPVPLSLVLAL 237
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
77-228 7.25e-08

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: 53.54  E-value: 7.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHevtvvdnfftgrkrnvehwigheNFELINHDVVEPLY---------IEVDQ----- 142
Cdd:cd05238     2 KVLITGASGFVGQRLAERLLSDVP-----------------------NERLILIDVVSPKApsgaprvtqIAGDLavpal 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 143 -----------IYHLASPASPPNYMyNPIKTLKTNTIGTLNMLGLAKRVGA--RLLLASTSEVYGDPEVHPQSEDYwghv 209
Cdd:cd05238    59 iealangrpdvVFHLAAIVSGGAEA-DFDLGYRVNVDGTRNLLEALRKNGPkpRFVFTSSLAVYGLPLPNPVTDHT---- 133
                         170
                  ....*....|....*....
gi 1046903405 210 nPIGPRACYDEGKRVAETM 228
Cdd:cd05238   134 -ALDPASSYGAQKAMCELL 151
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
79-300 1.76e-07

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


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 52.37  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  79 LITGGAGFVGSHLTDKLMMDGH--EVTVVDNFFTGRKRNVEHWIGHENFelINHDVVEPLYIE-----VDQIYHLASpAS 151
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGElkEVRVFDLRESPELLEDFSKSNVIKY--IQGDVTDKDDLDnalegVDVVIHTAS-AV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 152 PPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLL-ASTSEV-----YGDPEVHPQSEDYWghvnPIGPRACYDEGKRVA 225
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVyTSSAEVvgpnsYGQPILNGDEETPY----ESTHQDAYPRSKAIA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 226 ETMCyayMKQEGVEVRVARIFNT--------FGPRmhmndGRVVSNFILQALQ-GEPLTVYGSGSQTRAFQYVsdlvnGL 296
Cdd:pfam01073 154 EKLV---LKANGRPLKNGGRLYTcalrpagiYGEG-----DRLLVPFIVNLAKlGLAKFKTGDDNNLSDRVYV-----GN 220

                  ....
gi 1046903405 297 VALM 300
Cdd:pfam01073 221 VAWA 224
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
77-105 1.86e-07

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


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 52.37  E-value: 1.86e-07
                          10        20
                  ....*....|....*....|....*....
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVV 105
Cdd:COG1090     1 KILITGGTGFIGSALVAALLARGHEVVVL 29
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
78-196 2.19e-07

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 50.48  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVVD------NFFTGRKRNVEHWighenfELINHDVVEPLYIEVDQIYHLaspAS 151
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLLVrntkrlSKEDQEPVAVVEG------DLRDLDSLSDAVQGVDVVIHL---AG 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046903405 152 PPNYMYNPIktlKTNTIGTLNMLGLAKRVGA-RLLLASTSEVYGDP 196
Cdd:cd05226    72 APRDTRDFC---EVDVEGTRNVLEAAKEAGVkHFIFISSLGAYGDL 114
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
77-360 2.70e-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: 51.89  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEV--TV--------VDNFFTGRKRNvehwighENFELInhdVVEPL-----YIE-- 139
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKAGYKVrgTVrslsksakLKALLKAAGYN-------DRLEFV---IVDDLtapnaWDEal 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 140 --VDQIYHLASPASPPNYMYNPIkTLKTNTIGTLNMLGLAKRVGA--RLLLASTSEVYGDPEVHPQS----EDYWGHVN- 210
Cdd:cd05227    71 kgVDYVIHVASPFPFTGPDAEDD-VIDPAVEGTLNVLEAAKAAGSvkRVVLTSSVAAVGDPTAEDPGkvftEEDWNDLTi 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 211 -PIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIfN---TFGPRMHMNDGRVVSNFILQALQGEPltvyGSGSQTRAF 286
Cdd:cd05227   150 sKSNGLDAYIASKTLAEKAAWEFVKENKPKFELITI-NpgyVLGPSLLADELNSSNELINKLLDGKL----PAIPPNLPF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903405 287 QYVS--DLVNG-LVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLG 360
Cdd:cd05227   225 GYVDvrDVADAhVRALESPEAAGQRFIVSAGPFSFQEIADLLREEFPQLTAPFPAPNPLMLSILVKFDNRKSEELLG 301
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
81-361 2.22e-06

