|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-474 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 1051.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 1 MVKICCIGAGYVGGPTMAVMALKCPEIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLFFSTDVEKHVFESD 80
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 81 IVFVSVNTPTKTQGLGAGKAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEKILTHNSKGIEFQILSNPEFLA 160
Cdd:PLN02353 81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 161 EGTAIKDLYNPDRVLIGGRDTAAGQKAIKALRDVYAHWVPVEQIICTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 241 GADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLPEAANYWKQVVKVNDYQKIRFANRVVSSMFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 321 TVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDLSMARFDWDHPVPLQQiKAEGISEQ 400
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRHLQP-MSPTAVKQ 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222735 401 VNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPAFVFDGRNVVDAVKLREIGFIVYSIGKPLDSWL 474
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
3-469 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 573.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKCPEieVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCR-GKNLFFSTDVEKHVFESDI 81
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 82 VFVSVNTPTKTQGlgagkAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEKILTHNSK--GIEFQILSNPEFL 159
Cdd:COG1004 80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRgaGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 160 AEGTAIKDLYNPDRVLIGGRDtaagQKAIKALRDVYAHWVPVE-QIICTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVDS----ERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 239 ATGADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLPeaANYWKQVVKVNDYQKIRFANRVVSSM 318
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 319 FNTVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRdlsmarfdwdhpvplqqikaegIS 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRL----------------------LP 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222735 399 EQVNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPAfVFDGRNVVDAVKLREIGFIVYSIGKP 469
Cdd:COG1004 367 DDITYADDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
3-449 |
3.66e-115 |
|
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: 344.98 E-value: 3.66e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKcpEIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLF-FSTDVEKHVFESDI 81
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 82 VFVSVNTPTKTQGlgagkAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEK-ILTHNSK--GIEFQILSNPEF 158
Cdd:TIGR03026 80 IIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpILERSGLklGEDFYLAYNPEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 159 LAEGTAIKDLYNPDRVlIGGRDTAAGQKaikaLRDVYAHWVPVEqIICTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:TIGR03026 155 LREGNAVHDLLHPDRI-VGGETEEAGEA----VAELYSPIIDGP-VLVTSIETAEMIKLAENTFRAVKIAFANELARICE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 239 ATGADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLPeaANYWKQVVKVNDYQKIRFANRVVSSM 318
Cdd:TIGR03026 229 ALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 319 FNtVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDlsmarfdwdhpvplqqikaegis 398
Cdd:TIGR03026 307 GP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGL----------------------- 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15222735 399 eqvNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPaFVFDGRN 449
Cdd:TIGR03026 363 ---PSIDDLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGK-VVVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
3-189 |
6.82e-82 |
|
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: 251.40 E-value: 6.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKCpeIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLFFSTDVEKHVFESDIV 82
Cdd:pfam03721 2 KISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 83 FVSVNTPTKTQglgaGKAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAE-AIEKILTHNSK--GIEFQILSNPEFL 159
Cdd:pfam03721 80 FIAVGTPSKKG----GGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGGKkvGVDFDVASNPEFL 155
|
170 180 190
....*....|....*....|....*....|
gi 15222735 160 AEGTAIKDLYNPDRVLIGGRDTAAGQKAIK 189
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAEAALEE 185
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
328-452 |
5.72e-31 |
|
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: 114.91 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 328 AILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDLSmarfdwdhpvplqqikaegiseqvnVVSDA 407
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLT-------------------------YVSDL 55
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15222735 408 YEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPaFVFDGRNVVD 452
Cdd:smart00984 56 EEALKGADAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-474 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 1051.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 1 MVKICCIGAGYVGGPTMAVMALKCPEIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLFFSTDVEKHVFESD 80
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 81 IVFVSVNTPTKTQGLGAGKAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEKILTHNSKGIEFQILSNPEFLA 160
Cdd:PLN02353 81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 161 EGTAIKDLYNPDRVLIGGRDTAAGQKAIKALRDVYAHWVPVEQIICTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
Cdd:PLN02353 161 EGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 241 GADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLPEAANYWKQVVKVNDYQKIRFANRVVSSMFN 320
