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Conserved domains on  [gi|547919904|ref|WP_022322291|]
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MULTISPECIES: UDP-N-acetyl-D-mannosamine dehydrogenase [Parabacteroides]

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)

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
7-394 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: 567.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   7 GLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKASDVPEESDVYLIVVPTPFKG 86
Cdd:PRK11064  10 GLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAVPTPFKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  87 NHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPEL--------EGKIYIAYCPERVLPGNVIYE 158
Cdd:PRK11064  90 DHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqageQADINIAYCPERVLPGQVMVE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 159 LMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIELANK 238
Cdd:PRK11064 170 LIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIRLANR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 239 HPRVNILQPGSGVGGHCIAVDPYFLTSEFPYESQLISKAREINNYKAFWCAEKIENAILRFFLEHHRK---PVVALMGLS 315
Cdd:PRK11064 250 HPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRaseVKIACFGLA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 316 FKPDIDDLRESPAKYITSKVLQRSADTdILIVEPNVHEHPV-----FKLTDYKSAYTRADIVAFLVSHKEFKTLPHNE-- 388
Cdd:PRK11064 330 FKPNIDDLRESPAMEIAELIAQWHSGE-TLVVEPNIHQLPKkldglVTLVSLDEALATADVLVMLVDHSQFKAINGDNvh 408

                 ....*.
gi 547919904 389 EKVILD 394
Cdd:PRK11064 409 QQWVVD 414
 
Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
7-394 0e+00

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 567.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   7 GLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKASDVPEESDVYLIVVPTPFKG 86
Cdd:PRK11064  10 GLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAVPTPFKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  87 NHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPEL--------EGKIYIAYCPERVLPGNVIYE 158
Cdd:PRK11064  90 DHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqageQADINIAYCPERVLPGQVMVE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 159 LMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIELANK 238
Cdd:PRK11064 170 LIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIRLANR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 239 HPRVNILQPGSGVGGHCIAVDPYFLTSEFPYESQLISKAREINNYKAFWCAEKIENAILRFFLEHHRK---PVVALMGLS 315
Cdd:PRK11064 250 HPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRaseVKIACFGLA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 316 FKPDIDDLRESPAKYITSKVLQRSADTdILIVEPNVHEHPV-----FKLTDYKSAYTRADIVAFLVSHKEFKTLPHNE-- 388
Cdd:PRK11064 330 FKPNIDDLRESPAMEIAELIAQWHSGE-TLVVEPNIHQLPKkldglVTLVSLDEALATADVLVMLVDHSQFKAINGDNvh 408

                 ....*.
gi 547919904 389 EKVILD 394
Cdd:PRK11064 409 QQWVVD 414
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-400 0e+00

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 516.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   2 KACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGlQELCSKVMEFGKLKASDVPE---ESDVYLI 78
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEalaEADVVII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  79 VVPTPFKGNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELE-GK-IYIAYCPERVLPGNVI 156
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKaGEdFFLAYSPERINPGNKL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 157 YELMQNDRVIGGINSESTEKAIQFYRHFVRGTLHR-TNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIEL 235
Cdd:COG0677  160 HELRNIPKVVGGITPESAERAAALYGSVVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 236 ANKHPRVNILQPGSGVGGHCIAVDPYFLTS---EFPYESQLISKAREINNYKAFWCAEKIENAilrffLEHHRKPV---- 308
Cdd:COG0677  240 ANTKPGFLIFYPGPGVGGHCIPVDPYYLTWkarELGYHPRLILAAREINDSMPEYVVERVVKA-----LNEAGKSLkgar 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 309 VALMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNVHEHPV----FKLTDYKSAYTRADIVAFLVSHKEFKTL 384
Cdd:COG0677  315 VLVLGLAYKENVDDLRESPALDIIEELREYGA--EVDVHDPYVDEEEVegeyGELVDLEEALEGADAVVLAVDHDEFDEL 392
                        410       420
                 ....*....|....*....|.
gi 547919904 385 P-----HNEEKVILDFCGVFK 400
Cdd:COG0677  393 DpeelrLKGAKVVVDTRGVLD 413
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-394 1.60e-133

