|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
4-464 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 781.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 4 IKKICCIGAGYVGGPTCSVIAQMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLFFSTNIDDAIKEAD 83
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353 81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPKGKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVAHYWQQVIDINDYQRRRFASRIIDGLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 395 VTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 464
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
6-465 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 558.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 6 KICCIGAGYVGGPTCSVIAQMCPEirVTVVDVNESRINAWNSPTLPIYEPGLKEVV-EACRGKNLFFSTNIDDAIKEADL 84
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVaRNVAAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 85 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQIF-DANTKPNLNLQVLSNPEFL 163
Cdd:COG1004 80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 164 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPKG-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 242
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 243 ATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevAHYWQQVIDINDYQRRRFASRIIDGL 322
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 323 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvsedDQVSRL----VTIS 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAM----------------ENARRLlpddITYA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910837283 399 KDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAfIFDGRRVLDglHNELQTIGFQIETIGKK 465
Cdd:COG1004 373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLD--PEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
5-443 |
3.07e-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: 348.06 E-value: 3.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 5 KKICCIGAGYVGGPTCSVIAQMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLF-FSTNIDDAIKEAD 83
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 84 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQ--IFDANTKPNLNLQVLSNPE 161
Cdd:TIGR03026 79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 162 FLAEGTAIKDLKNPDRVLIGGDEtpegqRAVQALCAVYEHWVpKGKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGGETE-----EAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 242 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevAHYWQQVIDINDYQRRRFASRIIDG 321
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 322 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvseddqvsrlvtiskDP 401
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1910837283 402 YEACDGAHAVVICTEWDMFKELDYERIhKKMLKPAFIFDGRR 443
Cdd:TIGR03026 369 EEALKGADALVILTDHSEFKDLDLEKI-KDLMKGKVVVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
5-191 |
9.16e-71 |
|
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: 223.28 E-value: 9.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 5 KKICCIGAGYVGGPTCSVIAQMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLFFSTNIDDAIKEADL 84
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 85 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQ--IFDANTKPNLNLQVLSNPEF 162
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKpiIEEGGKKVGVDFDVASNPEF 154
|
170 180
....*....|....*....|....*....
gi 1910837283 163 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 191
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 ... |
332-446 |
3.65e-33 |
|
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: 121.07 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvseddqvSRLVTISKDPYEACDGAHAV 411
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
|
90 100 110
....*....|....*....|....*....|....*
gi 1910837283 412 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 446
Cdd:smart00984 66 VIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
4-464 |
0e+00 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 781.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 4 IKKICCIGAGYVGGPTCSVIAQMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLFFSTNIDDAIKEAD 83
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353 81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPKGKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVAHYWQQVIDINDYQRRRFASRIIDGLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 395 VTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 464
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
6-465 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 558.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 6 KICCIGAGYVGGPTCSVIAQMCPEirVTVVDVNESRINAWNSPTLPIYEPGLKEVV-EACRGKNLFFSTNIDDAIKEADL 84
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVaRNVAAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 85 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQIF-DANTKPNLNLQVLSNPEFL 163
Cdd:COG1004 80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 164 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPKG-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 242
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 243 ATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevAHYWQQVIDINDYQRRRFASRIIDGL 322
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 323 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvsedDQVSRL----VTIS 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAM----------------ENARRLlpddITYA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910837283 399 KDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAfIFDGRRVLDglHNELQTIGFQIETIGKK 465
Cdd:COG1004 373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLD--PEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
5-443 |
3.07e-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: 348.06 E-value: 3.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 5 KKICCIGAGYVGGPTCSVIAQMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLF-FSTNIDDAIKEAD 83
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 84 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQ--IFDANTKPNLNLQVLSNPE 161
Cdd:TIGR03026 79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 162 FLAEGTAIKDLKNPDRVLIGGDEtpegqRAVQALCAVYEHWVpKGKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGGETE-----EAGEAVAELYSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 242 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevAHYWQQVIDINDYQRRRFASRIIDG 321
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 322 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvseddqvsrlvtiskDP 401
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1910837283 402 YEACDGAHAVVICTEWDMFKELDYERIhKKMLKPAFIFDGRR 443
Cdd:TIGR03026 369 EEALKGADALVILTDHSEFKDLDLEKI-KDLMKGKVVVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
5-191 |
9.16e-71 |
|
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: 223.28 E-value: 9.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 5 KKICCIGAGYVGGPTCSVIAQMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLFFSTNIDDAIKEADL 84
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 85 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQ--IFDANTKPNLNLQVLSNPEF 162
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKpiIEEGGKKVGVDFDVASNPEF 154
|
170 180
....*....|....*....|....*....
