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Conserved domains on  [gi|1519667522|gb|RPG38866|]
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MAG: UDP-N-acetyl-D-mannosamine dehydrogenase [Muricauda sp. TMED12]

Protein Classification

nucleotide sugar dehydrogenase( domain architecture ID 1004558)

nucleotide sugar dehydrogenase such as UDP-N-acetyl-D-mannosamine dehydrogenase that catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA)

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0051287|GO:0016616|GO:0003979|GO:0000271

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
wecC super family cl32636
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 6-397 0e+00

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


The actual alignment was detected with superfamily member PRK11064:

Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 565.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRASTEAALANTYLIVVPT 85
Cdd:PRK11064    6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAVPT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  86 PFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPEL-----KGE---VFIAYCPERVLPGN 157
Cdd:PRK11064   86 PFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqAGEqadINIAYCPERVLPGQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 158 VMYELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELIN 237
Cdd:PRK11064  166 VMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIR 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 238 LANKHPRVNILQPGCGVGGHCIAVDPYFIVAEYPMESRIIGKAREVNNYKSFWCAEKIVSTKLEFELRHGRK---PKIAL 314
Cdd:PRK11064  246 LANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRaseVKIAC 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 315 LGLAFKPDIDDLRESPAKYIVQRvLQDSNNEDYYIVEPNIDN-----HNVFKLTEFTVAVKEADIIVILVAHKEFKQL-- 387
Cdd:PRK11064  326 FGLAFKPNIDDLRESPAMEIAEL-IAQWHSGETLVVEPNIHQlpkklDGLVTLVSLDEALATADVLVMLVDHSQFKAIng 404

                         410
                  ....*....|
gi 1519667522 388 TELENKVVLD 397
Cdd:PRK11064  405 DNVHQQWVVD 414
 
Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 6-397 0e+00

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 565.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRASTEAALANTYLIVVPT 85
Cdd:PRK11064    6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAVPT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  86 PFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPEL-----KGE---VFIAYCPERVLPGN 157
Cdd:PRK11064   86 PFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqAGEqadINIAYCPERVLPGQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 158 VMYELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELIN 237
Cdd:PRK11064  166 VMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIR 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 238 LANKHPRVNILQPGCGVGGHCIAVDPYFIVAEYPMESRIIGKAREVNNYKSFWCAEKIVSTKLEFELRHGRK---PKIAL 314
Cdd:PRK11064  246 LANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRaseVKIAC 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 315 LGLAFKPDIDDLRESPAKYIVQRvLQDSNNEDYYIVEPNIDN-----HNVFKLTEFTVAVKEADIIVILVAHKEFKQL-- 387
Cdd:PRK11064  326 FGLAFKPNIDDLRESPAMEIAEL-IAQWHSGETLVVEPNIHQlpkklDGLVTLVSLDEALATADVLVMLVDHSQFKAIng 404

                         410
                  ....*....|
gi 1519667522 388 TELENKVVLD 397
Cdd:PRK11064  405 DNVHQQWVVD 414
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-403 0e+00

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 520.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDlGEAVSYAVSNGFLRAST---EAALANTYLIV 82
Cdd:COG0677     2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTdpeALAEADVVIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  83 VPTPFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELK--GEVFIAYCPERVLPGNVMY 160
Cdd:COG0677    81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKagEDFFLAYSPERINPGNKLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHE-TNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLA 239
Cdd:COG0677   161 ELRNIPKVVGGITPESAERAAALYGSVVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 240 NKHPRVNILQPGCGVGGHCIAVDPYFIVA---EYPMESRIIGKAREVNNYKSFWCAEKIVStKLEFELRHGRKPKIALLG 316
Cdd:COG0677   241 NTKPGFLIFYPGPGVGGHCIPVDPYYLTWkarELGYHPRLILAAREINDSMPEYVVERVVK-ALNEAGKSLKGARVLVLG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 317 LAFKPDIDDLRESPAKYIVQRvLQDsNNEDYYIVEPNIDNHNV----FKLTEFTVAVKEADIIVILVAHKEFKQLT---- 388
Cdd:COG0677   320 LAYKENVDDLRESPALDIIEE-LRE-YGAEVDVHDPYVDEEEVegeyGELVDLEEALEGADAVVLAVDHDEFDELDpeel 397

