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Conserved domains on  [gi|302845927|ref|XP_002954501|]
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uncharacterized protein VOLCADRAFT_109932 [Volvox carteri f. nagariensis]

Protein Classification

UDP-sulfoquinovose synthase( domain architecture ID 10791412)

chloroplastic UDP-sulfoquinovose synthase converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02572 PLN02572
UDP-sulfoquinovose synthase
 33-476 0e+00

UDP-sulfoquinovose synthase


:

Pssm-ID: 215310 [Multi-domain]  Cd Length: 442  Bit Score: 850.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  33 VCALRASVGRKAASAAQvasravsvkvnAIATIERPAGPAPTSSGGGAGTRVMIIGGDGYCGWATALHLSARGYEVCIVD 112
Cdd:PLN02572  10 STSSKAFTSASPASAQS-----------TPAVTELATPSAPGSSSSSKKKKVMVIGGDGYCGWATALHLSKRGYEVAIVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 113 NLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEFLSQAFTSFQPEHVVHFGEQRSAPYSMIDRQK 192
Cdd:PLN02572  79 NLCRRLFDHQLGLDSLTPIASIHERVRRWKEVSGKEIELYVGDICDFEFLSEAFKSFEPDAVVHFGEQRSAPYSMIDRSR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 193 AVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEGYLTVTHNGRTDTLPYPKQGNSFYHLSKIHDSTN 272
Cdd:PLN02572 159 AVFTQHNNVIGTLNVLFAIKEFAPDCHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 273 MLFTCKAWKVAATDLNQGVVYGVRTEETMADPMLINRYDYDGIFGTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTV 352
Cdd:PLN02572 239 IAFTCKAWGIRATDLNQGVVYGVRTDETMMDEELINRLDYDGVFGTALNRFCVQAAVGHPLTVYGKGGQTRGFLDIRDTV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 353 RCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQNVPNPRVEAEEHYYNAKHTKLVELGLQPHLL 432
Cdd:PLN02572 319 RCIEIAIANPAKPGEFRVFNQFTEQFSVNELAKLVTKAGEKLGLDVEVISVPNPRVEAEEHYYNAKHTKLCELGLEPHLL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 302845927 433 ADSMIDSLLDFAVQYRDRVRMELIKPAVDWRKTGVKVNTMGAAV 476
Cdd:PLN02572 399 SDSLLDSLLNFAVKYKDRVDTTLILPAVSWKKIGVKPKTIAAKA 442
 
Name Accession Description Interval E-value
PLN02572 PLN02572
UDP-sulfoquinovose synthase
 33-476 0e+00

UDP-sulfoquinovose synthase


Pssm-ID: 215310 [Multi-domain]  Cd Length: 442  Bit Score: 850.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  33 VCALRASVGRKAASAAQvasravsvkvnAIATIERPAGPAPTSSGGGAGTRVMIIGGDGYCGWATALHLSARGYEVCIVD 112
Cdd:PLN02572  10 STSSKAFTSASPASAQS-----------TPAVTELATPSAPGSSSSSKKKKVMVIGGDGYCGWATALHLSKRGYEVAIVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 113 NLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEFLSQAFTSFQPEHVVHFGEQRSAPYSMIDRQK 192
Cdd:PLN02572  79 NLCRRLFDHQLGLDSLTPIASIHERVRRWKEVSGKEIELYVGDICDFEFLSEAFKSFEPDAVVHFGEQRSAPYSMIDRSR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 193 AVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEGYLTVTHNGRTDTLPYPKQGNSFYHLSKIHDSTN 272
Cdd:PLN02572 159 AVFTQHNNVIGTLNVLFAIKEFAPDCHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 273 MLFTCKAWKVAATDLNQGVVYGVRTEETMADPMLINRYDYDGIFGTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTV 352
Cdd:PLN02572 239 IAFTCKAWGIRATDLNQGVVYGVRTDETMMDEELINRLDYDGVFGTALNRFCVQAAVGHPLTVYGKGGQTRGFLDIRDTV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 353 RCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQNVPNPRVEAEEHYYNAKHTKLVELGLQPHLL 432
Cdd:PLN02572 319 RCIEIAIANPAKPGEFRVFNQFTEQFSVNELAKLVTKAGEKLGLDVEVISVPNPRVEAEEHYYNAKHTKLCELGLEPHLL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 302845927 433 ADSMIDSLLDFAVQYRDRVRMELIKPAVDWRKTGVKVNTMGAAV 476
Cdd:PLN02572 399 SDSLLDSLLNFAVKYKDRVDTTLILPAVSWKKIGVKPKTIAAKA 442
SQD1_like_SDR_e cd05255
UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) ...
 82-463 0e+00

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: 720.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  82 TRVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEF 161
Cdd:cd05255    1 MKVLILGGDGYCGWPTALHLSKRGHEVCIVDNLVRRRIDVELGLESLTPIASIHERLRAWKELTGKTIEFYVGDACDYEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 162 LSQAFTSFQPEHVVHFGEQRSAPYSMIDRQKAVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEGYL 241
Cdd:cd05255   81 LAELLASHEPDAVVHFAEQRSAPYSMIDREHANYTQHNNVIGTLNLLFAIKEFDPDCHLVKLGTMGEYGTPNIDIPEGYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 242 TVTHNGRTDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEETMADPMLINRYDYDGIFGTALN 321
Cdd:cd05255  161 TIEHNGRRDTLPYPKQAGSWYHLSKVHDSHNIMFACKAWGIRITDLNQGVVYGTKTEETEADERLINRFDYDGVFGTVLN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 322 RFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQ 401
Cdd:cd05255  241 RFCVQAAIGHPLTVYGKGGQTRGFISIRDTVQCLELALENPAKAGEYRVFNQFTEQFSVGELAEMVAEAGSKLGLDVKVE 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302845927 402 NVPNPRVEAEEHYYNAKHTKLVELGLQPHLLADSMIDSLLDFAVQYRDRVRMELIKPAVDWR 463
Cdd:cd05255  321 HLPNPRVEAEEHYYNAKNTKLLDLGLEPHYLSESLLDSILNFAVKYADRVDEKRILPKVLWK 382
UDPsulfquin_syn NF041015
UDP-sulfoquinovose synthase;
83-463 3.13e-180

