|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-452 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 811.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKAPDIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLFFSTDVRSAIQAADI 80
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKTYGVGSGRAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAETIKDILAANARGVKFEVLSNPEFLAE 160
Cdd:PLN02353 82 VFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 161 GTAVEDLKQPDRVLIGGERTPGGEAAVQTLADVYARWVPRDRIITTNLWSSELSKLVANAFLAQRISSINSISALCEATG 240
Cdd:PLN02353 162 GTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 241 ADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYLCDHFALPEVSSYWENVVKMNDWQKRRFATKIVRALFNS 320
Cdd:PLN02353 242 ADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFNT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 321 VADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRELLGPDKQ--------------DSRLT 386
Cdd:PLN02353 322 VSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDwdhprhlqpmsptaVKQVS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501343915 387 VVKSAYAAAEGAHGLAVLTEWDEFKTLDFKRIFESMAKPACVFDGRNILSLEALKSLGFRVYGVGK 452
Cdd:PLN02353 402 VVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGK 467
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-452 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 592.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKAPDieVRVVDMNAARIASWNSDALPVYEPGLDDVVKEAR-GRNLFFSTDVRSAIQAAD 79
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 80 IVFVAVNTPTKTYGvgsgrAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAETIKDILAANAR--GVKFEVLSNPEF 157
Cdd:COG1004 79 VVFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRgaGVDFDVVSNPEF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 158 LAEGTAVEDLKQPDRVLIGGErtpgGEAAVQTLADVYARWVPR-DRIITTNLWSSELSKLVANAFLAQRISSINSISALC 236
Cdd:COG1004 154 LREGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNgTPIIVTDLRSAELIKYAANAFLATKISFINEIANLC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 237 EATGADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYLCDHFALPevSSYWENVVKMNDWQKRRFATKIVRA 316
Cdd:COG1004 230 EKVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 317 LFNSVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEdiRRELLGPDkqdsrLTVVKSAYAAAE 396
Cdd:COG1004 308 LGGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMEN--ARRLLPDD-----ITYADDAYEALE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 501343915 397 GAHGLAVLTEWDEFKTLDFKRIFESMAKPAcVFDGRNILSLEALKSLGFRVYGVGK 452
Cdd:COG1004 381 GADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGR 435
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-433 |
2.69e-116 |
|
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: 346.91 E-value: 2.69e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKApdIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLF-FSTDVRSAIQAAD 79
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLG--HDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 80 IVFVAVNTPTKTYGvgsgrAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAE-TIKDILAAN--ARGVKFEVLSNPE 156
Cdd:TIGR03026 79 VIIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEeVVKPILERSglKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 157 FLAEGTAVEDLKQPDRVlIGGErtpgGEAAVQTLADVYARWVpRDRIITTNLWSSELSKLVANAFLAQRISSINSISALC 236
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRI-VGGE----TEEAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 237 EATGADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYlcdhfALPEV---SSYWENVVKMNDWQKRRFATKI 313
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIA-----KAKELgynPELIEAAREINDSQPDYVVEKI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 314 VRALFNsVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRrellgpdkqdsRLTVVKSAYA 393
Cdd:TIGR03026 303 KDLLGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVK-----------GLPSIDDLEE 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501343915 394 AAEGAHGLAVLTEWDEFKTLDFKRIFESMAKPAcVFDGRN 433
Cdd:TIGR03026 371 ALKGADALVILTDHSEFKDLDLEKIKDLMKGKV-VVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-186 |
1.25e-72 |
|
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: 226.75 E-value: 1.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKApdIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLFFSTDVRSAIQAADI 80
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKTygvgSGRAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAET-IKDILAAN--ARGVKFEVLSNPEF 157
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENlVKPIIEEGgkKVGVDFDVASNPEF 154
|
170 180
....*....|....*....|....*....