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: 388.89  E-value: 1.60e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904    1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKAS----DVPEESDVY 76
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATtdyeEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   77 LIVVPTPFKGNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEGK-IYIAYCPERVLPGNV 155
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEdFYLAYNPEFLREGNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  156 IYELMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIEL 235
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  236 ANKHPR--VNILQPGSGVGGHCIAVDPYFLTS---EFPYESQLISKAREINNYKAFWCAEKIENAilrffLEHHRKPVVA 310
Cdd:TIGR03026 241 AGTDPRigFNFLNPGPGVGGHCIPKDPLALIAkakELGYNPELIEAAREINDSQPDYVVEKIKDL-----LGPLKGKTVL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  311 LMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNVHEHPVFKLTDYKSAY---TRADIVAFLVSHKEFKTLPH- 386
Cdd:TIGR03026 316 ILGLAFKPNTDDVRESPALDIIELLKEKGA--KVKAYDPLVPEEEVKGLPSIDDLEealKGADALVILTDHSEFKDLDLe 393
                         410
                  ....*....|...
gi 547919904  387 -----NEEKVILD 394
Cdd:TIGR03026 394 kikdlMKGKVVVD 406
UDPMaNacDH_Arch NF040825
UDP-N-acetyl-D-mannosamine dehydrogenase;
1-401 7.74e-114

UDP-N-acetyl-D-mannosamine dehydrogenase;


Pssm-ID: 468765 [Multi-domain]  Cd Length: 418  Bit Score: 339.05  E-value: 7.74e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKASDVPEE---SDVYL 77
Cdd:NF040825   1 MKIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  78 IVVPTPFKGNhEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEGK-IYIAYCPERVLPGNVI 156
Cdd:NF040825  81 ICVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEELTGLKEGEdFYMAHAPERVMPGRIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 157 YELMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIELA 236
Cdd:NF040825 160 KELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNVFEAIELA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 237 NKHPRVNILQPGSGVGGHCIAVDPYFLTSEFPYESQLISKAREINNYKAFWCAEKIENAILRFFLEhHRKPVVALMGLSF 316
Cdd:NF040825 240 NTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLFAKDLLFEALEEANVP-PEEAVVTVLGLAY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 317 KPDIDDLRESPA----KYITSKVLQ-RSADtdilivePNV---HEhpvfkltDYKSAYTRADIVAFLVSHKEFKTLPHNE 388
Cdd:NF040825 319 KGDTDDTRNSPAlkfvELIEDDVKEvRTYD-------PYVggtHE-------SLEDAVKGADAIVIATDHSEFKSLNWEE 384
                        410
                 ....*....|....*....
gi 547919904 389 ------EKVILDFCGVFKK 401
Cdd:NF040825 385 lgklmrTKILIDGRHIIKE 403
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-179 6.96e-67

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: 210.57  E-value: 6.96e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904    1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVME---FGKLKASDVPEESDVYL 77
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSgrlSFTTDYSTAIEEADVIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   78 IVVPTPFK-GNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEG-KIYIAYCPERVLPGNV 155
Cdd:pfam03721  81 IAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGvDFDVASNPEFLREGSA 160
                         170       180
                  ....*....|....*....|....
gi 547919904  156 IYELMQNDRVIGGINSESTEKAIQ 179
Cdd:pfam03721 161 VYDLFNPDRVVIGVTEKCAEAALE 184
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
310-400 5.37e-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: 75.62  E-value: 5.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   310 ALMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNV----HEHPVFKLTDYKSAYTRADIVAFLVSHKEFKTLP 385
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGA--EVVVYDPYAmeeaREYGLTYVSDLEEALKGADAVVIATEHDEFRSLD 78
                           90       100
                   ....*....|....*....|.
gi 547919904   386 HNE------EKVILDFCGVFK 400
Cdd:smart00984  79 PEElkdlmkKPVVVDGRNILD 99
 
Name Accession Description Interval E-value
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
7-394 0e+00

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 567.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   7 GLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKASDVPEESDVYLIVVPTPFKG 86
Cdd:PRK11064  10 GLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAVPTPFKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  87 NHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPEL--------EGKIYIAYCPERVLPGNVIYE 158
Cdd:PRK11064  90 DHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqageQADINIAYCPERVLPGQVMVE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 159 LMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIELANK 238
Cdd:PRK11064 170 LIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIRLANR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 239 HPRVNILQPGSGVGGHCIAVDPYFLTSEFPYESQLISKAREINNYKAFWCAEKIENAILRFFLEHHRK---PVVALMGLS 315
Cdd:PRK11064 250 HPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRaseVKIACFGLA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 316 FKPDIDDLRESPAKYITSKVLQRSADTdILIVEPNVHEHPV-----FKLTDYKSAYTRADIVAFLVSHKEFKTLPHNE-- 388
Cdd:PRK11064 330 FKPNIDDLRESPAMEIAELIAQWHSGE-TLVVEPNIHQLPKkldglVTLVSLDEALATADVLVMLVDHSQFKAINGDNvh 408

                 ....*.
gi 547919904 389 EKVILD 394
Cdd:PRK11064 409 QQWVVD 414
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
2-400 0e+00