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


Pssm-ID: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 49.11  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  81 TGGAGFVGSHLTDKLMMDGHEV-TVVDNffTGRKRNVEHWIG----HENFELINHDVVEPLYIE-----VDQIYHLASP- 149
Cdd:cd08958     4 TGASGFIGSWLVKRLLQRGYTVrATVRD--PGDEKKVAHLLElegaKERLKLFKADLLDYGSFDaaidgCDGVFHVASPv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 150 ----ASPPNYMYNPikTLKtntiGTLNML------GLAKRVgarLLLASTSEVYGDPEVHPQS---EDYWGHVNPIGPRA 216
Cdd:cd08958    82 dfdsEDPEEEMIEP--AVK----GTLNVLeacakaKSVKRV---VFTSSVAAVVWNPNRGEGKvvdESCWSDLDFCKKTK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 217 C-YDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGP--RMHMNDGrvvSNFILQALQGEPLTvYGSGSqtraFQYVS--D 291
Cdd:cd08958   153 LwYALSKTLAEKAAWEFAEENGLDLVTVNPSLVVGPflQPSLNSS---SQLILSLLKGNAEM-YQNGS----LALVHvdD 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903405 292 LVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVgsgSEIQFLSE-AQDDPQKRKPDIKKAKLM-LGW 361
Cdd:cd08958   225 VADAHILLYEKPSASGRYICSSHVVTRPELAALLAKKY---PQYNIPTKfEDDQPGVARVKLSSKKLKdLGF 293
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
77-244 2.64e-06

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: 48.85  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLM-MDGHEVTVVDNFftgRKRNVEHWIgHENFELIN-------HDVVEPLyiEVDQIYHLAS 148
Cdd:cd05272     1 RILITGGLGQIGSELAKLLRkRYGKDNVIASDI---RKPPAHVVL-SGPFEYLDvldfkslEEIVVNH--KITWIIHLAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 149 PASPPNYMyNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGD-------PEVHPQSedywghvnpigPRACYDEG 221
Cdd:cd05272    75 LLSAVGEK-NPPLAWDVNMNGLHNVLELAREHNLRIFVPSTIGAFGPttprnntPDDTIQR-----------PRTIYGVS 142
                         170       180
                  ....*....|....*....|...
gi 1046903405 222 KRVAETMCYAYMKQEGVEVRVAR 244
Cdd:cd05272   143 KVAAELLGEYYHHKFGVDFRSLR 165
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
77-325 3.33e-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: 47.53  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVV----DNFFTGRKRNVEHWIGhenfELINHDVVEPLYIEVDQIYHLASPASP 152
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVRALvrdpEKAAALAAAGVEVVQG----DLDDPESLAAALAGVDAVFLLVPSGPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 153 PNYmynpiktlKTNTIGTLNMLGLAKRVGARLLLASTSevygdpeVHPQSEDYWGHVnpigpracydEGKRVAEtmcyAY 232
Cdd:COG0702    77 GDF--------AVDVEGARNLADAAKAAGVKRIVYLSA-------LGADRDSPSPYL----------RAKAAVE----EA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 233 MKQEGVEVRVARifntfgprmhmnDGRVVSNFILQALQ-GEPLTVYGSGSQTRaFQYVS--DLVNGLVALMNS--NVSSP 307
Cdd:COG0702   128 LRASGLPYTILR------------PGWFMGNLLGFFERlRERGVLPLPAGDGR-VQPIAvrDVAEAAAAALTDpgHAGRT 194
                         250
                  ....*....|....*...
gi 1046903405 308 VNLGNPEEHTILEFAQLI 325
Cdd:COG0702   195 YELGGPEALTYAELAAIL 212
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
77-336 8.95e-06