                         410
                  ....*....|....*.
gi 1519667522 389 -ELENKVVLDFSGALK 403
Cdd:COG0677   398 rLKGAKVVVDTRGVLD 413
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 6-397 7.97e-134

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 389.66  E-value: 7.97e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRASTEAAL----ANTYLI 81
Cdd:TIGR03026   3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEairdADVIII 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  82 VVPTPFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVF-IAYCPERVLPGNVMY 160
Cdd:TIGR03026  83 CVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFyLAYNPEFLREGNAVH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLAN 240
Cdd:TIGR03026 163 DLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEAAG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 241 KHPR--VNILQPGCGVGGHCIAVDPYFIVAEYPM---ESRIIGKAREVNNYKSFWCAEKIVSTkleFELRHGRkpKIALL 315
Cdd:TIGR03026 243 TDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKElgyNPELIEAAREINDSQPDYVVEKIKDL---LGPLKGK--TVLIL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 316 GLAFKPDIDDLRESPAKYIVQRVLQDSNNEDYYivEPNIDN---HNVFKLTEFTVAVKEADIIVILVAHKEFKQL----- 387
Cdd:TIGR03026 318 GLAFKPNTDDVRESPALDIIELLKEKGAKVKAY--DPLVPEeevKGLPSIDDLEEALKGADALVILTDHSEFKDLdleki 395

                         410
                  ....*....|.
gi 1519667522 388 -TELENKVVLD 397
Cdd:TIGR03026 396 kDLMKGKVVVD 406
UDPMaNacDH_Arch NF040825
UDP-N-acetyl-D-mannosamine dehydrogenase;
5-404 3.37e-103

UDP-N-acetyl-D-mannosamine dehydrogenase;


Pssm-ID: 468765 [Multi-domain]  Cd Length: 418  Bit Score: 311.70  E-value: 3.37e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   5 EVNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRAST---EAALANTYLI 81
Cdd:NF040825    2 KIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTdpeDLKGADAFII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  82 VVPTPFKNNhEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVF-IAYCPERVLPGNVMY 160
Cdd:NF040825   82 CVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEELTGLKEGEDFyMAHAPERVMPGRIFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLAN 240
Cdd:NF040825  161 ELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNVFEAIELAN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 241 KHPRVNILQPGCGVGGHCIAVDPYFIVAEYPMESRIIGKAREVNNyksfwcAEKIVSTKLEFEL--RHGRKPK---IALL 315
Cdd:NF040825  241 THPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINE------DMPLFAKDLLFEAleEANVPPEeavVTVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 316 GLAFKPDIDDLRESPAKYIVQRVLQDSNNEDYYivEPNID-NHNVFKlteftVAVKEADIIVILVAHKEFKQL------T 388
Cdd:NF040825  315 GLAYKGDTDDTRNSPALKFVELIEDDVKEVRTY--DPYVGgTHESLE-----DAVKGADAIVIATDHSEFKSLnweelgK 387

                         410
                  ....*....|....*.
gi 1519667522 389 ELENKVVLDFSGALKK 404
Cdd:NF040825  388 LMRTKILIDGRHIIKE 403
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 6-182 5.54e-59

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 190.15  E-value: 5.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVS---NGFLRASTEAALANTYLIV 82
Cdd:pfam03721   3 ISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSgrlSFTTDYSTAIEEADVIFIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  83 VPTPFK-NNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVF-IAYCPERVLPGNVMY 160
Cdd:pfam03721  83 VGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFdVASNPEFLREGSAVY 162

                         170       180
                  ....*....|....*....|..
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVE 182
Cdd:pfam03721 163 DLFNPDRVVIGVTEKCAEAALE 184
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 313-403 2.26e-17