Cdd:PLN02353 241 GADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 321 TVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDLSMARFDWDHPVPLQQiKAEGISEQ 400
Cdd:PLN02353 321 TVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRHLQP-MSPTAVKQ 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222735 401 VNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPAFVFDGRNVVDAVKLREIGFIVYSIGKPLDSWL 474
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGKPLDPWL 473
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
3-469 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 573.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKCPEieVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCR-GKNLFFSTDVEKHVFESDI 81
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 82 VFVSVNTPTKTQGlgagkAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEKILTHNSK--GIEFQILSNPEFL 159
Cdd:COG1004 80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRgaGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 160 AEGTAIKDLYNPDRVLIGGRDtaagQKAIKALRDVYAHWVPVE-QIICTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVDS----ERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 239 ATGADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLPeaANYWKQVVKVNDYQKIRFANRVVSSM 318
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 319 FNTVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRdlsmarfdwdhpvplqqikaegIS 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRL----------------------LP 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222735 399 EQVNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPAfVFDGRNVVDAVKLREIGFIVYSIGKP 469
Cdd:COG1004 367 DDITYADDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
3-449 |
3.66e-115 |
|
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: 344.98 E-value: 3.66e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKcpEIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLF-FSTDVEKHVFESDI 81
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 82 VFVSVNTPTKTQGlgagkAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEK-ILTHNSK--GIEFQILSNPEF 158
Cdd:TIGR03026 80 IIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpILERSGLklGEDFYLAYNPEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 159 LAEGTAIKDLYNPDRVlIGGRDTAAGQKaikaLRDVYAHWVPVEqIICTNLWSAELSKLAANAFLAQRISSVNAMSALCE 238
Cdd:TIGR03026 155 LREGNAVHDLLHPDRI-VGGETEEAGEA----VAELYSPIIDGP-VLVTSIETAEMIKLAENTFRAVKIAFANELARICE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 239 ATGADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLPeaANYWKQVVKVNDYQKIRFANRVVSSM 318
Cdd:TIGR03026 229 ALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDLL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 319 FNtVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDlsmarfdwdhpvplqqikaegis 398
Cdd:TIGR03026 307 GP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGL----------------------- 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15222735 399 eqvNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPaFVFDGRN 449
Cdd:TIGR03026 363 ---PSIDDLEEALKGADALVILTDHSEFKDLDLEKIKDLMKGK-VVVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
3-189 |
6.82e-82 |
|
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: 251.40 E-value: 6.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKCpeIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLFFSTDVEKHVFESDIV 82
Cdd:pfam03721 2 KISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 83 FVSVNTPTKTQglgaGKAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAE-AIEKILTHNSK--GIEFQILSNPEFL 159
Cdd:pfam03721 80 FIAVGTPSKKG----GGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTEnLVKPIIEEGGKkvGVDFDVASNPEFL 155
|
170 180 190
....*....|....*....|....*....|
gi 15222735 160 AEGTAIKDLYNPDRVLIGGRDTAAGQKAIK 189
Cdd:pfam03721 156 REGSAVYDLFNPDRVVIGVTEKCAEAALEE 185
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
3-452 |
1.42e-59 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 201.06 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKCpeIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQCRGKNLFFSTDVEKhVFESDIV 82
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAG--FRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPEA-LAEADVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 83 FVSVNTPtktqgLGAGKAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAE-----AIEKI--LTHnskGIEFQILSN 155
Cdd:COG0677 78 IIAVPTP-----LDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEevcvpILEKRsgLKA---GEDFFLAYS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 156 PEFLAEGTAIKDLYNPDRVlIGGRDTAAGQKAikalRDVYAHWVPVEQIICTNLWSAELSKLAANAFLAQRISSVNAMSA 235
Cdd:COG0677 150 PERINPGNKLHELRNIPKV-VGGITPESAERA----AALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 236 LCEATGADVTQVAHAVGTDTRI-----GPkflnasvGFGGSCFQKDILNLIYICECNGLP----EAANywkqvvKVNDYQ 306
Cdd:COG0677 225 ICDRLGIDVWEVIEAANTKPGFlifypGP-------GVGGHCIPVDPYYLTWKARELGYHprliLAAR------EINDSM 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 307 KIRFANRVVSSMFN---TVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRdlsmarfdw 383
Cdd:COG0677 292 PEYVVERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEG--------- 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222735 384 dhpvplqqikaegiseQVNVVSDAYEATKDAHGLCVLTEWDEFKSLDFKKIfdNMQKPAFVFDGRNVVD 452
Cdd:COG0677 363 ----------------EYGELVDLEEALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
211-304 |
4.02e-43 |
|
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: 147.14 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 211 SAELSKLAANAFLAQRISSVNAMSALCEATGADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIYICECNGLP 290
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|....