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


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 46.88  E-value: 8.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVV----------------DNFFTGRKRNVEHWIGhENFELINHDVVEP----- 135
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELLKRKNVSKIYclvrakdeeaalerliDNLKEYGLNLWDELEL-SRIKVVVGDLSKPnlgls 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 136 ------LYIEVDQIYHLASPAsppNYMYNPIKTLKTNTIGTLNMLGLA-KRVGARLLLASTSEVYGDPEVHPQSEDYWGH 208
Cdd:cd05235    80 dddyqeLAEEVDVIIHNGANV---NWVYPYEELKPANVLGTKELLKLAaTGKLKPLHFVSTLSVFSAEEYNALDDEESDD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 209 --VNPIGPRACYDEGKRVAETMCYAYMKqEGVEVRVARIFNTFGprmHMNDGRV-VSNFILQALQGEPLTVYGSGSQTRA 285
Cdd:cd05235   157 mlESQNGLPNGYIQSKWVAEKLLREAAN-RGLPVAIIRPGNIFG---DSETGIGnTDDFFWRLLKGCLQLGIYPISGAPL 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1046903405 286 FQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQ 336
Cdd:cd05235   233 DLSPVDWVARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYSIK 283
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
78-276 4.62e-05

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein mannosyl-transferase and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 44.81  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLM-MDGHEVTVVD----NFFTGRKRNVEHWIGHE-NFELINH--DVVEPLYIE-------VDQ 142
Cdd:pfam02719   1 VLVTGGGGSIGSELCRQILkFNPKKIILFSrdelKLYEIRQELREKFNDPKlRFFIVPVigDVRDRERLErameqygVDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 143 IYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGA-RLLLASTsevygDPEVHPqsedywghVNPIGpracydEG 221
Cdd:pfam02719  81 VFHAAAYKHVPLVEYNPMEAIKTNVLGTENVADAAIEAGVkKFVLIST-----DKAVNP--------TNVMG------AT 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903405 222 KRVAETMCYA---YMKQEGVEVRVARIFNTFGPRmhmndGRVVSNFILQALQGEPLTV 276
Cdd:pfam02719 142 KRLAEKLFQAanrESGSGGTRFSVVRFGNVLGSR-----GSVIPLFKKQIAEGGPVTV 194
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
76-254 1.26e-04

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 43.85  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRnVEHWI----GHENFELINHDVVEPLYIE-----VDQIYHL 146
Cdd:PLN02986    6 KLVCVTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKK-TEHLLaldgAKERLKLFKADLLEESSFEqaiegCDAVFHT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 147 ASPA-----SPPNYMYNPikTLKtntiGTLNMLGLAKRVGA--RLLLASTSE--VYGDPEVHPQ---SEDYWGHvnpigP 214
Cdd:PLN02986   85 ASPVfftvkDPQTELIDP--ALK----GTINVLNTCKETPSvkRVILTSSTAavLFRQPPIEANdvvDETFFSD-----P 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1046903405 215 RAC------YDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMH 254
Cdd:PLN02986  154 SLCretknwYPLSKILAENAAWEFAKDNGIDMVVLNPGFICGPLLQ 199
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
77-105 4.50e-04

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 41.00  E-value: 4.50e-04
                          10        20
                  ....*....|....*....|....*....
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVTVV 105
Cdd:COG2910     1 KIAVIGATGRVGSLIVREALARGHEVTAL 29
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
77-103 5.59e-04

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: 41.57  E-value: 5.59e-04
                          10        20
                  ....*....|....*....|....*..
gi 1046903405  77 RILITGGAGFVGSHLTDKLMMDGHEVT 103
Cdd:cd05262     2 KVFVTGATGFIGSAVVRELVAAGHEVV 28
rfaD PRK11150
ADP-L-glycero-D-mannoheptose-6-epimerase; Provisional
78-333 6.53e-04

ADP-L-glycero-D-mannoheptose-6-epimerase; Provisional


Pssm-ID: 182998 [Multi-domain]  Cd Length: 308  Bit Score: 41.23  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGH-EVTVVDNFFTGRK------RNVEHWIGHENFelINHDVVEPLYIEVDQIYHLASPA 150
Cdd:PRK11150    2 IIVTGGAGFIGSNIVKALNDKGItDILVVDNLKDGTKfvnlvdLDIADYMDKEDF--LAQIMAGDDFGDIEAIFHEGACS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 151 SPP----------NYMYNpiKTLktntigtlnmLGLAKRVGARLLLASTSEVYGDP-EVHPQSEDYWGHVNPIG-PRACY 218
Cdd:PRK11150   80 STTewdgkymmdnNYQYS--KEL----------LHYCLEREIPFLYASSAATYGGRtDDFIEEREYEKPLNVYGySKFLF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 219 DEGKRvaetmcyAYMKQEGVEVRVARIFNTFGPR-----------MHMNDgrvvsnfilQALQGE-PLTVYGSGSQTRAF 286
Cdd:PRK11150  148 DEYVR-------QILPEANSQICGFRYFNVYGPReghkgsmasvaFHLNN---------QLNNGEnPKLFEGSENFKRDF 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046903405 287 QYVSDlvnglVALMN-----SNVSSPVNLGNPEEHTILEFAQLIKNLVGSGS 333
Cdd:PRK11150  212 VYVGD-----VAAVNlwfweNGVSGIFNCGTGRAESFQAVADAVLAYHKKGE 258
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
78-197 8.93e-04