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 76.78  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  313 ALLGLAFKPDIDDLRESPAKYIVQRvLQDSNNE-DYY--IVEPNIDNHNVFKLTEFTVAVKEADIIVILVAHKEFKQLTE 389
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEE-LLEAGAEvVVYdpYAMEEAREYGLTYVSDLEEALKGADAVVIATEHDEFRSLDP 79

                           90       100
                   ....*....|....*....|
gi 1519667522  390 ------LENKVVLDFSGALK 403
Cdd:smart00984  80 eelkdlMKKPVVVDGRNILD 99
 
Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 6-397 0e+00

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 565.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRASTEAALANTYLIVVPT 85
Cdd:PRK11064    6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAVPT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  86 PFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPEL-----KGE---VFIAYCPERVLPGN 157
Cdd:PRK11064   86 PFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqAGEqadINIAYCPERVLPGQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 158 VMYELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELIN 237
Cdd:PRK11064  166 VMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIR 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 238 LANKHPRVNILQPGCGVGGHCIAVDPYFIVAEYPMESRIIGKAREVNNYKSFWCAEKIVSTKLEFELRHGRK---PKIAL 314
Cdd:PRK11064  246 LANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRaseVKIAC 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 315 LGLAFKPDIDDLRESPAKYIVQRvLQDSNNEDYYIVEPNIDN-----HNVFKLTEFTVAVKEADIIVILVAHKEFKQL-- 387
Cdd:PRK11064  326 FGLAFKPNIDDLRESPAMEIAEL-IAQWHSGETLVVEPNIHQlpkklDGLVTLVSLDEALATADVLVMLVDHSQFKAIng 404

                         410
                  ....*....|
gi 1519667522 388 TELENKVVLD 397
Cdd:PRK11064  405 DNVHQQWVVD 414
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-403 0e+00

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 520.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDlGEAVSYAVSNGFLRAST---EAALANTYLIV 82
Cdd:COG0677     2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTdpeALAEADVVIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  83 VPTPFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELK--GEVFIAYCPERVLPGNVMY 160
Cdd:COG0677    81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKagEDFFLAYSPERINPGNKLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHE-TNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLA 239
Cdd:COG0677   161 ELRNIPKVVGGITPESAERAAALYGSVVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 240 NKHPRVNILQPGCGVGGHCIAVDPYFIVA---EYPMESRIIGKAREVNNYKSFWCAEKIVStKLEFELRHGRKPKIALLG 316
Cdd:COG0677   241 NTKPGFLIFYPGPGVGGHCIPVDPYYLTWkarELGYHPRLILAAREINDSMPEYVVERVVK-ALNEAGKSLKGARVLVLG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 317 LAFKPDIDDLRESPAKYIVQRvLQDsNNEDYYIVEPNIDNHNV----FKLTEFTVAVKEADIIVILVAHKEFKQLT---- 388
Cdd:COG0677   320 LAYKENVDDLRESPALDIIEE-LRE-YGAEVDVHDPYVDEEEVegeyGELVDLEEALEGADAVVLAVDHDEFDELDpeel 397

                         410
                  ....*....|....*.
gi 1519667522 389 -ELENKVVLDFSGALK 403
Cdd:COG0677   398 rLKGAKVVVDTRGVLD 413
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 6-397 7.97e-134

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 389.66  E-value: 7.97e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRASTEAAL----ANTYLI 81
Cdd:TIGR03026   3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEairdADVIII 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  82 VVPTPFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVF-IAYCPERVLPGNVMY 160
Cdd:TIGR03026  83 CVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFyLAYNPEFLREGNAVH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLAN 240
Cdd:TIGR03026 163 DLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEAAG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 241 KHPR--VNILQPGCGVGGHCIAVDPYFIVAEYPM---ESRIIGKAREVNNYKSFWCAEKIVSTkleFELRHGRkpKIALL 315
Cdd:TIGR03026 243 TDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKElgyNPELIEAAREINDSQPDYVVEKIKDL---LGPLKGK--TVLIL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 316 GLAFKPDIDDLRESPAKYIVQRVLQDSNNEDYYivEPNIDN---HNVFKLTEFTVAVKEADIIVILVAHKEFKQL----- 387
Cdd:TIGR03026 318 GLAFKPNTDDVRESPALDIIELLKEKGAKVKAY--DPLVPEeevKGLPSIDDLEEALKGADALVILTDHSEFKDLdleki 395

