|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-459 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 805.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCPDIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADL 80
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 81 IFISVNTPTKTCGNGKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMHILRANQKpGIHYDILSNPEFLA 160
Cdd:PLN02353 82 VFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 161 EGTAINDLLNADRVLIGGEETPEGHQAVEKLSWIYEHWIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVCEAT 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 241 GADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPEVAAYWQQVIDMNEYQKRRFSQKIIESLFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 321 TVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIIDDLT-------HP--SVTESPEKVkKA 391
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSmnkfdwdHPrhLQPMSPTAV-KQ 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266945 392 VQIHSDPYSAVRATHALVICTEWDEFVDLDFKRIYQSMMKPAYIFDGRKILDHERLQQIGFHVQTIGK 459
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGK 467
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-460 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 561.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCPDIVItlVDKSSERIAQWNSDKLPIYEPGLDEVVKkcRNV---NLFFSTDIETAIKE 77
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAELGHEVTC--VDIDEEKIEALNAGEIPIYEPGLEELVA--RNVaagRLRFTTDLAEAVAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 78 ADLIFISVNTPTKTCGngkgrAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESI-MHILRANQKPGIHYDILSNP 156
Cdd:COG1004 77 ADVVFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVrAIIAEELRGAGVDFDVVSNP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 157 EFLAEGTAINDLLNADRVLIGGEetpeGHQAVEKLSWIYEHWIPKQN-ILTTNTWSSELSKLAANAFLAQRISSINSLSA 235
Cdd:COG1004 152 EFLREGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGTpIIVTDLRSAELIKYAANAFLATKISFINEIAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 236 VCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPevAAYWQQVIDMNEYQKRRFSQKII 315
Cdd:COG1004 228 LCEKVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 316 ESLFNTVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPeqiiddlthpsvtESPEKVKKAVQIH 395
Cdd:COG1004 306 EHLGGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAME-------------NARRLLPDDITYA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2266945 396 SDPYSAVRATHALVICTEWDEFVDLDFKRIYQSMMKPAyIFDGRKILDHERLQQIGFHVQTIGKK 460
Cdd:COG1004 373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-439 |
1.81e-118 |
|
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: 353.07 E-value: 1.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCPDIviTLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLF-FSTDIETAIKEAD 79
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDV--TGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 80 LIFISVNTPTKtcgngKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMH--ILRANQKPGIHYDILSNPE 157
Cdd:TIGR03026 79 VIIICVPTPLK-----EDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 158 FLAEGTAINDLLNADRVLIGgeETPEGHQAVEKLswiYEHwIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVC 237
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGG--ETEEAGEAVAEL---YSP-IIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 238 EATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENL--NLPEVAAywqqVIDMNEYQKRRFSQKII 315
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELgyNPELIEA----AREINDSQPDYVVEKIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 316 ESLFNtVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIiddlthpsvtespekvkKAVQIH 395
Cdd:TIGR03026 304 DLLGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEV-----------------KGLPSI 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2266945 396 SDPYSAVRATHALVICTEWDEFVDLDFKRIYqSMMKPAYIFDGR 439
Cdd:TIGR03026 366 DDLEEALKGADALVILTDHSEFKDLDLEKIK-DLMKGKVVVDTR 408
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-189 |
5.06e-85 |
|
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: 259.49 E-value: 5.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCpdIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADL 80
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 81 IFISVNTPTKTcgngKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAE-SIMHILRANQ-KPGIHYDILSNPEF 158
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGGkKVGVDFDVASNPEF 154
|
170 180 190
....*....|....*....|....*....|.
gi 2266945 159 LAEGTAINDLLNADRVLIGGEETPEGHQAVE 189
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAALEE 185
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
328-443 |
4.71e-30 |
|
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: 112.60 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 328 AILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEpeqiiddlthpsvtesPEKVKKAVQIHSDPYSAVRATHA 407
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAM----------------EEAREYGLTYVSDLEEALKGADA 64
|
90 100 110
....*....|....*....|....*....|....*.