UDP-sulfoquinovose synthase;


Pssm-ID: 468944 [Multi-domain]  Cd Length: 384  Bit Score: 509.53  E-value: 3.13e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEFL 162
Cdd:NF041015   2 KVLILGIDGYLGWPLALRLAKRGHEVIGIDNLSTRRAVEEVGSDSALPIPSMEERVRAAKEILGVDIKFYEGDVTDYDFL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 163 SQAFTSFQPEHVVHFGEQRSAPYSMIDRQKAVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEG-YL 241
Cdd:NF041015  82 KDVIKKFKPDAIVHFAEQRSAPYSMIDLEHAVYTMINNIIGTLNLIYAVKEIVPDIHILKMGTMGEYGTPNFDIPESaFV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 242 TVTHNGRTDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEEtMADPMLINRYDYDGIFGTALN 321
Cdd:NF041015 162 EAEINGKKDRIPFPRWAGSWYHWSKVHDSYNLMFANKLWGLTITDIMQGPVYGTRTEE-IIDEGLRTRFDFDEVWGTVVN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 322 RFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQ 401
Cdd:NF041015 241 RFCAEAVLGLPLTPYGKGGQTRGFLSLEDSIQALTLLLENPPEQGEYRVVNQFDEIYSVNEIAELVKKAGEELGLDVEIK 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302845927 402 NVPNPRVEAEEHYYNAKHTKLVELGLQPHLLADSMIDSLLDFAVQYRDRV--RMELIKPAVDWR 463
Cdd:NF041015 321 HVDNPRVEKEEHYYNPERKVLPSLGFKPKRNLKEEVKIMLEDLIPYKDRLerFKEVIMPKTKWK 384
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
83-443 4.89e-39

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 143.20  E-value: 4.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLcrrqfdltlgldtltpiatiHDRVRKWAEVSGkyISLQIGDICDWEFL 162
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRS--------------------PPGAANLAALPG--VEFVRGDLRDPEAL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 163 SQAFtsFQPEHVVHFGEQRSAPYSMIDRqkavfTQTNNVVGTLNVLFAIKELKPDcHLVKLGTMGEYGTPNIDIEEgylt 242
Cdd:COG0451   59 AAAL--AGVDAVVHLAAPAGVGEEDPDE-----TLEVNVEGTLNLLEAARAAGVK-RFVYASSSSVYGDGEGPIDE---- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 243 vthngrtdtlPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTeetmadpmlinrydydgifGTALNR 322
Cdd:COG0451  127 ----------DTPLRPVSPYGASKLAAELLARAYARRYGLPVTILRPGNVYGPGD-------------------RGVLPR 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 323 FVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEmrVFNQFTEQ-FSVNQLAEIVnreGRKLGLDVVVq 401
Cdd:COG0451  178 LIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGG--VYNVGGGEpVTLRELAEAI---AEALGRPPEI- 251

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 302845927 402 NVPNPRVEAEEHYYNAKHTKlVELGLQPHLLADSMIDSLLDF 443
Cdd:COG0451  252 VYPARPGDVRPRRADNSKAR-RELGWRPRTSLEEGLRETVAW 292
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 84-372 3.69e-18

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: 83.50  E-value: 3.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927   84 VMIIGGDGYCGWATALHLSARGYEVCIVDNLCrrqfdltlgldtlTPIATIHDRVRKWAEvsgkyislqiGDICDWEFLS 163
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLT-------------SASNTARLADLRFVE----------GDLTDRDALE 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  164 QAFTSFQPEHVVHFGEQRSAPYSMIDrqkAVFTQTNNVVGTLNVLFAIKELKPDcHLVKLGTMGEYGTPN-IDIEEgylt 242
Cdd:pfam01370  58 KLLADVRPDAVIHLAAVGGVGASIED---PEDFIEANVLGTLNLLEAARKAGVK-RFLFASSSEVYGDGAeIPQEE---- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  243 vthngrtDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGvrteetmadpmlinRYDYDGIFGTALNR 322
Cdd:pfam01370 130 -------TTLTGPLAPNSPYAAAKLAGEWLVLAYAAAYGLRAVILRLFNVYG--------------PGDNEGFVSRVIPA 188

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 302845927  323 FVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEmrVFN 372
Cdd:pfam01370 189 LIRRILEGKPILLWGDGTQRRDFLYVDDVARAILLALEHGAVKGE--IYN 236
 
Name Accession Description Interval E-value
PLN02572 PLN02572
UDP-sulfoquinovose synthase
 33-476 0e+00