gi 501343915 158 LAEGTAVEDLKQPDRVLIGGERTPGGEAA 186
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
327-435 |
1.84e-32 |
|
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: 118.76 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 327 AVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRellgpdkqdsRLTVVKSAYAAAEGAHGLAVLTE 406
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREY----------GLTYVSDLEEALKGADAVVIATE 70
|
90 100
....*....|....*....|....*....
gi 501343915 407 WDEFKTLDFKRIFESMAKPAcVFDGRNIL 435
Cdd:smart00984 71 HDEFRSLDPEELKDLMKKPV-VVDGRNIL 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-452 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 811.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKAPDIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLFFSTDVRSAIQAADI 80
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEADI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKTYGVGSGRAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAETIKDILAANARGVKFEVLSNPEFLAE 160
Cdd:PLN02353 82 VFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSNPEFLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 161 GTAVEDLKQPDRVLIGGERTPGGEAAVQTLADVYARWVPRDRIITTNLWSSELSKLVANAFLAQRISSINSISALCEATG 240
Cdd:PLN02353 162 GTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 241 ADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYLCDHFALPEVSSYWENVVKMNDWQKRRFATKIVRALFNS 320
Cdd:PLN02353 242 ADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMFNT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 321 VADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRELLGPDKQ--------------DSRLT 386
Cdd:PLN02353 322 VSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDwdhprhlqpmsptaVKQVS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501343915 387 VVKSAYAAAEGAHGLAVLTEWDEFKTLDFKRIFESMAKPACVFDGRNILSLEALKSLGFRVYGVGK 452
Cdd:PLN02353 402 VVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLDHEKLREIGFIVYSIGK 467
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-452 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 592.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKAPDieVRVVDMNAARIASWNSDALPVYEPGLDDVVKEAR-GRNLFFSTDVRSAIQAAD 79
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 80 IVFVAVNTPTKTYGvgsgrAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAETIKDILAANAR--GVKFEVLSNPEF 157
Cdd:COG1004 79 VVFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRgaGVDFDVVSNPEF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 158 LAEGTAVEDLKQPDRVLIGGErtpgGEAAVQTLADVYARWVPR-DRIITTNLWSSELSKLVANAFLAQRISSINSISALC 236
Cdd:COG1004 154 LREGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNgTPIIVTDLRSAELIKYAANAFLATKISFINEIANLC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 237 EATGADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYLCDHFALPevSSYWENVVKMNDWQKRRFATKIVRA 316
Cdd:COG1004 230 EKVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 317 LFNSVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEdiRRELLGPDkqdsrLTVVKSAYAAAE 396
Cdd:COG1004 308 LGGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMEN--ARRLLPDD-----ITYADDAYEALE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 501343915 397 GAHGLAVLTEWDEFKTLDFKRIFESMAKPAcVFDGRNILSLEALKSLGFRVYGVGK 452
Cdd:COG1004 381 GADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLDPEELRAAGFTYYGIGR 435
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-433 |
2.69e-116 |
|
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: 346.91 E-value: 2.69e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKApdIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLF-FSTDVRSAIQAAD 79
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLG--HDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 80 IVFVAVNTPTKTYGvgsgrAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAE-TIKDILAAN--ARGVKFEVLSNPE 156
Cdd:TIGR03026 79 VIIICVPTPLKEDG-----SPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEeVVKPILERSglKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 157 FLAEGTAVEDLKQPDRVlIGGErtpgGEAAVQTLADVYARWVpRDRIITTNLWSSELSKLVANAFLAQRISSINSISALC 236
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRI-VGGE----TEEAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 237 EATGADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYlcdhfALPEV---SSYWENVVKMNDWQKRRFATKI 313
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIA-----KAKELgynPELIEAAREINDSQPDYVVEKI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 314 VRALFNsVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRrellgpdkqdsRLTVVKSAYA 393
Cdd:TIGR03026 303 KDLLGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVK-----------GLPSIDDLEE 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501343915 394 AAEGAHGLAVLTEWDEFKTLDFKRIFESMAKPAcVFDGRN 433
Cdd:TIGR03026 371 ALKGADALVILTDHSEFKDLDLEKIKDLMKGKV-VVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-186 |
1.25e-72 |
|
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: 226.75 E-value: 1.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIACKApdIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLFFSTDVRSAIQAADI 80
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKTygvgSGRAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAET-IKDILAAN--ARGVKFEVLSNPEF 157
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENlVKPIIEEGgkKVGVDFDVASNPEF 154
|
170 180
....*....|....*....|....*....