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 516.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   2 KACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGlQELCSKVMEFGKLKASDVPE---ESDVYLI 78
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEalaEADVVII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  79 VVPTPFKGNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELE-GK-IYIAYCPERVLPGNVI 156
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKaGEdFFLAYSPERINPGNKL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 157 YELMQNDRVIGGINSESTEKAIQFYRHFVRGTLHR-TNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIEL 235
Cdd:COG0677  160 HELRNIPKVVGGITPESAERAAALYGSVVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 236 ANKHPRVNILQPGSGVGGHCIAVDPYFLTS---EFPYESQLISKAREINNYKAFWCAEKIENAilrffLEHHRKPV---- 308
Cdd:COG0677  240 ANTKPGFLIFYPGPGVGGHCIPVDPYYLTWkarELGYHPRLILAAREINDSMPEYVVERVVKA-----LNEAGKSLkgar 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 309 VALMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNVHEHPV----FKLTDYKSAYTRADIVAFLVSHKEFKTL 384
Cdd:COG0677  315 VLVLGLAYKENVDDLRESPALDIIEELREYGA--EVDVHDPYVDEEEVegeyGELVDLEEALEGADAVVLAVDHDEFDEL 392
                        410       420
                 ....*....|....*....|.
gi 547919904 385 P-----HNEEKVILDFCGVFK 400
Cdd:COG0677  393 DpeelrLKGAKVVVDTRGVLD 413
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-394 1.60e-133

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: 388.89  E-value: 1.60e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904    1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKAS----DVPEESDVY 76
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATtdyeEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   77 LIVVPTPFKGNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEGK-IYIAYCPERVLPGNV 155
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEdFYLAYNPEFLREGNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  156 IYELMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIEL 235
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  236 ANKHPR--VNILQPGSGVGGHCIAVDPYFLTS---EFPYESQLISKAREINNYKAFWCAEKIENAilrffLEHHRKPVVA 310
Cdd:TIGR03026 241 AGTDPRigFNFLNPGPGVGGHCIPKDPLALIAkakELGYNPELIEAAREINDSQPDYVVEKIKDL-----LGPLKGKTVL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  311 LMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNVHEHPVFKLTDYKSAY---TRADIVAFLVSHKEFKTLPH- 386
Cdd:TIGR03026 316 ILGLAFKPNTDDVRESPALDIIELLKEKGA--KVKAYDPLVPEEEVKGLPSIDDLEealKGADALVILTDHSEFKDLDLe 393
                         410
                  ....*....|...
gi 547919904  387 -----NEEKVILD 394
Cdd:TIGR03026 394 kikdlMKGKVVVD 406
UDPMaNacDH_Arch NF040825
UDP-N-acetyl-D-mannosamine dehydrogenase;
1-401 7.74e-114

UDP-N-acetyl-D-mannosamine dehydrogenase;


Pssm-ID: 468765 [Multi-domain]  Cd Length: 418  Bit Score: 339.05  E-value: 7.74e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKASDVPEE---SDVYL 77
Cdd:NF040825   1 MKIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  78 IVVPTPFKGNhEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEGK-IYIAYCPERVLPGNVI 156
Cdd:NF040825  81 ICVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEELTGLKEGEdFYMAHAPERVMPGRIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 157 YELMQNDRVIGGINSESTEKAIQFYRHFVRGTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIELA 236
Cdd:NF040825 160 KELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNVFEAIELA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 237 NKHPRVNILQPGSGVGGHCIAVDPYFLTSEFPYESQLISKAREINNYKAFWCAEKIENAILRFFLEhHRKPVVALMGLSF 316
Cdd:NF040825 240 NTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLFAKDLLFEALEEANVP-PEEAVVTVLGLAY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 317 KPDIDDLRESPA----KYITSKVLQ-RSADtdilivePNV---HEhpvfkltDYKSAYTRADIVAFLVSHKEFKTLPHNE 388
Cdd:NF040825 319 KGDTDDTRNSPAlkfvELIEDDVKEvRTYD-------PYVggtHE-------SLEDAVKGADAIVIATDHSEFKSLNWEE 384
                        410
                 ....*....|....*....
gi 547919904 389 ------EKVILDFCGVFKK 401
Cdd:NF040825 385 lgklmrTKILIDGRHIIKE 403
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-394 7.98e-68