                         410
                  ....*....|.
gi 1519667522 388 -TELENKVVLD 397
Cdd:TIGR03026 396 kDLMKGKVVVD 406
UDPMaNacDH_Arch NF040825
UDP-N-acetyl-D-mannosamine dehydrogenase;
5-404 3.37e-103

UDP-N-acetyl-D-mannosamine dehydrogenase;


Pssm-ID: 468765 [Multi-domain]  Cd Length: 418  Bit Score: 311.70  E-value: 3.37e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   5 EVNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRAST---EAALANTYLI 81
Cdd:NF040825    2 KIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTdpeDLKGADAFII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  82 VVPTPFKNNhEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVF-IAYCPERVLPGNVMY 160
Cdd:NF040825   82 CVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEELTGLKEGEDFyMAHAPERVMPGRIFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVEFYRKYVTGELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLAN 240
Cdd:NF040825  161 ELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNVFEAIELAN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 241 KHPRVNILQPGCGVGGHCIAVDPYFIVAEYPMESRIIGKAREVNNyksfwcAEKIVSTKLEFEL--RHGRKPK---IALL 315
Cdd:NF040825  241 THPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINE------DMPLFAKDLLFEAleEANVPPEeavVTVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 316 GLAFKPDIDDLRESPAKYIVQRVLQDSNNEDYYivEPNID-NHNVFKlteftVAVKEADIIVILVAHKEFKQL------T 388
Cdd:NF040825  315 GLAYKGDTDDTRNSPALKFVELIEDDVKEVRTY--DPYVGgTHESLE-----DAVKGADAIVIATDHSEFKSLnweelgK 387

                         410
                  ....*....|....*.
gi 1519667522 389 ELENKVVLDFSGALKK 404
Cdd:NF040825  388 LMRTKILIDGRHIIKE 403
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
6-397 4.76e-61

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 203.33  E-value: 4.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVSNGFLRAST--EAALANT--YLI 81
Cdd:COG1004     3 IAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTdlAEAVAEAdvVFI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  82 VVPTPFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVFIAYCPERVLPGNVMYE 161
Cdd:COG1004    83 AVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGAGVDFDVVSNPEFLREGSAVED 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 162 LVHNDR-VIGGVDEKSTKKAVEFYRKYVTGE--LHETNARTAEMCKLVENS---SRdvqIAFANELSLICDKADIDVWEL 235
Cdd:COG1004   163 FLRPDRiVIGVDSERAAEVLRELYAPFVRNGtpIIVTDLRSAELIKYAANAflaTK---ISFINEIANLCEKVGADVEEV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 236 ---INLankHPRvnI----LQPGCGVGGHC--------IAvdpyfIVAEYPMESRIIGKAREVNNYKSFWCAEKIVsTKL 300
Cdd:COG1004   240 argIGL---DSR--IgpkfLYAGIGYGGSCfpkdvralIA-----TARELGYDLRLLEAVEEVNERQKRRLVEKIR-EHL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 301 EFELRhGRkpKIALLGLAFKPDIDDLRESPAKYIVQRVLQdsnnEDYYIV--EPnIDNHNVFKLTEFTV--------AVK 370
Cdd:COG1004   309 GGDLK-GK--TIAVLGLAFKPNTDDMRESPALDIIEALLE----AGARVRayDP-VAMENARRLLPDDItyaddayeALE 380

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1519667522 371 EADIIVILVAHKEFKQL------TELENKVVLD 397
Cdd:COG1004   381 GADALVILTEWPEFRALdfarlkALMKGPVIFD 413
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 6-182 5.54e-59