UDP-sulfoquinovose synthase


Pssm-ID: 215310 [Multi-domain]  Cd Length: 442  Bit Score: 850.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  33 VCALRASVGRKAASAAQvasravsvkvnAIATIERPAGPAPTSSGGGAGTRVMIIGGDGYCGWATALHLSARGYEVCIVD 112
Cdd:PLN02572  10 STSSKAFTSASPASAQS-----------TPAVTELATPSAPGSSSSSKKKKVMVIGGDGYCGWATALHLSKRGYEVAIVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 113 NLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEFLSQAFTSFQPEHVVHFGEQRSAPYSMIDRQK 192
Cdd:PLN02572  79 NLCRRLFDHQLGLDSLTPIASIHERVRRWKEVSGKEIELYVGDICDFEFLSEAFKSFEPDAVVHFGEQRSAPYSMIDRSR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 193 AVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEGYLTVTHNGRTDTLPYPKQGNSFYHLSKIHDSTN 272
Cdd:PLN02572 159 AVFTQHNNVIGTLNVLFAIKEFAPDCHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 273 MLFTCKAWKVAATDLNQGVVYGVRTEETMADPMLINRYDYDGIFGTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTV 352
Cdd:PLN02572 239 IAFTCKAWGIRATDLNQGVVYGVRTDETMMDEELINRLDYDGVFGTALNRFCVQAAVGHPLTVYGKGGQTRGFLDIRDTV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 353 RCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQNVPNPRVEAEEHYYNAKHTKLVELGLQPHLL 432
Cdd:PLN02572 319 RCIEIAIANPAKPGEFRVFNQFTEQFSVNELAKLVTKAGEKLGLDVEVISVPNPRVEAEEHYYNAKHTKLCELGLEPHLL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 302845927 433 ADSMIDSLLDFAVQYRDRVRMELIKPAVDWRKTGVKVNTMGAAV 476
Cdd:PLN02572 399 SDSLLDSLLNFAVKYKDRVDTTLILPAVSWKKIGVKPKTIAAKA 442
SQD1_like_SDR_e cd05255
UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) ...
 82-463 0e+00

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: 720.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  82 TRVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEF 161
Cdd:cd05255    1 MKVLILGGDGYCGWPTALHLSKRGHEVCIVDNLVRRRIDVELGLESLTPIASIHERLRAWKELTGKTIEFYVGDACDYEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 162 LSQAFTSFQPEHVVHFGEQRSAPYSMIDRQKAVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEGYL 241
Cdd:cd05255   81 LAELLASHEPDAVVHFAEQRSAPYSMIDREHANYTQHNNVIGTLNLLFAIKEFDPDCHLVKLGTMGEYGTPNIDIPEGYI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 242 TVTHNGRTDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEETMADPMLINRYDYDGIFGTALN 321
Cdd:cd05255  161 TIEHNGRRDTLPYPKQAGSWYHLSKVHDSHNIMFACKAWGIRITDLNQGVVYGTKTEETEADERLINRFDYDGVFGTVLN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 322 RFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQ 401
Cdd:cd05255  241 RFCVQAAIGHPLTVYGKGGQTRGFISIRDTVQCLELALENPAKAGEYRVFNQFTEQFSVGELAEMVAEAGSKLGLDVKVE 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302845927 402 NVPNPRVEAEEHYYNAKHTKLVELGLQPHLLADSMIDSLLDFAVQYRDRVRMELIKPAVDWR 463
Cdd:cd05255  321 HLPNPRVEAEEHYYNAKNTKLLDLGLEPHYLSESLLDSILNFAVKYADRVDEKRILPKVLWK 382
UDPsulfquin_syn NF041015
UDP-sulfoquinovose synthase;
83-463 3.13e-180

UDP-sulfoquinovose synthase;


Pssm-ID: 468944 [Multi-domain]  Cd Length: 384  Bit Score: 509.53  E-value: 3.13e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLTLGLDTLTPIATIHDRVRKWAEVSGKYISLQIGDICDWEFL 162
Cdd:NF041015   2 KVLILGIDGYLGWPLALRLAKRGHEVIGIDNLSTRRAVEEVGSDSALPIPSMEERVRAAKEILGVDIKFYEGDVTDYDFL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 163 SQAFTSFQPEHVVHFGEQRSAPYSMIDRQKAVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYGTPNIDIEEG-YL 241
Cdd:NF041015  82 KDVIKKFKPDAIVHFAEQRSAPYSMIDLEHAVYTMINNIIGTLNLIYAVKEIVPDIHILKMGTMGEYGTPNFDIPESaFV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 242 TVTHNGRTDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEEtMADPMLINRYDYDGIFGTALN 321
Cdd:NF041015 162 EAEINGKKDRIPFPRWAGSWYHWSKVHDSYNLMFANKLWGLTITDIMQGPVYGTRTEE-IIDEGLRTRFDFDEVWGTVVN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 322 RFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEMRVFNQFTEQFSVNQLAEIVNREGRKLGLDVVVQ 401
Cdd:NF041015 241 RFCAEAVLGLPLTPYGKGGQTRGFLSLEDSIQALTLLLENPPEQGEYRVVNQFDEIYSVNEIAELVKKAGEELGLDVEIK 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302845927 402 NVPNPRVEAEEHYYNAKHTKLVELGLQPHLLADSMIDSLLDFAVQYRDRV--RMELIKPAVDWR 463
Cdd:NF041015 321 HVDNPRVEKEEHYYNPERKVLPSLGFKPKRNLKEEVKIMLEDLIPYKDRLerFKEVIMPKTKWK 384
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
83-443 4.89e-39

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 143.20  E-value: 4.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLcrrqfdltlgldtltpiatiHDRVRKWAEVSGkyISLQIGDICDWEFL 162
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRS--------------------PPGAANLAALPG--VEFVRGDLRDPEAL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 163 SQAFtsFQPEHVVHFGEQRSAPYSMIDRqkavfTQTNNVVGTLNVLFAIKELKPDcHLVKLGTMGEYGTPNIDIEEgylt 242
Cdd:COG0451   59 AAAL--AGVDAVVHLAAPAGVGEEDPDE-----TLEVNVEGTLNLLEAARAAGVK-RFVYASSSSVYGDGEGPIDE---- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 243 vthngrtdtlPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTeetmadpmlinrydydgifGTALNR 322
Cdd:COG0451  127 ----------DTPLRPVSPYGASKLAAELLARAYARRYGLPVTILRPGNVYGPGD-------------------RGVLPR 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 323 FVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEmrVFNQFTEQ-FSVNQLAEIVnreGRKLGLDVVVq 401
Cdd:COG0451  178 LIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGG--VYNVGGGEpVTLRELAEAI---AEALGRPPEI- 251