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 221.05  E-value: 7.98e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVMEFGKLKAS-DVPE---ESDVY 76
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTtDLAEavaEADVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  77 LIVVPTPFKGNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEGKIYIAYCPE--RvlPGN 154
Cdd:COG1004   81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGAGVDFDVVSNPEflR--EGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 155 VIYELMQNDR-VIGGINSESTEKAIQFYRHFVRGT--LHRTNARTAEMCKLTENS---SRdvqIAFANELSLICDKAGIN 228
Cdd:COG1004  159 AVEDFLRPDRiVIGVDSERAAEVLRELYAPFVRNGtpIIVTDLRSAELIKYAANAflaTK---ISFINEIANLCEKVGAD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 229 VWELIElANKH-PRvnI----LQPGSGVGGHCiavdpyfltseFP--------------YESQLISKAREINNYKAFWCA 289
Cdd:COG1004  236 VEEVAR-GIGLdSR--IgpkfLYAGIGYGGSC-----------FPkdvraliatarelgYDLRLLEAVEEVNERQKRRLV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 290 EKIENAiLRFFLEHHRkpvVALMGLSFKPDIDDLRESPAKYITSKVLQRSAD---TDIlIVEPNVHEHPVFKLTDYKSAY 366
Cdd:COG1004  302 EKIREH-LGGDLKGKT---IAVLGLAFKPNTDDMRESPALDIIEALLEAGARvraYDP-VAMENARRLLPDDITYADDAY 376
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 547919904 367 ---TRADIVAFLVSHKEFKTLPHNEEK------VILD 394
Cdd:COG1004  377 ealEGADALVILTEWPEFRALDFARLKalmkgpVIFD 413
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-179 6.96e-67

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: 210.57  E-value: 6.96e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904    1 MKACFMGLGYIGLPTAIIAAGSGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQELCSKVME---FGKLKASDVPEESDVYL 77
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSgrlSFTTDYSTAIEEADVIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   78 IVVPTPFK-GNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELEG-KIYIAYCPERVLPGNV 155
Cdd:pfam03721  81 IAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGvDFDVASNPEFLREGSA 160
                         170       180
                  ....*....|....*....|....
gi 547919904  156 IYELMQNDRVIGGINSESTEKAIQ 179
Cdd:pfam03721 161 VYDLFNPDRVVIGVTEKCAEAALE 184
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
1-384 2.63e-44

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 159.08  E-value: 2.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   1 MKACFMGLGYIGLPTAIiAAGSGIQVIGVDVNPK-VVEMTNRgiihiVEPGLQELCSKVMEFGKLKASDVPE---ESDVY 76
Cdd:PRK15182   7 VKIAIIGLGYVGLPLAV-EFGKSRQVVGFDVNKKrILELKNG-----VDVNLETTEEELREARYLKFTSEIEkikECNFY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  77 LIVVPTPFKGNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPEL--EGKIYIAYCPERVLPGN 154
Cdd:PRK15182  81 IITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMtfNQDFYVGYSPERINPGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 155 VIYELMQNDRVIGGINSESTEKAIQFYRHFVR-GTLHRTNARTAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELI 233
Cdd:PRK15182 161 KKHRLTNIKKITSGSTAQIAELIDEVYQQIISaGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 234 ELANKHPRVNILQPGSgVGGHCIAVDPYFLTSE---FPYESQLISKAREINNYKAFWCAEKIENAILRFFLEHHRKPVVa 310
Cdd:PRK15182 241 RAAGSKWNFLPFRPGL-VGGHCIGVDPYYLTHKsqgIGYYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSSVL- 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547919904 311 LMGLSFKPDIDDLRESPAKYITSKVLQRSADTDI----LIVEPNVHEHPVFKLTDYKSAYTRADIVAflVSHKEFKTL 384
Cdd:PRK15182 319 ILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIfdpwVDAEEVRREYGIIPVSEVKSSHYDAIIVA--VGHQQFKQM 394
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
196-282 3.77e-34

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: 122.10  E-value: 3.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  196 TAEMCKLTENSSRDVQIAFANELSLICDKAGINVWELIELANKHPR--VNILQPGSGVGGHCIAVDPYFLTS---EFPYE 270
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIYlarELGVP 80
                          90
                  ....*....|..
gi 547919904  271 SQLISKAREINN 282
Cdd:pfam00984  81 ARLLEAAREVNE 92
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
1-384 9.50e-29