gi 2266945 408 LVICTEWDEFVDLDFKRIyQSMMKPAYIFDGRKILD 443
Cdd:smart00984 65 VVIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-459 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 805.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCPDIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADL 80
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 81 IFISVNTPTKTCGNGKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMHILRANQKpGIHYDILSNPEFLA 160
Cdd:PLN02353 82 VFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 161 EGTAINDLLNADRVLIGGEETPEGHQAVEKLSWIYEHWIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVCEAT 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 241 GADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPEVAAYWQQVIDMNEYQKRRFSQKIIESLFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 321 TVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIIDDLT-------HP--SVTESPEKVkKA 391
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSmnkfdwdHPrhLQPMSPTAV-KQ 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266945 392 VQIHSDPYSAVRATHALVICTEWDEFVDLDFKRIYQSMMKPAYIFDGRKILDHERLQQIGFHVQTIGK 459
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGK 467
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-460 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 561.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCPDIVItlVDKSSERIAQWNSDKLPIYEPGLDEVVKkcRNV---NLFFSTDIETAIKE 77
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAELGHEVTC--VDIDEEKIEALNAGEIPIYEPGLEELVA--RNVaagRLRFTTDLAEAVAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 78 ADLIFISVNTPTKTCGngkgrAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESI-MHILRANQKPGIHYDILSNP 156
Cdd:COG1004 77 ADVVFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVrAIIAEELRGAGVDFDVVSNP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 157 EFLAEGTAINDLLNADRVLIGGEetpeGHQAVEKLSWIYEHWIPKQN-ILTTNTWSSELSKLAANAFLAQRISSINSLSA 235
Cdd:COG1004 152 EFLREGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGTpIIVTDLRSAELIKYAANAFLATKISFINEIAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 236 VCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPevAAYWQQVIDMNEYQKRRFSQKII 315
Cdd:COG1004 228 LCEKVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 316 ESLFNTVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPeqiiddlthpsvtESPEKVKKAVQIH 395
Cdd:COG1004 306 EHLGGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAME-------------NARRLLPDDITYA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2266945 396 SDPYSAVRATHALVICTEWDEFVDLDFKRIYQSMMKPAyIFDGRKILDHERLQQIGFHVQTIGKK 460
Cdd:COG1004 373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-439 |
1.81e-118 |
|
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: 353.07 E-value: 1.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCPDIviTLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLF-FSTDIETAIKEAD 79
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDV--TGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 80 LIFISVNTPTKtcgngKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMH--ILRANQKPGIHYDILSNPE 157
Cdd:TIGR03026 79 VIIICVPTPLK-----EDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 158 FLAEGTAINDLLNADRVLIGgeETPEGHQAVEKLswiYEHwIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVC 237
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGG--ETEEAGEAVAEL---YSP-IIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 238 EATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENL--NLPEVAAywqqVIDMNEYQKRRFSQKII 315
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELgyNPELIEA----AREINDSQPDYVVEKIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 316 ESLFNtVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIiddlthpsvtespekvkKAVQIH 395
Cdd:TIGR03026 304 DLLGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEV-----------------KGLPSI 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2266945 396 SDPYSAVRATHALVICTEWDEFVDLDFKRIYqSMMKPAYIFDGR 439
Cdd:TIGR03026 366 DDLEEALKGADALVILTDHSEFKDLDLEKIK-DLMKGKVVVDTR 408
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-189 |
5.06e-85 |
|
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: 259.49 E-value: 5.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTCAVMALKCpdIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADL 80
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 81 IFISVNTPTKTcgngKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAE-SIMHILRANQ-KPGIHYDILSNPEF 158
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGGkKVGVDFDVASNPEF 154
|
170 180 190
....*....|....*....|....*....|.
