|
Name |
Accession |
Description |
Interval |
E-value |
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-488 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 852.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 3 FPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTlgrtIDVAL 82
Cdd:PRK14352 1 APRPTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPE----VDIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 83 QDRPLGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVM 162
Cdd:PRK14352 77 QDEQPGTGHAVQCALEALPADFDGTVVVTAGDVPLLDGETLADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQDGEVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 163 AIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRV 242
Cdd:PRK14352 157 AIVEQKDATPSQRAIREVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAIAREAGHRVGAHHADDSAEVAGVNDRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 243 QLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVV 322
Cdd:PRK14352 237 QLAALGAELNRRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 323 RTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTS 402
Cdd:PRK14352 317 RTHGSESEIGAGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 403 KRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGSPAAQASKRASEMAC 482
Cdd:PRK14352 397 KHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSEGPQRNIEGWVQRKRPGTPAAEAAEAASEAAA 476
|
....*.
gi 489500362 483 QQPTQP 488
Cdd:PRK14352 477 QQSTGP 482
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
6-468 |
0e+00 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 734.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 6 DTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELAdtlgrtIDVALQDR 85
Cdd:COG1207 2 PLAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLD------VEFVLQEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PLGTGHAVLCGLSALPDDyAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIV 165
Cdd:COG1207 76 QLGTGHAVQQALPALPGD-DGTVLVLYGDVPLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 166 EQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLA 245
Cdd:COG1207 155 EEKDATEEQRAIREINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADGLKVAAVQPEDPWEVLGVNDRVQLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 246 ELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTH 325
Cdd:COG1207 235 EAERILQRRIAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 326 GSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRR 405
Cdd:COG1207 315 IEDAVVGAGATVGPFARLRPGTVLGEGVKIGNFVEVKNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489500362 406 TTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGS 468
Cdd:COG1207 395 TVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIEGWVRPKKKKK 457
|
|
| glmU |
TIGR01173 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
7-466 |
0e+00 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273482 [Multi-domain] Cd Length: 451 Bit Score: 675.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGEladtlgRTIDVALQDRP 86
Cdd:TIGR01173 1 LSVVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALAN------RDVNWVLQAEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 87 LGTGHAVLCGLSALPDDyaGNVVVTSGDTPLLDADTLADLIATHRAvsAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVE 166
Cdd:TIGR01173 75 LGTGHAVLQALPFLSDD--GDVLVLYGDVPLISAETLERLLEAHRQ--NGITLLTAKLDDPTGYGRIIRENDGKVTAIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 167 QTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAE 246
Cdd:TIGR01173 151 DKDANAEQKAIKEINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRAVQVDDSDEVLGVNDRLQLAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 247 LASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVV-RTH 325
Cdd:TIGR01173 231 LERILQRRIAKKLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKVKIGDDVVIGPGCVIKNSVIGSNVVIKaYSV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 326 GSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRR 405
Cdd:TIGR01173 311 LEGSEIGEGCDVGPFARLRPGSVLGAGVHIGNFVEVKNARIGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHK 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489500362 406 TTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRP 466
Cdd:TIGR01173 391 TIIGDGVFIGSNTQLVAPVKVGDGATIAAGSTVTKDVPEGALAISRARQRNIEGWVRPKKK 451
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-465 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 577.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 8 AVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQriaplvgELADTLGRTIDVALQDRPL 87
Cdd:PRK14354 4 YAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAE-------EVKEVLGDRSEFALQEEQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 88 GTGHAVLCGLSALPDdYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQ 167
Cdd:PRK14354 77 GTGHAVMQAEEFLAD-KEGTTLVICGDTPLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKIVEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 168 TDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAEL 247
Cdd:PRK14354 156 KDATEEEKQIKEINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGEKVGAYQTEDFEESLGVNDRVALAEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 248 ASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGS 327
Cdd:PRK14354 236 EKVMRRRINEKHMVNGVTIIDPESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVDSTIGDGVTITNSVIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 328 SSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTT 407
Cdd:PRK14354 316 ESKVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVNYDGKNKFKTI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 408 VGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKR 465
Cdd:PRK14354 396 IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKEGYVKKLP 453
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-466 |
1.12e-160 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 463.45 E-value: 1.12e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 5 GDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADtlgrtIDVALQD 84
Cdd:PRK14355 2 NNLAAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 85 RPLGTGHAVLCGLSALpDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAI 164
Cdd:PRK14355 77 EQLGTGHAVACAAPAL-DGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 165 VEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQL 244