gi 501343915 158 LAEGTAVEDLKQPDRVLIGGERTPGGEAA 186
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
2-436 |
4.97e-54 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 185.65 E-value: 4.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 2 KICCIGAGYVGGPTMAMIAcKAPdIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRNLFFSTDVrSAIQAADIV 81
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFA-KAG-FRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDP-EALAEADVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 82 FVAVNTPtktygVGSGRAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAETI-KDILAANA---RGVKFEVLSNPEF 157
Cdd:COG0677 78 IIAVPTP-----LDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVcVPILEKRSglkAGEDFFLAYSPER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 158 LAEGTAVEDLKQPDRVlIGGErtpgGEAAVQTLADVYARWVPRDRIITTNLWSSELSKLVANAFLAQRISSINSISALCE 237
Cdd:COG0677 153 INPGNKLHELRNIPKV-VGGI----TPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 238 ATGADVDEVARAIGKDsrigPKFLKAS--VGFGGSCFQKDILNLVY----LCDHFALPEVSSywenvvKMNDWQKRRFAT 311
Cdd:COG0677 228 RLGIDVWEVIEAANTK----PGFLIFYpgPGVGGHCIPVDPYYLTWkareLGYHPRLILAAR------EINDSMPEYVVE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 312 KIVRALFN---SVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRELLGPdkqdsrltvv 388
Cdd:COG0677 298 RVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGEL---------- 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 501343915 389 KSAYAAAEGAHGLAVLTEWDEFKTLDFKRIfeSMAKPACVFDGRNILS 436
Cdd:COG0677 368 VDLEEALEGADAVVLAVDHDEFDELDPEEL--RLKGAKVVVDTRGVLD 413
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
210-303 |
1.02e-39 |
|
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: 137.89 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 210 SSELSKLVANAFLAQRISSINSISALCEATGADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLVYLCDHFALP 289
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|....
gi 501343915 290 evSSYWENVVKMND 303
Cdd:pfam00984 81 --ARLLEAAREVNE 92
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
327-435 |
2.34e-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: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 327 AVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRELLGpdkqdsrLTVVKSAYAAAEGAHGLAVLTE 406
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDG-------VTLVDDLEEALKGADAIVILTD 73
|
90 100
....*....|....*....|....*....
gi 501343915 407 WDEFKTLDFKRIFESMAKPAcVFDGRNIL 435
Cdd:pfam03720 74 HDEFKSLDWEKLKKLMKPPV-VFDGRNVL 101
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
327-435 |
1.84e-32 |
|
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: 118.76 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 327 AVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRellgpdkqdsRLTVVKSAYAAAEGAHGLAVLTE 406
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREY----------GLTYVSDLEEALKGADAVVIATE 70
|
90 100
....*....|....*....|....*....
