|
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: 786.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 4 IKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEAD 83
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353 81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 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: 562.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 6 KICCIGAGYVGGPTCSVIAHMCPEirVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCR-GKNLFFSTNIDDAIKEADL 84
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 85 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIF-DANTKPNLNLQVLSNPEFL 163
Cdd:COG1004 80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 164 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPRE-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 242
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 243 ATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDSL 322
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 323 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvsedDQVSRL----VTIS 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAM----------------ENARRLlpddITYA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507813 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 |
1.79e-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: 346.14 E-value: 1.79e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 5 KKICCIGAGYVGGPTCSVIAHMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLF-FSTNIDDAIKEAD 83
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 84 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRR--IFDANTKPNLNLQVLSNPE 161
Cdd:TIGR03026 79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 162 FLAEGTAIKDLKNPDRVLIGgdETPEGQRAVQALcavYEHWVpREKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGG--ETEEAGEAVAEL---YSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 242 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDS 321
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 322 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvseddqvsrlvtiskDP 401
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 4507813 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 |
2.27e-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: 224.82 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 5 KKICCIGAGYVGGPTCSVIAHMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADL 84
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 85 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESI--RRIFDANTKPNLNLQVLSNPEF 162
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKVGVDFDVASNPEF 154
|
170 180
....*....|....*....|....*....
gi 4507813 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 |
3.88e-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: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvseddqvSRLVTISKDPYEACDGAHAV 411
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
|
90 100 110
....*....|....*....|....*....|....*
gi 4507813 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: 786.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 4 IKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEAD 83
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 84 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 163
Cdd:PLN02353 81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 164 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 243
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 244 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 323
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 324 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 394
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 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: 562.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 6 KICCIGAGYVGGPTCSVIAHMCPEirVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCR-GKNLFFSTNIDDAIKEADL 84
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 85 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIF-DANTKPNLNLQVLSNPEFL 163
Cdd:COG1004 80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 164 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPRE-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 242
Cdd:COG1004 155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 243 ATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDSL 322
Cdd:COG1004 231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 323 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvsedDQVSRL----VTIS 398
Cdd:COG1004 309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAM----------------ENARRLlpddITYA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507813 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 |
1.79e-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: 346.14 E-value: 1.79e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 5 KKICCIGAGYVGGPTCSVIAHMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLF-FSTNIDDAIKEAD 83
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 84 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRR--IFDANTKPNLNLQVLSNPE 161
Cdd:TIGR03026 79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 162 FLAEGTAIKDLKNPDRVLIGgdETPEGQRAVQALcavYEHWVpREKILTTNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGG--ETEEAGEAVAEL---YSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 242 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDS 321
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 322 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvseddqvsrlvtiskDP 401
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 4507813 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 |
2.27e-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: 224.82 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 5 KKICCIGAGYVGGPTCSVIAHMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADL 84
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 85 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESI--RRIFDANTKPNLNLQVLSNPEF 162
Cdd:pfam03721 79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKVGVDFDVASNPEF 154
|
170 180
....*....|....*....|....*....
gi 4507813 163 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 191
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
6-446 |
3.09e-54 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 187.58 E-value: 3.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 6 KICCIGAGYVGGPTCSVIAHMCpeIRVTVVDVNESRINAWNSPTLPIYEPG---LKEVVESCRgknLFFSTNIDdAIKEA 82
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAG--FRVIGFDINPERVEELNAGEDPILEPGdelLAEAVAAGR---LRATTDPE-ALAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 83 DLVFISVNTPTKtygmgKGRAADLKYIEACARRIVQN-SNGYKIVTEkSTVPVRAAESI-RRIFDANT--KPNLNLQVLS 158
Cdd:COG0677 75 DVVIIAVPTPLD-----EDKEPDLSYLESASETIAPHlKPGDLVVLE-STVYPGTTEEVcVPILEKRSglKAGEDFFLAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 159 NPEFLAEGTAIKDLKNPDRVlIGGDeTPEGQRAVQALcavYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSIS 238
Cdd:COG0677 149 SPERINPGNKLHELRNIPKV-VGGI-TPESAERAAAL---YGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 239 ALCEATGADVEEVATAIGMDQRIgNKFlKASVGFGGSCFQKDVLNLVYLCEALNLP----EVARywqqviDMNDYQRRRF 314
Cdd:COG0677 224 LICDRLGIDVWEVIEAANTKPGF-LIF-YPGPGVGGHCIPVDPYYLTWKARELGYHprliLAAR------EINDSMPEYV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 315 ASRIIDSLFN---TVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvseDDQV 391
Cdd:COG0677 296 VERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVD---------------EEEV 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 4507813 392 SRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKmlKPAFIFDGRRVLD 446
Cdd:COG0677 361 EGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEELRLK--GAKVVVDTRGVLD 413
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
215-308 |
3.69e-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: 147.52 E-value: 3.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 215 SSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLP 294
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|....