Cdd:PRK14355 156 VEEKDATPEERSIREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAAEGLRCLAFPVADPDEIMGVNDRAQL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 245 AELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGasVVRT 324
Cdd:PRK14355 236 AEAARVLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDD--VTVK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 325 HGS---SSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGT 401
Cdd:PRK14355 314 AGSvleDSVVGDDVAIGPMAHLRPGTELSAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489500362 402 SKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRP 466
Cdd:PRK14355 394 KKHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKEGWKLRKKD 458
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-464 |
4.78e-157 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 453.62 E-value: 4.78e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 8 AVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPlvgELADTLGrtIDVALQDRPL 87
Cdd:PRK14360 3 AVAILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQ---SLAHLPG--LEFVEQQPQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 88 GTGHAVLCGLSALpDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQ 167
Cdd:PRK14360 78 GTGHAVQQLLPVL-KGFEGDLLVLNGDVPLLRPETLEALLNTHRSSNADVTLLTARLPNPKGYGRVFCDGNNLVEQIVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 168 TDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILrsdgQTVHASHVDDSALVAGVNNRVQLAEL 247
Cdd:PRK14360 157 RDCTPAQRQNNRINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTVSLL----DPVMAVEVEDYQEINGINDRKQLAQC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 248 ASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGS 327
Cdd:PRK14360 233 EEILQNRIKEKWMLAGVTFIDPASCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIENSQIGENVTVLYSVVS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 328 SSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTT 407
Cdd:PRK14360 313 DSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDGVKKHRTV 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489500362 408 VGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRK 464
Cdd:PRK14360 393 IGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKENWKKKS 449
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-465 |
6.39e-153 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 443.15 E-value: 6.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQriapLVGELADTLGRTIDVALQDRP 86
Cdd:PRK14353 6 CLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAE----AVAAAAAKIAPDAEIFVQKER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 87 LGTGHAVLCGLSALpDDYAGNVVVTSGDTPLLDADTLADLIAtHRAVSAAVTVLTTTLDDPFGYGRILrTQDHEVMAIVE 166
Cdd:PRK14353 82 LGTAHAVLAAREAL-AGGYGDVLVLYGDTPLITAETLARLRE-RLADGADVVVLGFRAADPTGYGRLI-VKGGRLVAIVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 167 QTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDsALVAGVNNRVQLAE 246
Cdd:PRK14353 159 EKDASDEERAITLCNSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIARAEGLRVAVVEAPE-DEVRGINSRAELAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 247 LASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTqllgrtqiggrcVVGPDttltdVAVGDGAsVVR--T 324
Cdd:PRK14353 238 AEAVWQARRRRAAMLAGVTLIAPETVFFSYDTVIGRDVVIEPNV------------VFGPG-----VTVASGA-VIHafS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 325 HGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKR 404
Cdd:PRK14353 300 HLEGAHVGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGAGANIGAGTITCNYDGFNKH 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489500362 405 RTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKR 465
Cdd:PRK14353 380 RTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKPGWAKKLR 440
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
9-465 |
6.52e-144 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 420.32 E-value: 6.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLApQRLIVVLGHDHQRIAPLVGEladtlgrTIDVALQDRPLG 88
Cdd:PRK14357 3 ALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPE-------WVKIFLQEEQLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 89 TGHAVLCGLSAL-PDDyagNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRtqDHEVMAIVEQ 167
Cdd:PRK14357 75 TAHAVMCARDFIePGD---DLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIR--DGGKYRIVED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 168 TDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILrsdgQTVHASHVDDSALVAGVNNRVQLAEL 247
Cdd:PRK14357 150 KDAPEEEKKIKEINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAVNFA----EKVRVVKTEDLLEITGVNTRIQLAWL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 248 ASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGS 327
Cdd:PRK14357 226 EKQLRMRILEELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKIIRSECE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 328 SSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTT 407
Cdd:PRK14357 306 KSVIEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTF 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 408 VGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKR 465
Cdd:PRK14357 386 IEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWVLKKR 443
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-466 |
2.01e-130 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 386.30 E-value: 2.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 8 AVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDhqriaplvGEL-ADTLGR-TIDVALQDR 85
Cdd:PRK09451 7 SVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHG--------GDLlKQTLADePLNWVLQAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PLGTGHAVLCGLSALPDDYagNVVVTSGDTPLLDADTLADLIATHRAvsAAVTVLTTTLDDPFGYGRILRTQDhEVMAIV 165
Cdd:PRK09451 79 QLGTGHAMQQAAPFFADDE--DILMLYGDVPLISVETLQRLRDAKPQ--GGIGLLTVKLDNPTGYGRITRENG-KVVGIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 166 EQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLA 245
Cdd:PRK09451 154 EQKDATDEQRQIQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGREIVAVHPQRLSEVEGVNNRLQLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 246 ELaselnRRVVAAHQ-----LAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGA- 319
Cdd:PRK09451 234 RL-----ERVYQAEQaekllLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCVIGDDCe 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 320 ----SVVRthgsSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVF 395