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 190.15  E-value: 5.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   6 VNILGLGYIGLPTAALIAKNGTHVHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVS---NGFLRASTEAALANTYLIV 82
Cdd:pfam03721   3 ISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSgrlSFTTDYSTAIEEADVIFIA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  83 VPTPFK-NNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPELKGEVF-IAYCPERVLPGNVMY 160
Cdd:pfam03721  83 VGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFdVASNPEFLREGSAVY 162

                         170       180
                  ....*....|....*....|..
gi 1519667522 161 ELVHNDRVIGGVDEKSTKKAVE 182
Cdd:pfam03721 163 DLFNPDRVVIGVTEKCAEAALE 184
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
5-387 1.50e-42

Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 154.46  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   5 EVNILGLGYIGLPTAALIAKNgTHVHGVDINKDVVETINNG---KIHIVEPDLGEAvsyavsnGFLRASTEAAL---ANT 78
Cdd:PRK15182    8 KIAIIGLGYVGLPLAVEFGKS-RQVVGFDVNKKRILELKNGvdvNLETTEEELREA-------RYLKFTSEIEKikeCNF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  79 YLIVVPTPFKNNHEPDISFVESATENIIPLLKKGDTYIIESTSPVGTTEKMMHLIYEKRPEL--KGEVFIAYCPERVLPG 156
Cdd:PRK15182   80 YIITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMtfNQDFYVGYSPERINPG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 157 NVMYELVHNDRVIGGVDEKSTKKAVEFYRKYVT-GELHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADIDVWEL 235
Cdd:PRK15182  160 DKKHRLTNIKKITSGSTAQIAELIDEVYQQIISaGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 236 INLANKHPRVNILQPGCgVGGHCIAVDPYFI------VAEYPmesRIIGKAREVNNYKSFWCAEKIVSTKLEFELrHGRK 309
Cdd:PRK15182  240 LRAAGSKWNFLPFRPGL-VGGHCIGVDPYYLthksqgIGYYP---EIILAGRRLNDNMGNYVSEQLIKAMIKKGI-NVEG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 310 PKIALLGLAFKPDIDDLRESPAKYIVQRVLQDSNNEDyyIVEPNIDNHNVFK----LTEFTVAVKEADIIVILVAHKEFK 385
Cdd:PRK15182  315 SSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVD--IFDPWVDAEEVRReygiIPVSEVKSSHYDAIIVAVGHQQFK 392


                  ..
gi 1519667522 386 QL 387
Cdd:PRK15182  393 QM 394
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 199-285 2.11e-33

UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 460015 [Multi-domain]  Cd Length: 92  Bit Score: 120.18  E-value: 2.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 199 TAEMCKLVENSSRDVQIAFANELSLICDKADIDVWELINLANKHPR--VNILQPGCGVGGHCIAVDPYFIVA---EYPME 273
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIYlarELGVP 80

                          90
                  ....*....|..
gi 1519667522 274 SRIIGKAREVNN 285
Cdd:pfam00984  81 ARLLEAAREVNE 92
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 9-341 2.09e-26

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 110.15  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   9 LGLGYIGLPTAALIAKNGTH--VHGVDINKDVVETINNGKIHIVEPDLGEAVSYAVS-NGFLRASTEAALANTYLIVVP- 84
Cdd:PLN02353    7 IGAGYVGGPTMAVIALKCPDieVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGkNLFFSTDVEKHVAEADIVFVSv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  85 -TPFKNN-----HEPDISFVESATEnIIPLLKKGDTYIIE-STSPVGTTEKMMHLIYEKRPELKGEVFIAycPERVLPGN 157
Cdd:PLN02353   87 nTPTKTRglgagKAADLTYWESAAR-MIADVSKSDKIVVEkSTVPVKTAEAIEKILTHNSKGINFQILSN--PEFLAEGT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 158 VMYELVHNDRV-IGGVDEKSTKKAVE----FYRKYVTGE-LHETNARTAEMCKLVENSSRDVQIAFANELSLICDKADID 231
Cdd:PLN02353  164 AIEDLFKPDRVlIGGRETPEGQKAVQalkdVYAHWVPEErIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATGAD 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 232 VWELINLANKHPRV--NILQPGCGVGGHCIAVDPYFIVaeYPMESRIIGKARE-------VNNYKSFWCAEKIVSTKleF 302
Cdd:PLN02353  244 VSQVSHAVGKDSRIgpKFLNASVGFGGSCFQKDILNLV--YICECNGLPEVAEywkqvikMNDYQKSRFVNRVVSSM--F 319