gi 2266945 159 LAEGTAINDLLNADRVLIGGEETPEGHQAVE 189
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAALEE 185
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
2-443 |
4.33e-54 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 186.42 E-value: 4.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 2 KVCCIGAGYVGGPTCAVMALKCPDiVITlVDKSSERIAQWNSDKLPIYEPGlDEVVKKC-RNVNLFFSTDIEtAIKEADL 80
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAGFR-VIG-FDINPERVEELNAGEDPILEPG-DELLAEAvAAGRLRATTDPE-ALAEADV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 81 IFISVNTPTKtcgngKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIM--HI-----LRANQKPGIHYdil 153
Cdd:COG0677 77 VIIAVPTPLD-----EDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCvpILekrsgLKAGEDFFLAY--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 154 sNPEFLAEGTAINDLLNADRVlIGGEeTPEGHQAVEKLswiYEHWIPKQNILTTNTWSSELSKLAANAFLAQRISSINSL 233
Cdd:COG0677 149 -SPERINPGNKLHELRNIPKV-VGGI-TPESAERAAAL---YGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 234 SAVCEATGADVSEVARAVGldSRIGSKFLQASVGFGGSCFQKDILNLIYicenlNLPEVAaYWQQVIDM----NEYQKRR 309
Cdd:COG0677 223 ALICDRLGIDVWEVIEAAN--TKPGFLIFYPGPGVGGHCIPVDPYYLTW-----KARELG-YHPRLILAareiNDSMPEY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 310 FSQKIIESLFN---TVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQiIDDLTHPSVTESPe 386
Cdd:COG0677 295 VVERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEE-VEGEYGELVDLEE- 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2266945 387 kvkkavqihsdpysAVRATHALVICTEWDEFVDLDFKRIyqSMMKPAYIFDGRKILD 443
Cdd:COG0677 373 --------------ALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
211-304 |
1.78e-42 |
|
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: 145.60 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 211 SSELSKLAANAFLAQRISSINSLSAVCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLP 290
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|....
gi 2266945 291 evAAYWQQVIDMNE 304
Cdd:pfam00984 81 --ARLLEAAREVNE 92
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
328-444 |
1.06e-34 |
|
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: 125.38 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 328 AILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIIDDLTHpsvtespekvkkaVQIHSDPYSAVRATHA 407
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDG-------------VTLVDDLEEALKGADA 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 2266945 408 LVICTEWDEFVDLDFKRIYQsMMKPAYIFDGRKILDH 444
Cdd:pfam03720 68 IVILTDHDEFKSLDWEKLKK-LMKPPVVFDGRNVLDP 103
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
328-443 |
4.71e-30 |
|
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: 112.60 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 328 AILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEpeqiiddlthpsvtesPEKVKKAVQIHSDPYSAVRATHA 407
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAM----------------EEAREYGLTYVSDLEEALKGADA 64
|
90 100 110
....*....|....*....|....*....|....*.
gi 2266945 408 LVICTEWDEFVDLDFKRIyQSMMKPAYIFDGRKILD 443
Cdd:smart00984 65 VVIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
1-370 |
1.05e-27 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 113.96 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVG---GPTCA----VMALkcpDIVITLVDKSSERIAqwnsdklPIYEPGLDEVVKKcRNVNLFFSTDIET 73
Cdd:PRK15057 1 MKITISGTGYVGlsnGLLIAqnheVVAL---DILPSRVAMLNDRIS-------PIVDKEIQQFLQS-DKIHFNATLDKNE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 74 AIKEADLIFISvnTPTKTcgNGKGRAADLKYVESAARMIAEIAQSNKIVVeKSTVPVRAAESIMHILRANqkpgihyDIL 153