gi 501343915 407 WDEFKTLDFKRIFESMAKPAcVFDGRNIL 435
Cdd:smart00984 71 HDEFRSLDPEELKDLMKKPV-VVDGRNIL 98
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
2-418 |
6.14e-31 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 123.17 E-value: 6.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 2 KICCIGAGYVGGPTMAMIACKapDIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEA-RGRNLFFSTdvrsAIQAADI 80
Cdd:PRK11064 5 TISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAvEGGYLRATT----TPEPADA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKtygvgSGRAADLRFIESVARTIAEVATTPKIIVEKSTIPVKTAETIKDILAANARGVKF----------E 150
Cdd:PRK11064 79 FLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFpqqageqadiN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 151 VLSNPEFLAEGTAVEDLKQPDRVlIGGERTPGGEAAVqtlaDVYARWVpRDRIITTNLWSSELSKLVANAFLAQRISSIN 230
Cdd:PRK11064 154 IAYCPERVLPGQVMVELIKNDRV-IGGMTPVCSARAS----ELYKIFL-EGECVVTNSRTAEMCKLTENSFRDVNIAFAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 231 SISALCEATGADVDEVARAIGKDSRIgpKFLKASVGFGGSCFQKDILNLVYLCdhfalPEVSSYWENVVKMNDWQKRRFA 310
Cdd:PRK11064 228 ELSLICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPWFIVAQN-----PQQARLIRTAREVNDGKPHWVI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 311 TKIVRALFNSVA-------DKKIAVLGFAFKKDTNDTRESPAISVCRDLLA-EQARVAVYDPQVTEEdirrellgPDKQD 382
Cdd:PRK11064 301 DQVKAAVADCLAatdkrasEVKIACFGLAFKPNIDDLRESPAMEIAELIAQwHSGETLVVEPNIHQL--------PKKLD 372
|
410 420 430
....*....|....*....|....*....|....*.
gi 501343915 383 SRLTVVKSAYAAAEgAHGLAVLTEWDEFKTLDFKRI 418
Cdd:PRK11064 373 GLVTLVSLDEALAT-ADVLVMLVDHSQFKAINGDNV 407
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
1-369 |
3.10e-25 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 106.65 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPTMAMIAckaPDIEVRVVDMNAARIASWNSDALPVYEPGLDDVVKEARGRnlFFST-DVRSAIQAAD 79
Cdd:PRK15057 1 MKITISGTGYVGLSNGLLIA---QNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQSDKIH--FNATlDKNEAYRDAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 80 IVFVAVNT---PTKTYGVGSGraadlrfIESVARTIAEVATTPKIIVeKSTIPVK-TAETIKDILAANargvkfeVLSNP 155
Cdd:PRK15057 76 YVIIATPTdydPKTNYFNTSS-------VESVIKDVVEINPYAVMVI-KSTVPVGfTAAMHKKYRTEN-------IIFSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 156 EFLAEGTAVEDLKQPDRVLIGgERTPGGEAAVQTLAD-VYARWVPrdrIITTNLWSSELSKLVANAFLAQRISSINSISA 234
Cdd:PRK15057 141 EFLREGKALYDNLHPSRIVIG-ERSERAERFAALLQEgAIKQNIP---TLFTDSTEAEAIKLFANTYLAMRVAYFNELDS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 235 LCEATGADVDEVARAIGKDSRIGPKFLKASVGFGGSCFQKDILNLvyLCDHFALPevSSYWENVVKMNDWQKRRFATKIV 314
Cdd:PRK15057 217 YAESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQL--LANYQSVP--NNLISAIVDANRTRKDFIADAIL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 501343915 315 ralfnSVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEE 369
Cdd:PRK15057 293 -----SRKPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKED 342
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
1-374 |
4.45e-16 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 79.73 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPtMAMIACKAPdiEVRVVDMNAARIASWNsDALPVYEPGLDDVVKEARgrNLFFSTDVRSaIQAADI 80