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1519667522 303 ELRHGRKpkIALLGLAFKPDIDDLRESPAKYIVQRVLQD 341
Cdd:PLN02353  320 NTVSGKK--IAVLGFAFKKDTGDTRETPAIDVCKGLLGD 356
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
 5-394 1.36e-20

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 92.78  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522   5 EVNILGLGYIGLPTAALIAKNgTHVHGVDINKDVVETINNGKIHIVEPDLGEAVsyAVSNGFLRASTEAALA--NTYLIV 82
Cdd:PRK15057    2 KITISGTGYVGLSNGLLIAQN-HEVVALDILPSRVAMLNDRISPIVDKEIQQFL--QSDKIHFNATLDKNEAyrDADYVI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  83 VPTPfkNNHEP-----DISFVESATENIIPlLKKGDTYIIESTSPVGTTEKMmhliyekRPELKGEVFIaYCPERVLPGN 157
Cdd:PRK15057   79 IATP--TDYDPktnyfNTSSVESVIKDVVE-INPYAVMVIKSTVPVGFTAAM-------HKKYRTENII-FSPEFLREGK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 158 VMYELVHNDRVIGGvdeKSTKKAVEFYRKYVTGELHE------TNARTAEMCKLVENSSRDVQIAFANELSLICDKADID 231
Cdd:PRK15057  148 ALYDNLHPSRIVIG---ERSERAERFAALLQEGAIKQniptlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLN 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 232 VWELINLANKHPRV--NILQPGCGVGGHCIAVDPYFIVAEY-PMESRIIGKAREVNNYKSFWCAEKIVStklefelrhgR 308
Cdd:PRK15057  225 TRQIIEGVCLDPRIgnHYNNPSFGYGGYCLPKDTKQLLANYqSVPNNLISAIVDANRTRKDFIADAILS----------R 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 309 KPK-IALLGLAFKPDIDDLRESPAKYIVQRVlqDSNNEDYYIVEPNIDNHNVFK------LTEFTvavKEADIIvilVAH 381
Cdd:PRK15057  295 KPQvVGIYRLIMKSGSDNFRASSIQGIMKRI--KAKGVEVIIYEPVMKEDSFFNsrlerdLATFK---QQADVI---ISN 366

                         410
                  ....*....|...
gi 1519667522 382 KEFKQLTELENKV 394
Cdd:PRK15057  367 RMAEELKDVADKV 379
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 313-403 2.26e-17

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 76.78  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522  313 ALLGLAFKPDIDDLRESPAKYIVQRvLQDSNNE-DYY--IVEPNIDNHNVFKLTEFTVAVKEADIIVILVAHKEFKQLTE 389
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEE-LLEAGAEvVVYdpYAMEEAREYGLTYVSDLEEALKGADAVVIATEHDEFRSLDP 79

                           90       100
                   ....*....|....*....|
gi 1519667522  390 ------LENKVVLDFSGALK 403
Cdd:smart00984  80 eelkdlMKKPVVVDGRNILD 99
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 313-404 1.28e-15

UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 427462 [Multi-domain]  Cd Length: 103  Bit Score: 72.22  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519667522 313 ALLGLAFKPDIDDLRESPAKYIVQRVLQDSNNEDYY--IVEPNIDNHNVFKLT---EFTVAVKEADIIVILVAHKEFKQL 387
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYdpYVPEEAIEALGDGVTlvdDLEEALKGADAIVILTDHDEFKSL 80

                          90       100
                  ....*....|....*....|...
gi 1519667522 388 TE------LENKVVLDFSGALKK 404
Cdd:pfam03720  81 DWeklkklMKPPVVFDGRNVLDP 103
 
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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