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: 41.06  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEV--TVVDnfftGRKRNVEHWIG-----HENFEL-INHDVVEPLYIEV----DQIYH 145
Cdd:cd05193     1 VLVTGASGFVASHVVEQLLERGYKVraTVRD----PSKVKKVNHLLdldakPGRLELaVADLTDEQSFDEVikgcAGVFH 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903405 146 LASP----ASPPNYMYNPiktlktNTIGTLNMLGLAKRVGA--RLLLASTSEVYGDPE 197
Cdd:cd05193    77 VATPvsfsSKDPNEVIKP------AIGGTLNALKAAAAAKSvkRFVLTSSAGSVLIPK 128
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
68-107 1.41e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.44  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1046903405  68 KFLSEKDRKRILITGgAGFVGSHLTDKLMMDGHEVTVVDN 107
Cdd:COG0569    88 ERGIKKLKMHVIIIG-AGRVGRSLARELEEEGHDVVVIDK 126
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
78-229 2.27e-03

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 39.71  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVV-----DNFFTGRKRNVE----HWIGHENF-----ELINHDVVEP-------- 135
Cdd:TIGR01746   2 VLLTGATGFLGAYLLEELLRRSTRAKVIclvraDSEEHAMERLREalrsYRLWHENLameriEVVAGDLSKPrlglsdae 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405 136 ---LYIEVDQIYHLASPAsppNYMYnPIKTLK-TNTIGTLNMLGLAKRVGARLL-LASTSEVYGDPEVHPQS-EDYWGHV 209
Cdd:TIGR01746  82 werLAENVDTIVHNGALV---NHVY-PYSELRgANVLGTVEVLRLAASGRAKPLhYVSTISVGAAIDLSTGVtEDDATVT 157
                         170       180
                  ....*....|....*....|
gi 1046903405 210 NPIGPRACYDEGKRVAETMC 229
Cdd:TIGR01746 158 PYPGLAGGYTQSKWVAELLV 177
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
76-105 2.40e-03

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: 39.54  E-value: 2.40e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1046903405  76 KRILITGGAGFVGSHLTDKLMMDGHEVTVV 105
Cdd:cd05271     1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVP 30
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
78-195 4.97e-03

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


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 38.46  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGgAGFVGSHLTDKLMMDGHEVTVVdnffTGRKRNVEHWIGHENFELInHDVVEPLYIEVDQI--YHLASPASPPNY 155
Cdd:cd05266     1 VLILG-CGYLGQRLARQLLAQGWQVTGT----TRSPEKLAADRPAGVTPLA-ADLTQPGLLADVDHlvISLPPPAGSYRG 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046903405 156 MYNPIKTLktnTIGTLNMLGLAKRVGarlLLASTSeVYGD 195
Cdd:cd05266    75 GYDPGLRA---LLDALAQLPAVQRVI---YLSSTG-VYGD 107
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
78-155 5.60e-03

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 38.08  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903405  78 ILITGGAGFVGSHLTDKLMMDGHEVTVV--DNFFTG--RKRNVEHWIGhenfELINHDVVEPLYIEVDQIYHLASPASPP 153
Cdd:cd05231     1 ILVTGATGRIGSKVATTLLEAGRPVRALvrSDERAAalAARGAEVVVG----DLDDPAVLAAALAGVDAVFFLAPPAPTA 76

                  ..
gi 1046903405 154 NY 155
Cdd:cd05231    77 DA 78
trkA PRK09496
Trk system potassium transporter TrkA;
77-107 7.70e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 38.18  E-value: 7.70e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1046903405  77 RILITGgAGFVGSHLTDKLMMDGHEVTVVDN 107
Cdd:PRK09496    2 KIIIVG-AGQVGYTLAENLSGENNDVTVIDT 31
 
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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