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 302845927 402 NVPNPRVEAEEHYYNAKHTKlVELGLQPHLLADSMIDSLLDF 443
Cdd:COG0451  252 VYPARPGDVRPRRADNSKAR-RELGWRPRTSLEEGLRETVAW 292
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 84-372 6.50e-33

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: 123.56  E-value: 6.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  84 VMIIGGDGYCGWATALHLSARGYEVCIVDNLcrrqfdltlgldtltpiatihdrvrkwaevsgkyislqigdicdwefls 163
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERGHEVVVIDRL------------------------------------------------- 31

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 164 qaftsfqpEHVVHFGEQRSAPYSMidrQKAVFTQTNNVVGTLNVLFAIKELKPdCHLVKLGTMGEYGTPNIDIEEgyltv 243
Cdd:cd08946   32 --------DVVVHLAALVGVPASW---DNPDEDFETNVVGTLNLLEAARKAGV-KRFVYASSASVYGSPEGLPEE----- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 244 thngrTDTLPYPkqgNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTeetmadpmlinrydyDGIFGTALNRF 323
Cdd:cd08946   95 -----EETPPRP---LSPYGVSKLAAEHLLRSYGESYGLPVVILRLANVYGPGQ---------------RPRLDGVVNDF 151

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 302845927 324 VVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGemRVFN 372
Cdd:cd08946  152 IRRALEGKPLTVFGGGNQTRDFIHVDDVVRAILHALENPLEGG--GVYN 198
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
83-372 3.40e-18

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


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 85.52  E-value: 3.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSAR--GYEVCIVDNLCRRqfdltlG-LDTLTPIATiHDRVRkwaevsgkyisLQIGDICDW 159
Cdd:COG1088    3 RILVTGGAGFIGSNFVRYLLAKypGAEVVVLDKLTYA------GnLENLADLED-DPRYR-----------FVKGDIRDR 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 160 EFLSQAFTSFQPEHVVHFGEQRSAPYSMIDrqKAVFTQTnNVVGTLNVLFAIKELK-PDCHLVKLGTMGEYGTPnidIEE 238
Cdd:COG1088   65 ELVDELFAEHGPDAVVHFAAESHVDRSIDD--PAAFVET-NVVGTFNLLEAARKYWvEGFRFHHVSTDEVYGSL---GED 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 239 GYLTVTHngrtdtlPYpkQGNSFYHLSKIhdSTNMLftCKAWkvAATdlnqgvvYGVRTeetmadpmLINR----YdydG 314
Cdd:COG1088  139 GPFTETT-------PL--DPSSPYSASKA--ASDHL--VRAY--HRT-------YGLPV--------VITRcsnnY---G 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302845927 315 I--FGTAL-NRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAArGEmrVFN 372
Cdd:COG1088  186 PyqFPEKLiPLFITNALEGKPLPVYGDGKQVRDWLYVEDHCRAIDLVLEKGRP-GE--TYN 243
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 84-372 3.69e-18

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: 83.50  E-value: 3.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927   84 VMIIGGDGYCGWATALHLSARGYEVCIVDNLCrrqfdltlgldtlTPIATIHDRVRKWAEvsgkyislqiGDICDWEFLS 163
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLT-------------SASNTARLADLRFVE----------GDLTDRDALE 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  164 QAFTSFQPEHVVHFGEQRSAPYSMIDrqkAVFTQTNNVVGTLNVLFAIKELKPDcHLVKLGTMGEYGTPN-IDIEEgylt 242
Cdd:pfam01370  58 KLLADVRPDAVIHLAAVGGVGASIED---PEDFIEANVLGTLNLLEAARKAGVK-RFLFASSSEVYGDGAeIPQEE---- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  243 vthngrtDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGvrteetmadpmlinRYDYDGIFGTALNR 322
Cdd:pfam01370 130 -------TTLTGPLAPNSPYAAAKLAGEWLVLAYAAAYGLRAVILRLFNVYG--------------PGDNEGFVSRVIPA 188

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 302845927  323 FVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEmrVFN 372
Cdd:pfam01370 189 LIRRILEGKPILLWGDGTQRRDFLYVDDVARAILLALEHGAVKGE--IYN 236
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
85-437 2.17e-16

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 79.90  E-value: 2.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927   85 MIIGGDGYCGWATALHLSARGYEVCIVDNLcrrqfDLTLGLDTLTPIATIHDRVRkwaevsgkyISLQIGDICDWEFLSQ 164
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVRR-----SSSFNTGRLEHLYDDHLNGN---------LVLHYGDLTDSSNLVR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  165 AFTSFQPEHVVHFGEQRSAPYSMidrQKAVFTQTNNVVGTLNVLFAIKELKPD--CHLVKLGTMGEYGTPnidiEEGYLT 242
Cdd:pfam16363  67 LLAEVQPDEIYNLAAQSHVDVSF---EQPEYTADTNVLGTLRLLEAIRSLGLEkkVRFYQASTSEVYGKV----QEVPQT 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  243 VTHngrtdtlpyPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEETmADPMLInrydydgifgtalNR 322
Cdd:pfam16363 140 ETT---------PFYPRSPYAAAKLYADWIVVNYRESYGLFACNGILFNHESPRRGER-FVTRKI-------------TR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  323 FVVQAAVG-HPLTVYGKGGQTRGFLDIRDTVRciqiAIDNPAARGEMRVFNQFT-EQFSVNQLAEIVNRE------GRKL 394
Cdd:pfam16363 197 GVARIKLGkQEKLYLGNLDAKRDWGHARDYVE----AMWLMLQQDKPDDYVIATgETHTVREFVEKAFLElgltitWEGK 272