gi 15222735 291 eaANYWKQVVKVND 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 ... |
328-453 |
3.66e-35 |
|
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: 126.54 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 328 AILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDLsmarfdwdhpvplqqikaegisEQVNVVSDA 407
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALG----------------------DGVTLVDDL 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15222735 408 YEATKDAHGLCVLTEWDEFKSLDFKKIFDNMqKPAFVFDGRNVVDA 453
Cdd:pfam03720 59 EEALKGADAIVILTDHDEFKSLDWEKLKKLM-KPPVVFDGRNVLDP 103
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
328-452 |
5.72e-31 |
|
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: 114.91 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 328 AILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDLSmarfdwdhpvplqqikaegiseqvnVVSDA 407
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLT-------------------------YVSDL 55
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15222735 408 YEATKDAHGLCVLTEWDEFKSLDFKKIFDNMQKPaFVFDGRNVVD 452
Cdd:smart00984 56 EEALKGADAVVIATEHDEFRSLDPEELKDLMKKP-VVVDGRNILD 99
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
2-377 |
1.20e-28 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 116.66 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 2 VKICCIGAGYVGGPTMAVMAlkcPEIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQcrgKNLFFSTDVEKHVFESDI 81
Cdd:PRK15057 1 MKITISGTGYVGLSNGLLIA---QNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQS---DKIHFNATLDKNEAYRDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 82 VFVSVNTPT----KTQGLGAgkaadltywESAARMIADVSK--SSKIVVEKSTVPVR-TAEAIEKILTHNskgiefqILS 154
Cdd:PRK15057 75 DYVIIATPTdydpKTNYFNT---------SSVESVIKDVVEinPYAVMVIKSTVPVGfTAAMHKKYRTEN-------IIF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 155 NPEFLAEGTAIKDLYNPDRVLIGGRDTAAGQKAIKALRDVYAHWVPVeqiICTNLWSAELSKLAANAFLAQRISSVNAMS 234
Cdd:PRK15057 139 SPEFLREGKALYDNLHPSRIVIGERSERAERFAALLQEGAIKQNIPT---LFTDSTEAEAIKLFANTYLAMRVAYFNELD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 235 ALCEATGADVTQVAHAVGTDTRIGPKFLNASVGFGGSCFQKDILNLIyicecnglpeaANYwkQVVKVNDYQKIRFANRV 314
Cdd:PRK15057 216 SYAESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLL-----------ANY--QSVPNNLISAIVDANRT 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222735 315 ----VSSMFNTVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEE-----QIRRDLS 377
Cdd:PRK15057 283 rkdfIADAILSRKPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKEDsffnsRLERDLA 354
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
3-356 |
1.22e-28 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 117.01 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 3 KICCIGAGYVGGPTMAVMALKcpEIEVVVVDISEPRINAWNSDRLPIYEPGLEDVVKQC-RGKNLFFSTDVEkhvfESDI 81
Cdd:PRK11064 5 TISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAvEGGYLRATTTPE----PADA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 82 VFVSVNTPTKtqglgAGKAADLTYWESAARMIADVSKSSKIVVEKSTVPVRTAEAIEKILTHNSKGIEF----------Q 151
Cdd:PRK11064 79 FLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFpqqageqadiN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 152 ILSNPEFLAEGTAIKDLYNPDRVlIGGRDTAAGQKAikalRDVYAHWVPVEQIIcTNLWSAELSKLAANAFLAQRISSVN 231
Cdd:PRK11064 154 IAYCPERVLPGQVMVELIKNDRV-IGGMTPVCSARA----SELYKIFLEGECVV-TNSRTAEMCKLTENSFRDVNIAFAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 232 AMSALCEATGADVTQVAHAVGTDTRIgpKFLNASVGFGGSCFQKDILnliYICECNglPEAANYWKQVVKVNDYQKIRFA 311
Cdd:PRK11064 228 ELSLICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPW---FIVAQN--PQQARLIRTAREVNDGKPHWVI 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15222735 312 NRVVSSM--FNTVSGK-----KIAILGFAFKKDTGDTRETPAIDVCnRLVAD 356
Cdd:PRK11064 301 DQVKAAVadCLAATDKrasevKIACFGLAFKPNIDDLRESPAMEIA-ELIAQ 351
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
2-394 |
2.10e-18 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 87.05 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 2 VKICCIGAGYVGGPtMAVMALKCPEieVVVVDISEPRINAWNSDrlpiYEPGLEDVVKQCR-GKNLFFSTDVEKhVFESD 80
Cdd:PRK15182 7 VKIAIIGLGYVGLP-LAVEFGKSRQ--VVGFDVNKKRILELKNG----VDVNLETTEEELReARYLKFTSEIEK-IKECN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 81 IVFVSVNTPTKTQglgagKAADLTYWESAARMIADVSKSSKIVVEKSTV-PVRTAEAIEKILTHNSK---GIEFQILSNP 156
Cdd:PRK15182 79 FYIITVPTPINTY-----KQPDLTPLIKASETVGTVLNRGDIVVYESTVyPGCTEEECVPILARMSGmtfNQDFYVGYSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 157 EFLAEGTAIKDLYNPDRVLIGGRDTAAgqkaiKALRDVYahwvpvEQIICTNLWSAELSKLAANAFL---AQR---ISSV 230
Cdd:PRK15182 154 ERINPGDKKHRLTNIKKITSGSTAQIA-----ELIDEVY------QQIISAGTYKAESIKVAEAAKVienTQRdlnIALV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 231 NAMSALCEATGADVTQVAHAVGTDTRIGPkFLNASVGfgGSCFQKDILNLIYICECNGlpeaanYWKQVV----KVNDYQ 306
Cdd:PRK15182 223 NELAIIFNRLNIDTEAVLRAAGSKWNFLP-FRPGLVG--GHCIGVDPYYLTHKSQGIG------YYPEIIlagrRLNDNM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222735 307 KIRFANRVVSSMFN---TVSGKKIAILGFAFKKDTGDTRETPAIDVCNRLVADKAKLSIYDPQVLEEQIRRDLSMarfdw 383
Cdd:PRK15182 294 GNYVSEQLIKAMIKkgiNVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRREYGI----- 368
|
410
....*....|.
gi 15222735 384 dhpVPLQQIKA 394
Cdd:PRK15182 369 ---IPVSEVKS 376
|
|
| |