gi 1910837283 163 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 191
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
6-446 |
3.19e-56 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 192.58 E-value: 3.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 6 KICCIGAGYVGGPTCSVIAQMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEACRGKNLFFSTNIDdAIKEADLV 85
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAG--FRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPE-ALAEADVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 86 FISVNTPTKtygmgKGRAADLKYIEACARRIVQN-SHGYKIVTEkSTVPVRAAESI-RQIFDANT--KPNLNLQVLSNPE 161
Cdd:COG0677 78 IIAVPTPLD-----EDKEPDLSYLESASETIAPHlKPGDLVVLE-STVYPGTTEEVcVPILEKRSglKAGEDFFLAYSPE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 162 FLAEGTAIKDLKNPDRVlIGGDeTPEGQRAVQALcavYEHWVPKGKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:COG0677 152 RINPGNKLHELRNIPKV-VGGI-TPESAERAAAL---YGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALIC 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 242 EATGADVEEVATAIGMDQRIgNKFlKASVGFGGSCFQKDVLNLVYLCEALNLPEvahywqQVI----DINDYQRRRFASR 317
Cdd:COG0677 227 DRLGIDVWEVIEAANTKPGF-LIF-YPGPGVGGHCIPVDPYYLTWKARELGYHP------RLIlaarEINDSMPEYVVER 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 318 IIDGLFN---TVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvseDDQVSRL 394
Cdd:COG0677 299 VVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVD---------------EEEVEGE 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1910837283 395 VTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKmlKPAFIFDGRRVLD 446
Cdd:COG0677 364 YGELVDLEEALEGADAVVLAVDHDEFDELDPEELRLK--GAKVVVDTRGVLD 413
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
215-308 |
1.36e-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: 145.98 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 215 SSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLP 294
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|....
gi 1910837283 295 evAHYWQQVIDIND 308
Cdd:pfam00984 81 --ARLLEAAREVNE 92
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
332-446 |
1.09e-37 |
|
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: 133.47 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHpgvseddqvsrlVTISKDPYEACDGAHAV 411
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDG------------VTLVDDLEEALKGADAI 68
|
90 100 110
....*....|....*....|....*....|....*
gi 1910837283 412 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 446
Cdd:pfam03720 69 VILTDHDEFKSLDWEKL-KKLMKPPVVFDGRNVLD 102
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
332-446 |
3.65e-33 |
|
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: 121.07 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvseddqvSRLVTISKDPYEACDGAHAV 411
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
|
90 100 110
....*....|....*....|....*....|....*
gi 1910837283 412 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 446
Cdd:smart00984 66 VIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
6-369 |
1.56e-29 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 119.36 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 6 KICCIGAGYVGGPTCSVIAQmcpEIRVTVVDVNESRINAWNSPTLPIYEpglKEVVEACRGKNLFFSTNID--DAIKEAD 83
Cdd:PRK15057 2 KITISGTGYVGLSNGLLIAQ---NHEVVALDILPSRVAMLNDRISPIVD---KEIQQFLQSDKIHFNATLDknEAYRDAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 84 LVFISvnTPTKtYGmGKGRAADLKYIEACARRIVQnSHGYKIVTEKSTVPVRAAESIRQIFdaNTKpnlnlQVLSNPEFL 163