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 302845927  395 GLDVVVQNVPNPRVEAEEHYYNAKH--------TKLV-ELGLQPHLLADSMI 437
Cdd:pfam16363 273 GEIGYFKASGKVHVLIDPRYFRPGEvdrllgdpSKAKeELGWKPKVSFEELV 324
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
 82-372 2.89e-16

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: 79.64  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  82 TRVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLTLGldtltpiatihdRVRKWAEVSG-KYIslqIGDICDWE 160
Cdd:cd05258    1 MRVLITGGAGFIGSNLARFFLKQGWEVIGFDNLMRRGSFGNLA------------WLKANREDGGvRFV---HGDIRNRN 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 161 FLSQAFtsFQPEHVVHFGEQRSAPYSmIDRQKAVFTqtNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYG-TPN---IDI 236
Cdd:cd05258   66 DLEDLF--EDIDLIIHTAAQPSVTTS-ASSPRLDFE--TNALGTLNVLEAARQHAPNAPFIFTSTNKVYGdLPNylpLEE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 237 EEGYLT-----VTHNGRTDTLPYPkQGNSFYHLSKihdstnmlftckawkVAATDLNQ--GVVYGVRTeetmadpmLINR 309
Cdd:cd05258  141 LETRYElapegWSPAGISESFPLD-FSHSLYGASK---------------GAADQYVQeyGRIFGLKT--------VVFR 196

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302845927 310 YdydGI------FGTALNRFV---VQAAV-GHPLTVYGKGG-QTRGFLDIRDTVRCIQIAIDNPAARGEmRVFN 372
Cdd:cd05258  197 C---GCltgprqFGTEDQGWVayfLKCAVtGKPLTIFGYGGkQVRDVLHSADLVNLYLRQFQNPDRRKG-EVFN 266
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 83-390 1.20e-15

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: 77.26  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLCrrqfdlTLGLDTLTPiatIHDRVRkwaevsgkYISLQIGDICDWEFL 162
Cdd:cd05256    1 RVLVTGGAGFIGSHLVERLLERGHEVIVLDNLS------TGKKENLPE---VKPNVK--------FIEGDIRDDELVEFA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 163 SQAftsfqPEHVVHFGEQRSAPYSMIDrqkAVFTQTNNVVGTLNVLFAIKELKPDcHLVKLGTMGEYGtpnidIEEGYLT 242
Cdd:cd05256   64 FEG-----VDYVFHQAAQASVPRSIED---PIKDHEVNVLGTLNLLEAARKAGVK-RFVYASSSSVYG-----DPPYLPK 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 243 VthngrTDTLPYPKqgnSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRteetmADPmlinrydyDGIFGTALNR 322
Cdd:cd05256  130 D-----EDHPPNPL---SPYAVSKYAGELYCQVFARLYGLPTVSLRYFNVYGPR-----QDP--------NGGYAAVIPI 188

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302845927 323 FVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNpAARGEmrVFNQFT-EQFSVNQLAEIVNRE 390
Cdd:cd05256  189 FIERALKGEPPTIYGDGEQTRDFTYVEDVVEANLLAATA-GAGGE--VYNIGTgKRTSVNELAELIREI 254
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 83-213 1.06e-14

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: 74.88  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQfdltlgLDTLTPIATIHdrvrkwaevsgkyISLQIGDICDWEFL 162
Cdd:cd05247    1 KVLVTGGAGYIGSHTVVELLEAGYDVVVLDNLSNGH------REALPRIEKIR-------------IEFYEGDIRDRAAL 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 302845927 163 SQAFTSFQPEHVVHFGEQRSAPYSMidrQKAVFTQTNNVVGTLNVLFAIKE 213
Cdd:cd05247   62 DKVFAEHKIDAVIHFAALKAVGESV---QKPLKYYDNNVVGTLNLLEAMRA 109
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
83-213 7.66e-13

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


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 69.28  E-value: 7.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLC--RRQFdltlgldtltpiatihdrVRKWAEvsgkyisLQIGDICDWE 160
Cdd:COG1087    2 KILVTGGAGYIGSHTVVALLEAGHEVVVLDNLSngHREA------------------VPKGVP-------FVEGDLRDRA 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302845927 161 FLSQAFTSFQPEHVVHF------GEqrsapySMidrQKAVFTQTNNVVGTLNVLFAIKE 213
Cdd:COG1087   57 ALDRVFAEHDIDAVIHFaalkavGE------SV---EKPLKYYRNNVVGTLNLLEAMRE 106
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
 83-364 1.51e-11

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: 65.44  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLcRRQFDLTLGldtltpiatiHDRVRKWAEVSG-KYISlqiGDICDWEF 161
Cdd:cd05253    2 KILVTGAAGFIGFHVAKRLLERGDEVVGIDNL-NDYYDVRLK----------EARLELLGKSGGfKFVK---GDLEDREA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 162 LSQAFTSFQPEHVVHFGEQRSAPYSMIDRQKAVftqTNNVVGTLNVLFAIKELKPDcHLVKLGTMGEYG-TPNIDIEEgy 240
Cdd:cd05253   68 LRRLFKDHEFDAVIHLAAQAGVRYSLENPHAYV---DSNIVGFLNLLELCRHFGVK-HLVYASSSSVYGlNTKMPFSE-- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 241 ltvthNGRTDT--LPYP--KQGN-----SFYHLSKIHDSTNMLFTckawkvaatdlnqgvVYGVRTEETMAdpmlinryd 311
Cdd:cd05253  142 -----DDRVDHpiSLYAatKKANelmahTYSHLYGIPTTGLRFFT---------------VYGPWGRPDMA--------- 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302845927 312 ydgIFgtalnRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAA 364
Cdd:cd05253  193 ---LF-----LFTKAILEGKPIDVFNDGNMSRDFTYIDDIVEGVVRALDTPAK 237
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
 82-372 1.67e-10