Cdd:PRK15182 7 VKIAIIGLGYVGLP-LAVEFGKSR--QVVGFDVNKKRILELK-NGVDVNLETTEEELREAR--YLKFTSEIEK-IKECNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKTYgvgsgRAADLRFIESVARTIAEVATTPKIIVEKSTI-PVKTAETIKDILAaNARGVKFE----VLSNP 155
Cdd:PRK15182 80 YIITVPTPINTY-----KQPDLTPLIKASETVGTVLNRGDIVVYESTVyPGCTEEECVPILA-RMSGMTFNqdfyVGYSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 156 EFLAEGTAVEDLKQPDRVliggerTPGGEAAVQTLAD-VYARWVPRDRIITTNLWSSELSKLVANAFLAQRISSINSISA 234
Cdd:PRK15182 154 ERINPGDKKHRLTNIKKI------TSGSTAQIAELIDeVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 235 LCEATGADVDEVARAIGKDSRIGPkFLKASVGfgGSCFQKDILNLVYLCDHFAlpevssYWENVV----KMNDWQKRRFA 310
Cdd:PRK15182 228 IFNRLNIDTEAVLRAAGSKWNFLP-FRPGLVG--GHCIGVDPYYLTHKSQGIG------YYPEIIlagrRLNDNMGNYVS 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501343915 311 TKIVRALFN---SVADKKIAVLGFAFKKDTNDTRESPAISVCRDLLAEQARVAVYDPQVTEEDIRRE 374
Cdd:PRK15182 299 EQLIKAMIKkgiNVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRRE 365
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-145 |
1.02e-03 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 40.82 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGyvggpTMA------MIACKAPDIEVRVVDMNAARIASWnsdalpvyepglddvvKEARGRNLffSTDVRSA 74
Cdd:COG0345 3 MKIGFIGAG-----NMGsaiikgLLKSGVPPEDIIVSDRSPERLEAL----------------AERYGVRV--TTDNAEA 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501343915 75 IQAADIVFVAVntptKTYgvgsgraadlrFIESVARTIAEVATTPKIIVekSTIPVKTAETIKDILAANAR 145
Cdd:COG0345 60 AAQADVVVLAV----KPQ-----------DLAEVLEELAPLLDPDKLVI--SIAAGVTLATLEEALGGGAP 113
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
1-160 |
2.81e-03 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 39.63 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGyVGGPTMAMIACKApDIEVRVVDMNAARIASWNSD-ALPVYEPG--LDDvvkeargrNLFFSTDVRSAIQA 77
Cdd:COG0240 1 MKIAVLGAG-SWGTALAKVLARN-GHEVTLWGRDPEVAEEINETrENPRYLPGvkLPE--------NLRATSDLEEALAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 78 ADIVFVAVntPTKtygvgsgraadlrFIESVARTIAEVATTPKIIV------EKSTIpvKT-AETIKDILAANARGVkfe 150
Cdd:COG0240 71 ADLVLLAV--PSQ-------------ALREVLEQLAPLLPPGAPVVsatkgiEPGTG--LLmSEVIAEELPGALRIA--- 130
|
170
....*....|
gi 501343915 151 VLSNPEFLAE 160
Cdd:COG0240 131 VLSGPSFAEE 140
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
1-252 |
4.45e-03 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 38.94 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 1 MKICCIGAGYVGGPtMAMIACKApDIEVRVVDMNAARIASWnsdalpvyepglddvvkEARGRNLFfsTDVRSAIQAADI 80
Cdd:COG2084 2 MKVGFIGLGAMGAP-MARNLLKA-GHEVTVWNRTPAKAEAL-----------------VAAGARVA--ASPAEAAAAADV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 81 VFVAVNTPTKTYGVGSGRAAdlrfiesvartIAEVATTPKIIVEKSTIPVKTAETIKDILAanARGVKF---EVLSNPEF 157
Cdd:COG2084 61 VITMLPDDAAVEEVLLGEDG-----------LLAALRPGAVVVDMSTISPETARELAAAAA--ARGVRYldaPVSGGPAG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501343915 158 LAEGTAVedlkqpdrVLIGGErtpggeaavqtlADVYARWVPRDRIITTNLW------SSELSKLVANAFLAqriSSINS 231
Cdd:COG2084 128 AEAGTLT--------IMVGGD------------EAAFERARPVLEAMGKRIVhvgdagAGQAAKLANNLLLA---GTMAA 184
|
250 260
....*....|....*....|....
gi 501343915 232 IS---ALCEATGADVDEVARAIGK 252
Cdd:COG2084 185 LAealALAEKAGLDPETLLEVLSG 208
|
|
| |