gi 4507813 295 evARYWQQVIDMND 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 4507813 332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHpgvseddqvsrlVTISKDPYEACDGAHAV 411
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDG------------VTLVDDLEEALKGADAI 68
|
90 100 110
....*....|....*....|....*....|....*
gi 4507813 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 |
3.88e-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: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 332 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvseddqvSRLVTISKDPYEACDGAHAV 411
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
|
90 100 110
....*....|....*....|....*....|....*
gi 4507813 412 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 446
Cdd:smart00984 66 VIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
6-369 |
2.28e-29 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 118.97 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 6 KICCIGAGYVGGPTCSVIAHmcpEIRVTVVDVNESRINAWNSPTLPIYEpglKEVVESCRGKNLFFSTNID--DAIKEAD 83
Cdd:PRK15057 2 KITISGTGYVGLSNGLLIAQ---NHEVVALDILPSRVAMLNDRISPIVD---KEIQQFLQSDKIHFNATLDknEAYRDAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 84 LVFISvnTPTKtYGmGKGRAADLKYIEACARRIVQnSNGYKIVTEKSTVPVRAAESIRRIFdaNTKpnlnlQVLSNPEFL 163
Cdd:PRK15057 76 YVIIA--TPTD-YD-PKTNYFNTSSVESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHKKY--RTE-----NIIFSPEFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 164 AEGTAIKDLKNPDRVLIGgdetPEGQRAvQALCAVYEHWVPREKILT--TNTWSSELSKLAANAFLAQRISSINSISALC 241
Cdd:PRK15057 144 REGKALYDNLHPSRIVIG----ERSERA-ERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 242 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLvyLCEALNLPEvaRYWQQVIDMNDYQRRRFASRIIDS 321
Cdd:PRK15057 219 ESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQL--LANYQSVPN--NLISAIVDANRTRKDFIADAILSR 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 4507813 322 lfntvTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDP 369
Cdd:PRK15057 295 -----KPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
5-359 |
1.29e-21 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 96.98 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 5 KKICCIGAGYVGGPTCSVIAHMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESC-RGKNLFFSTniddAIKEAD 83
Cdd:PRK11064 4 ETISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAvEGGYLRATT----TPEPAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 84 LVFISVNTPTKtygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFdANTKPNL----------N 153
Cdd:PRK11064 78 AFLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWL-AEARPDLtfpqqageqaD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 154 LQVLSNPEFLAEGTAIKDLKNPDRVlIGGdETPE-GQRAVqalcAVYEHWVPREKILTtNTWSSELSKLAANAFLAQRIS 232
Cdd:PRK11064 152 INIAYCPERVLPGQVMVELIKNDRV-IGG-MTPVcSARAS----ELYKIFLEGECVVT-NSRTAEMCKLTENSFRDVNIA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 233 SINSISALCEATGADVEEVAtaigmdqRIGNK-----FLKASVGFGGSCFQKDVLNLVYLCealnlPEVARYWQQVIDMN 307
Cdd:PRK11064 225 FANELSLICADQGINVWELI-------RLANRhprvnILQPGPGVGGHCIAVDPWFIVAQN-----PQQARLIRTAREVN 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 4507813 308 D----YQRRRFASRIIDSLFNT---VTDKKIAILGFAFKKDTGDTRESSSIYISKYLMD 359
Cdd:PRK11064 293 DgkphWVIDQVKAAVADCLAATdkrASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQ 351
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
1-376 |
4.07e-11 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 64.71 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 1 MFEIK--KICCIGAGYVGGPtcsVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEScrgKNLFFSTNIDDa 78
Cdd:PRK15182 1 MFGIDevKIAIIGLGYVGLP---LAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREA---RYLKFTSEIEK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 79 IKEADLVFISVNTPTKTYgmgkgRAADLKYIEACARRI----------VQNSNGYKIVTEKSTVPVRAAESirrifdaNT 148
Cdd:PRK15182 74 IKECNFYIITVPTPINTY-----KQPDLTPLIKASETVgtvlnrgdivVYESTVYPGCTEEECVPILARMS-------GM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 149 KPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDetpegQRAVQALCAVYEhwvpreKILTTNTWSSELSKLAANAFL- 227
Cdd:PRK15182 142 TFNQDFYVGYSPERINPGDKKHRLTNIKKITSGST-----AQIAELIDEVYQ------QIISAGTYKAESIKVAEAAKVi 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 228 --AQR---ISSINSISALCEATGADVEEVATAIGMDQrignKFLKASVGF-GGSCFQKDVLNLVYLCEALNL-PEVARYW 300
Cdd:PRK15182 211 enTQRdlnIALVNELAIIFNRLNIDTEAVLRAAGSKW----NFLPFRPGLvGGHCIGVDPYYLTHKSQGIGYyPEIILAG 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507813 301 QQVID-MNDYQRRRFASRIIDSLFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQI 376
Cdd:PRK15182 287 RRLNDnMGNYVSEQLIKAMIKKGIN-VEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEV 362
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
5-89 |
8.41e-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: 38.12 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507813 5 KKICCIGAG-----YVGGptcsVIAHMCPEIRVTVVDVNESRINAWNSptlpiyEPGLKevvescrgknlfFSTNIDDAI 79
Cdd:COG0345 3 MKIGFIGAGnmgsaIIKG----LLKSGVPPEDIIVSDRSPERLEALAE------RYGVR------------VTTDNAEAA 60
|
90
....*....|
gi 4507813 80 KEADLVFISV 89
Cdd:COG0345 61 AQADVVVLAV 70
|
|
| |