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: 62.18  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  82 TRVMIIGGDGYCGWATALHLSARG--YEVCIVDNL--CRRqfdltlgLDTLTPIatihdrvrkwaEVSGKYISLQiGDIC 157
Cdd:cd05246    1 MKILVTGGAGFIGSNFVRYLLNKYpdYKIINLDKLtyAGN-------LENLEDV-----------SSSPRYRFVK-GDIC 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 158 DWEFLSQAFTSFQPEHVVHFgeqrsAPYSMIDR---QKAVFTQTnNVVGTLNVLFAIKELKPDcHLVKLGTMGEYGtpni 234
Cdd:cd05246   62 DAELVDRLFEEEKIDAVIHF-----AAESHVDRsisDPEPFIRT-NVLGTYTLLEAARKYGVK-RFVHISTDEVYG---- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 235 DI-EEGYLTVTHngrtdtlpyPKQGNSFYHLSKIhdSTNMLftCKAW----KVAATDLNQGVVYGVRT--EEtmadpmLI 307
Cdd:cd05246  131 DLlDDGEFTETS---------PLAPTSPYSASKA--AADLL--VRAYhrtyGLPVVITRCSNNYGPYQfpEK------LI 191

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302845927 308 nrydydgifgtalNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRciqiAIDNPAARGEM-RVFN 372
Cdd:cd05246  192 -------------PLFILNALDGKPLPIYGDGLNVRDWLYVEDHAR----AIELVLEKGRVgEIYN 240
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
 83-355 8.71e-10

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 60.05  E-value: 8.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYE-VCIVDNLCrrqfdLTLGLDTLTPIATiHDRvrkwaevsgkyISLQIGDICDWEF 161
Cdd:PRK10217   3 KILITGGAGFIGSALVRYIINETSDaVVVVDKLT-----YAGNLMSLAPVAQ-SER-----------FAFEKVDICDRAE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 162 LSQAFTSFQPEHVVHFgeqrsAPYSMIDRQ---KAVFTQTnNVVGTLNVLFAIKELkpdCHLVKLGTMGEYGTPNIDIEE 238
Cdd:PRK10217  66 LARVFTEHQPDCVMHL-----AAESHVDRSidgPAAFIET-NIVGTYTLLEAARAY---WNALTEDKKSAFRFHHISTDE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 239 GY--LTVTHNGRTDTLPYPKqgNSFYHLSKIhdSTNMLftCKAWKVAatdlnqgvvYGVRTEETMADpmliNRYDYDGIF 316
Cdd:PRK10217 137 VYgdLHSTDDFFTETTPYAP--SSPYSASKA--SSDHL--VRAWLRT---------YGLPTLITNCS----NNYGPYHFP 197

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 302845927 317 GTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCI 355
Cdd:PRK10217 198 EKLIPLMILNALAGKPLPVYGNGQQIRDWLYVEDHARAL 236
PLN02240 PLN02240
UDP-glucose 4-epimerase
 77-208 1.37e-09

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 59.59  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  77 GGGAGTRVMIIGGDGYCGWATALHLSARGYEVCIVDNlcrrqfdltlgLDTLTPIATihDRVRKWAEVSGKYISLQIGDI 156
Cdd:PLN02240   1 MSLMGRTILVTGGAGYIGSHTVLQLLLAGYKVVVIDN-----------LDNSSEEAL--RRVKELAGDLGDNLVFHKVDL 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302845927 157 CDWEFLSQAFTSFQPEHVVHF------GEQRSAPYSMIDrqkavftqtNNVVGTLNVL 208
Cdd:PLN02240  68 RDKEALEKVFASTRFDAVIHFaglkavGESVAKPLLYYD---------NNLVGTINLL 116
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
 83-213 1.43e-09

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 59.44  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLtlgldtltpIATIHdrvrkwaEVSGKYISLQIGDICDWEFL 162
Cdd:PRK10675   2 RVLVTGGSGYIGSHTCVQLLQNGHDVVILDNLCNSKRSV---------LPVIE-------RLGGKHPTFVEGDIRNEALL 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 302845927 163 SQAFTSFQPEHVVHF------GEQRSAPYSMIDrqkavftqtNNVVGTLNVLFAIKE 213
Cdd:PRK10675  66 TEILHDHAIDTVIHFaglkavGESVQKPLEYYD---------NNVNGTLRLISAMRA 113
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
 29-387 2.69e-07

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 52.71  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  29 VGGRVCALRASVGR-KAASAAQVASRAVSvkvnaIATIERPAGPAPTSSGGGAG-------------TRVMIIGGDGYCG 94
Cdd:PLN02166  59 IGSTFFILQPSLSRlGPAESTSLITRSVS-----IAVTDSPPSSSTFNSSGGGGrtgrvpvgigrkrLRIVVTGGAGFVG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  95 WATALHLSARGYEVCIVDNLCRRQFDLTLGLDTLTPIATI-HDRVRKwaevsgkyISLQIgdicdweflSQAFTSFQPEH 173
Cdd:PLN02166 134 SHLVDKLIGRGDEVIVIDNFFTGRKENLVHLFGNPRFELIrHDVVEP--------ILLEV---------DQIYHLACPAS 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 174 VVHFgeqrsapysmidRQKAVFTQTNNVVGTLNVLFAIKelkpdchlvKLGTmgeygtpnidieEGYLTVTHNGRTDTLP 253
Cdd:PLN02166 197 PVHY------------KYNPVKTIKTNVMGTLNMLGLAK---------RVGA------------RFLLTSTSEVYGDPLE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 254 YPKQGNSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEE---TMADPMLINRydydgifGTALNRFVVQAAVG 330
Cdd:PLN02166 244 HPQKETYWGNVNPIGERSCYDEGKRTAETLAMDYHRGAGVEVRIARifnTYGPRMCLDD-------GRVVSNFVAQTIRK 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 302845927 331 HPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAArGEMRVFNqfTEQFSVNQLAEIV 387
Cdd:PLN02166 317 QPMTVYGDGKQTRSFQYVSDLVDGLVALMEGEHV-GPFNLGN--PGEFTMLELAEVV 370
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
 83-212 1.02e-06