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 117.08  E-value: 9.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   1 MKACFMGLGYIGLPT-AIIAAG-SGIQVIGVDVNPKVVEMTNRGIIHIVEPGLQEL---C-SKVMEFgklkASDVPE--- 71
Cdd:PLN02353   2 VKICCIGAGYVGGPTmAVIALKcPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVvkqCrGKNLFF----STDVEKhva 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  72 ESDVYLIVVPTPFK-----GNHEPDISYVEAATRMVAPFLKKGDLFVIESTSPVGTTEKMANLLYALRPELegKIYIAYC 146
Cdd:PLN02353  78 EADIVFVSVNTPTKtrglgAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGI--NFQILSN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 147 PERVLPGNVIYELMQNDRV-IGGINSESTEKAIQ----FYRHFV-RGTLHRTNARTAEMCKLTENSSRDVQIAFANELSL 220
Cdd:PLN02353 156 PEFLAEGTAIEDLFKPDRVlIGGRETPEGQKAVQalkdVYAHWVpEERIITTNLWSAELSKLAANAFLAQRISSVNAMSA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 221 ICDKAGINVWELIELANKHPRV--NILQPGSGVGGHCIAVD---------PYFLTSEFPYESQLISkareINNYKAFWCA 289
Cdd:PLN02353 236 LCEATGADVSQVSHAVGKDSRIgpKFLNASVGFGGSCFQKDilnlvyiceCNGLPEVAEYWKQVIK----MNDYQKSRFV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 290 EKIENAILRFFlehhRKPVVALMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNVHE---------------H 354
Cdd:PLN02353 312 NRVVSSMFNTV----SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKA--KLSIYDPQVTEeqiqrdlsmnkfdwdH 385
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 547919904 355 PVF----------KLTDYKSAYTRAD---IVAFLVSHKEFKTL 384
Cdd:PLN02353 386 PRHlqpmsptavkQVSVVWDAYEATKgahGICILTEWDEFKTL 428
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
1-391 1.92e-25

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 106.65  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   1 MKACFMGLGYIGLPTAIIAAGSGiQVIGVDVNPKVVEMTNRGIIHIVEPGLQE-LCSKVMEF-GKLKASDVPEESDVYLI 78
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIAQNH-EVVALDILPSRVAMLNDRISPIVDKEIQQfLQSDKIHFnATLDKNEAYRDADYVII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  79 VVPTpfkgNHEPDISY-----VEAATRMVAPfLKKGDLFVIESTSPVGTTEKMANllyALRPElegkiYIAYCPERVLPG 153
Cdd:PRK15057  80 ATPT----DYDPKTNYfntssVESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHK---KYRTE-----NIIFSPEFLREG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 154 NVIYELMQNDRVIGGinsESTEKAIQFYRHFVRGTLHR------TNARTAEMCKLTENSSRDVQIAFANELSLICDKAGI 227
Cdd:PRK15057 147 KALYDNLHPSRIVIG---ERSERAERFAALLQEGAIKQniptlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 228 NVWELIELANKHPRV--NILQPGSGVGGHCIAVDPYFLTSEF-PYESQLISKAREINNYKAFWCAEkienAILRfflehh 304
Cdd:PRK15057 224 NTRQIIEGVCLDPRIgnHYNNPSFGYGGYCLPKDTKQLLANYqSVPNNLISAIVDANRTRKDFIAD----AILS------ 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904 305 RKP-VVALMGLSFKPDIDDLRESPAKYITSKVlqRSADTDILIVEPNVHEHPVFK------LTDYKSaytRADIVaflVS 377
Cdd:PRK15057 294 RKPqVVGIYRLIMKSGSDNFRASSIQGIMKRI--KAKGVEVIIYEPVMKEDSFFNsrlerdLATFKQ---QADVI---IS 365
                        410
                 ....*....|....
gi 547919904 378 HKEFKTLPHNEEKV 391
Cdd:PRK15057 366 NRMAEELKDVADKV 379
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
310-400 5.37e-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: 75.62  E-value: 5.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904   310 ALMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNV----HEHPVFKLTDYKSAYTRADIVAFLVSHKEFKTLP 385
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGA--EVVVYDPYAmeeaREYGLTYVSDLEEALKGADAVVIATEHDEFRSLD 78
                           90       100
                   ....*....|....*....|.
gi 547919904   386 HNE------EKVILDFCGVFK 400
Cdd:smart00984  79 PEElkdlmkKPVVVDGRNILD 99
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
310-401 6.90e-13

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: 64.52  E-value: 6.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547919904  310 ALMGLSFKPDIDDLRESPAKYITSKVLQRSAdtDILIVEPNVHEHPVFKL-------TDYKSAYTRADIVAFLVSHKEFK 382
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGA--EVKVYDPYVPEEAIEALgdgvtlvDDLEEALKGADAIVILTDHDEFK 78
                          90       100
                  ....*....|....*....|....*
gi 547919904  383 TLP------HNEEKVILDFCGVFKK 401
Cdd:pfam03720  79 SLDweklkkLMKPPVVFDGRNVLDP 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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