Cdd:PRK15057 76 YVIIA--TPTD-YD-PKTNYFNTSSVESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHKKY--RTE-----NIIFSPEFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 164 AEGTAIKDLKNPDRVLIGgdetPEGQRAvQALCAVYEHWVPKGKILT--TNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:PRK15057 144 REGKALYDNLHPSRIVIG----ERSERA-ERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 242 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLvyLCEALNLPEvaHYWQQVIDINDYQRRRFASRIIdg 321
Cdd:PRK15057 219 ESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQL--LANYQSVPN--NLISAIVDANRTRKDFIADAIL-- 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1910837283 322 lfnTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDP 369
Cdd:PRK15057 293 ---SRKPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
5-359 |
9.80e-23 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 100.06 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 5 KKICCIGAGYVGGPTCSVIAQMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVV-EACRGKNLFFSTniddAIKEAD 83
Cdd:PRK11064 4 ETISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVkTAVEGGYLRATT----TPEPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 84 LVFISVNTPTKtygmgKGRAADLKYIEACARRIVQNSHGYKIVTEKSTVPVRAAESIRQIFdANTKPNL----------N 153
Cdd:PRK11064 78 AFLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWL-AEARPDLtfpqqageqaD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 154 LQVLSNPEFLAEGTAIKDLKNPDRVlIGGdETPE-GQRAVqalcAVYEHWVpKGKILTTNTWSSELSKLAANAFLAQRIS 232
Cdd:PRK11064 152 INIAYCPERVLPGQVMVELIKNDRV-IGG-MTPVcSARAS----ELYKIFL-EGECVVTNSRTAEMCKLTENSFRDVNIA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 233 SINSISALCEATGADVEEVAtaigmdqRIGNK-----FLKASVGFGGSCFQKDVLNLVYLCealnlPEVAHYWQQVIDIN 307
Cdd:PRK11064 225 FANELSLICADQGINVWELI-------RLANRhprvnILQPGPGVGGHCIAVDPWFIVAQN-----PQQARLIRTAREVN 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1910837283 308 D----YQRRRFASRIIDGLFNT---VTDKKIAILGFAFKKDTGDTRESSSIYISKYLMD 359
Cdd:PRK11064 293 DgkphWVIDQVKAAVADCLAATdkrASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQ 351
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
1-376 |
1.66e-11 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 65.86 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 1 MFEIK--KICCIGAGYVGGPtcsVIAQMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEAcrgKNLFFSTNIDDa 78
Cdd:PRK15182 1 MFGIDevKIAIIGLGYVGLP---LAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREA---RYLKFTSEIEK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 79 IKEADLVFISVNTPTKTYgmgkgRAADLKYIEACARRI----------VQNSHGYKIVTEKSTVPVRAAESirqifdaNT 148
Cdd:PRK15182 74 IKECNFYIITVPTPINTY-----KQPDLTPLIKASETVgtvlnrgdivVYESTVYPGCTEEECVPILARMS-------GM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 149 KPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDetpegQRAVQALCAVYEHWVPKGKILTTNTWSSELSKLAANAFLA 228
Cdd:PRK15182 142 TFNQDFYVGYSPERINPGDKKHRLTNIKKITSGST-----AQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 229 QRISSINSISALCEATGADVEEVATAIGMDQrignKFLKASVGF-GGSCFQKDVLNLVYLCEALNL-PEVAHYWQQVID- 305
Cdd:PRK15182 217 LNIALVNELAIIFNRLNIDTEAVLRAAGSKW----NFLPFRPGLvGGHCIGVDPYYLTHKSQGIGYyPEIILAGRRLNDn 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1910837283 306 INDYQRRRFASRIIDGLFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQI 376
Cdd:PRK15182 293 MGNYVSEQLIKAMIKKGIN-VEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEV 362
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
5-89 |
4.50e-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: 38.89 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910837283 5 KKICCIGAG-----YVGGptcsVIAQMCPEIRVTVVDVNESRINAWNSptlpiyEPGlkevVEACrgknlffsTNIDDAI 79
Cdd:COG0345 3 MKIGFIGAGnmgsaIIKG----LLKSGVPPEDIIVSDRSPERLEALAE------RYG----VRVT--------TDNAEAA 60
|
90
....*....|
gi 1910837283 80 KEADLVFISV 89
Cdd:COG0345 61 AQADVVVLAV 70
|
|
| |