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: 50.58  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVDNLC--RRqfdltlglDTLTPIATIhdrvrkwaevsgkyiSLQIGDICDWE 160
Cdd:cd08957    2 KVLITGGAGQIGSHLIEHLLERGHQVVVIDNFAtgRR--------EHLPDHPNL---------------TVVEGSIADKA 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 302845927 161 FLSQAFTSFQPEHVVHFGEQRSAPYSMIDRqkavfTQTnNVVGTLNVLFAIK 212
Cdd:cd08957   59 LVDKLFGDFKPDAVVHTAAAYKDPDDWYED-----TLT-NVVGGANVVQAAK 104
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
 83-230 1.78e-06

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: 49.52  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVcivDNLCRRQFDLTLGldtltpiatihdrVRKWAEVSGKYISLQIGDICDWEFL 162
Cdd:cd05260    1 RALITGITGQDGSYLAEFLLEKGYEV---HGIVRRSSSFNTD-------------RIDHLYINKDRITLHYGDLTDSSSL 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302845927 163 SQAFTSFQPEHVVHFGEQRSAPYSMIDrqkAVFTQTNNVVGTLNVLFAIKELKPDCHLVKLGTMGEYG 230
Cdd:cd05260   65 RRAIEKVRPDEIYHLAAQSHVKVSFDD---PEYTAEVNAVGTLNLLEAIRILGLDARFYQASSSEEYG 129
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
 317-406 1.11e-05

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: 47.25  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 317 GTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNPAARGEMRVFNqfTEQFSVNQLAEIVnregRKL-G 395
Cdd:cd05230  183 GRVVSNFIVQALRGEPITVYGDGTQTRSFQYVSDLVEGLIRLMNSDYFGGPVNLGN--PEEFTILELAELV----KKLtG 256

                         90
                 ....*....|.
gi 302845927 396 LDVVVQNVPNP 406
Cdd:cd05230  257 SKSEIVFLPLP 267
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
 146-215 1.80e-05

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: 46.54  E-value: 1.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 146 GKYISLQIGDICDWEFLSQAFTSFQPEHVVHFGEQrsaPYSMIDRQKAVFTQTNNVVGTLNVLFAIKELK 215
Cdd:cd05252   51 DNKISSTRGDIRDLNALREAIREYEPEIVFHLAAQ---PLVRLSYKDPVETFETNVMGTVNLLEAIRETG 117
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
 83-398 4.57e-05

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 45.39  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHLSARGYEVCIVD-NLCRRQFDLtlgldtltpiatihDRVRkwaevsgkYISlqiGDICDWEF 161
Cdd:cd05264    1 RVLIVGGNGFIGSHLVDALLEEGPQVRVFDrSIPPYELPL--------------GGVD--------YIK---GDYENRAD 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 162 LSQAFTsfQPEHVVHFGEQRSAPYSMIDRQKAVFTqtnNVVGTLNVLFAIKELKPDCHLV--KLGTMgeYGTPnidieeG 239
Cdd:cd05264   56 LESALV--GIDTVIHLASTTNPATSNKNPILDIQT---NVAPTVQLLEACAAAGIGKIIFasSGGTV--YGVP------E 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 240 YLTVTHNGRTDTLpypkqgnSFYHLSKIHDSTNMLFTCKAWKVAATDLNQGVVYGVRTEetmadpmlINRYDydGIFGTA 319
Cdd:cd05264  123 QLPISESDPTLPI-------SSYGISKLAIEKYLRLYQYLYGLDYTVLRISNPYGPGQR--------PDGKQ--GVIPIA 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 320 LNRfvvqAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQIAIDNpaaRGEMRVFNQFT-EQFSVNQL-AEIVNREGRKLGLD 397
Cdd:cd05264  186 LNK----ILRGEPIEIWGDGESIRDYIYIDDLVEALMALLRS---KGLEEVFNIGSgIGYSLAELiAEIEKVTGRSVQVI 258


                 .
gi 302845927 398 V 398
Cdd:cd05264  259 Y 259
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
 83-353 5.79e-05

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 45.17  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  83 RVMIIGGDGYCGWATALHlsargyevcIVDNlcrrQFDLTLGLDTLTPIATIHDRVRkwAEVSGKYISLQIgDICDWEFL 162
Cdd:PRK10084   2 KILVTGGAGFIGSAVVRH---------IINN----TQDSVVNVDKLTYAGNLESLAD--VSDSERYVFEHA-DICDRAEL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 163 SQAFTSFQPEHVVHFgeqrsAPYSMIDRQ---KAVFTQTnNVVGTLNVLFAIK--------ELKPDCHLVKLGTMGEYGT 231
Cdd:PRK10084  66 DRIFAQHQPDAVMHL-----AAESHVDRSitgPAAFIET-NIVGTYVLLEAARnywsaldeDKKNAFRFHHISTDEVYGD 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 232 -PNIDIEEGYLTVTHngRTDTLPYPKqgNSFYHLSKIhdSTNMLftCKAWKVAatdlnqgvvYGVRTEETMADpmliNRY 310
Cdd:PRK10084 140 lPHPDEVENSEELPL--FTETTAYAP--SSPYSASKA--SSDHL--VRAWLRT---------YGLPTIVTNCS----NNY 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 302845927 311 D-YDgiFGTALNRFVVQAAV-GHPLTVYGKGGQTRGFLDIRDTVR 353
Cdd:PRK10084 199 GpYH--FPEKLIPLVILNALeGKPLPIYGKGDQIRDWLYVEDHAR 241
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 80-208 7.11e-05