Cdd:PRK15057 70 AYRDADYVIIA--TPTDY--DPKTNYFNTSSVESVIKDVVEINPYAVMVI-KSTVPVGFTAAMHKKYRTE-------NII 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 154 SNPEFLAEGTAINDLLNADRVLIGgeetpEGHQAVEKLSWIYEHWIPKQNILT--TNTWSSELSKLAANAFLAQRISSIN 231
Cdd:PRK15057 138 FSPEFLREGKALYDNLHPSRIVIG-----ERSERAERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 232 SLSAVCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPEVAAywqqVIDMNEYQKRRFS 311
Cdd:PRK15057 213 ELDSYAESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQSVPNNLISA----IVDANRTRKDFIA 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2266945 312 QKIIESlfntvSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPE 370
Cdd:PRK15057 289 DAILSR-----KPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKED 342
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
2-427 |
4.35e-26 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 109.69 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 2 KVCCIGAGYVGGPTCAVMAlKCPDIVITlVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTdieTAIKEADLI 81
Cdd:PRK11064 5 TISVIGLGYIGLPTAAAFA-SRQKQVIG-VDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRAT---TTPEPADAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 82 FISVNTPTKtcgngKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMHILRAN-------QKPGIHYDIls 154
Cdd:PRK11064 80 LIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEArpdltfpQQAGEQADI-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 155 N----PEFLAEGTAINDLLNADRVlIGGeETPE-GHQAVEklswIYEHWIPKQNILtTNTWSSELSKLAANAFLAQRISS 229
Cdd:PRK11064 153 NiaycPERVLPGQVMVELIKNDRV-IGG-MTPVcSARASE----LYKIFLEGECVV-TNSRTAEMCKLTENSFRDVNIAF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 230 INSLSAVCEATGADVSEVARAVGLDSRIgsKFLQASVGFGGSCFQKD---IL-------NLIYICENLNlpEVAAYWqqV 299
Cdd:PRK11064 226 ANELSLICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDpwfIVaqnpqqaRLIRTAREVN--DGKPHW--V 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 300 IDmneyqkrRFSQKIIESLfnTVSDKR-----IAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYdpkVEpeqiid 374
Cdd:PRK11064 300 ID-------QVKAAVADCL--AATDKRasevkIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLV---VE------ 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2266945 375 dlthPSVTESPEKVKKAVQIHSDPYSAVRAThALVICTEWDEFVDLDFKRIYQ 427
Cdd:PRK11064 362 ----PNIHQLPKKLDGLVTLVSLDEALATAD-VLVMLVDHSQFKAINGDNVHQ 409
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
1-372 |
1.06e-15 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 78.96 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 1 MKVCCIGAGYVGGPTcAVMALKCPDIVITLVDKssERIAQWNsDKLPIYEPGLDEVVKKCRNvnLFFSTDIETaIKEADL 80
Cdd:PRK15182 7 VKIAIIGLGYVGLPL-AVEFGKSRQVVGFDVNK--KRILELK-NGVDVNLETTEEELREARY--LKFTSEIEK-IKECNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 81 IFISVNTPTKTCgngkgRAADLKYVESAARMIAEIAQSNKIVVEKSTV-PVRAAESIMHILRANQKPGIHYD--ILSNPE 157
Cdd:PRK15182 80 YIITVPTPINTY-----KQPDLTPLIKASETVGTVLNRGDIVVYESTVyPGCTEEECVPILARMSGMTFNQDfyVGYSPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 158 FLAEGTAINDLLNADRVLIGGEEtpeghQAVEKLSWIYehwipkQNILTTNTWSSELSKLAANAFL---AQR---ISSIN 231
Cdd:PRK15182 155 RINPGDKKHRLTNIKKITSGSTA-----QIAELIDEVY------QQIISAGTYKAESIKVAEAAKVienTQRdlnIALVN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266945 232 SLSAVCEATGADVSEVARAVGldsrigSK--FLQASVGF-GGSCFQKDILNLIYICENLNL-PEVAAYWQQVID-MNEYQ 306
Cdd:PRK15182 224 ELAIIFNRLNIDTEAVLRAAG------SKwnFLPFRPGLvGGHCIGVDPYYLTHKSQGIGYyPEIILAGRRLNDnMGNYV 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2266945 307 KRRFSQKIIESLFNtVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQI 372
Cdd:PRK15182 298 SEQLIKAMIKKGIN-VEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEV 362
|
|
| |