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: 44.53  E-value: 7.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  80 AGTRVMIIGGDGYCGWATALHLSARG-YEVCIVDNLCRRQFDLTLGLdtltPIATIHDRVRkwaevsgkYIslqIGDICD 158
Cdd:cd05237    1 KGKTILVTGGAGSIGSELVRQILKFGpKKLIVFDRDENKLHELVREL----RSRFPHDKLR--------FI---IGDVRD 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 159 WEFLSQAFTSFQPEHVVHFgeqrSA----------PYSMIDrqkavftqtNNVVGTLNVL 208
Cdd:cd05237   66 KERLRRAFKERGPDIVFHA----AAlkhvpsmednPEEAIK---------TNVLGTKNVI 112
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
 336-434 1.26e-04

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: 43.83  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 336 YGKGGQTRGFLDIRDTVRCIQIAIDNPAARGemrVFNQFTEQF-SVNQLAEIVNREgrkLGLDVVVQNVPNPR--VEAEE 412
Cdd:cd05248  209 YADGEQLRDFVYVKDVVKVNLFFLENPSVSG---IFNVGTGRArSFNDLASATFKA---LGKEVKIEYIDFPEdlRGKYQ 282

                         90       100
                 ....*....|....*....|....
gi 302845927 413 HYYNAKHTKLVELGL--QPHLLAD 434
Cdd:cd05248  283 SFTEADISKLRAAGYtkEFHSLEE 306
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
 23-108 7.84e-04

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 41.67  E-value: 7.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  23 SVASMRVGGRVCALRASVGRKAASAAQVASRAVSVKVNAIATIERPAGPAPTSSGGGAG-TRVMIIGGDGYCGWATALHL 101
Cdd:PLN02657   1 HLSSSLFSLRAAAAASSSPSNRLAASLGGALVRRAAAASRGSRATAAAAAQSFRSKEPKdVTVLVVGATGYIGKFVVREL 80


                 ....*..
gi 302845927 102 SARGYEV 108
Cdd:PLN02657  81 VRRGYNV 87
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 84-213 7.93e-04

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


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 41.50  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  84 VMIIGGDGYCGWATALHLSARGYEVCIvdnLCRRQFDlTLGLDtltpiatiHDRVrKWAEvsgkyislqiGDICDWEFLS 163
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYRVRA---LVRSGSD-AVLLD--------GLPV-EVVE----------GDLTDAASLA 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 302845927 164 QAFTsfQPEHVVHFgeqrSAPYSMIDRQKAVFTQTNnVVGTLNVLFAIKE 213
Cdd:cd05228   58 AAMK--GCDRVFHL----AAFTSLWAKDRKELYRTN-VEGTRNVLDAALE 100
PLN02206 PLN02206
UDP-glucuronate decarboxylase
 81-352 1.36e-03

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 41.12  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  81 GTRVMIIGGDGYCGWATALHLSARGYEVCIVDNLC--RRQ----------FDLtLGLDTLTPIATIHDRVRKWAevsgky 148
Cdd:PLN02206 119 GLRVVVTGGAGFVGSHLVDRLMARGDSVIVVDNFFtgRKEnvmhhfsnpnFEL-IRHDVVEPILLEVDQIYHLA------ 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 149 islqigdiCdweflsqaftsfqPEHVVHFgeqrsapysmidRQKAVFTQTNNVVGTLNVLFAIKELkpDCHLVKLGTMGE 228
Cdd:PLN02206 192 --------C-------------PASPVHY------------KFNPVKTIKTNVVGTLNMLGLAKRV--GARFLLTSTSEV 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 229 YGTP--------------NIDIEEGYLTVTHNGRTDTLPYPKQGNSFYHLSKIHDStnmlftckawkvaatdlnqgvvYG 294
Cdd:PLN02206 237 YGDPlqhpqvetywgnvnPIGVRSCYDEGKRTAETLTMDYHRGANVEVRIARIFNT----------------------YG 294

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302845927 295 VRteetmadpMLINRydydgifGTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTV 352
Cdd:PLN02206 295 PR--------MCIDD-------GRVVSNFVAQALRKEPLTVYGDGKQTRSFQFVSDLV 337
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 25-221 3.69e-03

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 39.67  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927  25 ASMRVGGRVCALRASvgrkAASAAQVASRAVSVKVNAIATIERPAGPAPTSSGGGAGTrVMIIGGDGYCGWATALHLSAR 104
Cdd:cd05274   99 DAADEAAALAALLAG----APGEDELALRGGQRLVPRLVRAPAAALELAAAPGGLDGT-YLITGGLGGLGLLVARWLAAR 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302845927 105 GYEVCIVdnLCRRqfdltlgldtlTPIATIHDRVRKWaEVSGKYISLQIGDICDWEFLSQAFTSFQPE----HVVHF-GE 179
Cdd:cd05274  174 GARHLVL--LSRR-----------GPAPRAAARAALL-RAGGARVSVVRCDVTDPAALAALLAELAAGgplaGVIHAaGV 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 302845927 180 QRSAPYSMIDRQKAVFTQTNNVVGTLNVLFAIKELKPDCHLV 221
Cdd:cd05274  240 LRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFFVL 281
 
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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