Cdd:PRK09451 309 ispySVVE----DANLGAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTIT 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489500362 396 VNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWvqrKRP 466
Cdd:PRK09451 385 CNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGW---QRP 452
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
9-463 |
6.34e-129 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 383.18 E-value: 6.34e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAplvgelADTLGRTIDVALQDRPLG 88
Cdd:PRK14358 10 VVILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVE------AALQGSGVAFARQEQQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 89 TGHAVLCGLSALPDDYAgNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQT 168
Cdd:PRK14358 84 TGDAFLSGASALTEGDA-DILVLYGDTPLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 169 DATPSQREIREVNAGVYAFDIAALRSAlSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELA 248
Cdd:PRK14358 163 DATDAEKAIGEFNSGVYVFDARAPELA-RRIGNDNKAGEYYLTDLLGLYRAGGAQVRAFKLSDPDEVLGANDRAGLAQLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 249 SELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGAsVVRTHG-- 326
Cdd:PRK14358 242 ATLRRRINEAHMKAGVTLQDPGTILIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSVLHEGA-VIKPHSvl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 327 SSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRT 406
Cdd:PRK14358 321 EGAEVGAGSDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNKHQS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489500362 407 TVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQR 463
Cdd:PRK14358 401 KVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNLEGWSRR 457
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-457 |
1.01e-123 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 369.05 E-value: 1.01e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLgrtidvALQDRP 86
Cdd:PRK14356 6 TGALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARF------VLQEQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 87 LGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIAthRAVSAAVTVLTTTLDDPFGYGRILRTQDHeVMAIVE 166
Cdd:PRK14356 80 LGTGHALQCAWPSLTAAGLDRVLVVNGDTPLVTTDTIDDFLK--EAAGADLAFMTLTLPDPGAYGRVVRRNGH-VAAIVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 167 QTDATPSQR--EIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQL 244
Cdd:PRK14356 157 AKDYDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAVAEGMNVLGVNCGEDPNLLGVNTPAEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 245 AELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVR- 323
Cdd:PRK14356 237 VRSEELLRARIVEKHLESGVLIHAPESVRIGPRATIEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVVSSGATIHSf 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 324 THGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSK 403
Cdd:PRK14356 317 SHLEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNK 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489500362 404 RRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNI 457
Cdd:PRK14356 397 HRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQKNL 450
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
9-244 |
1.98e-113 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 334.10 E-value: 1.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELAdtlgrtIDVALQDRPLG 88
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPN------VEFVLQEEQLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 89 TGHAVLCGLSALpDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQT 168
Cdd:cd02540 75 TGHAVKQALPAL-KDFEGDVLVLYGDVPLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVEEK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489500362 169 DATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQL 244
Cdd:cd02540 154 DATEEEKAIREVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVAAVLADDEEEVLGVNDRVQL 229
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-459 |
5.15e-108 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 327.72 E-value: 5.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 6 DTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQrLIVVLGHDHQRIAPLVGELADTlgrtIDVALQD- 84
Cdd:PRK14359 2 KLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAISDD-VHVVLHHQKERIKEAVLEYFPG----VIFHTQDl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 85 --RPlGTGHAvlcgLSALPDDYAgNVVVTSGDTPLLDADTLADLIATHRAVSAAVTvlttTLDDPFGYGRILrTQDHEVM 162
Cdd:PRK14359 77 enYP-GTGGA----LMGIEPKHE-RVLILNGDMPLVEKDELEKLLENDADIVMSVF----HLADPKGYGRVV-IENGQVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 163 AIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVaGVNNRV 242
Cdd:PRK14359 146 KIVEQKDANEEELKIKSVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAVFVDEENFM-GVNSKF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 243 QLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGrcvvgpdttltdvavgdgaSVV 322
Cdd:PRK14359 225 ELAKAEEIMQERIKKNAMKQGVIMRLPETIYIESGVEFEGECELEEGVRILGKSKIEN-------------------SHI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 323 RTHGS-SSSIGDGAAVGPFTYLRPGTALgADGKLGAFVEVKNSTIgTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGT 401
Cdd:PRK14359 286 KAHSViEESIIENSDVGPLAHIRPKSEI-KNTHIGNFVETKNAKL-NGVKAGHLSYLGDCEIDEGTNIGAGTITCNYDGK 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 402 SKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIEN 459
Cdd:PRK14359 364 KKHKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIKN 421
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
263-454 |
2.13e-101 |
|
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.
Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 302.03 E-value: 2.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 263 GVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVR-THGSSSSIGDGAAVGPFT 341
Cdd:cd03353 1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKAsSVIEGAVIGNGATVGPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 342 YLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTTVGSHVRTGSDTMFV 421
Cdd:cd03353 81 HLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDNVFIGSNSQLV 160
|
170 180 190
....*....|....*....|....*....|...
gi 489500362 422 APVTIGDGAYTGAGTVVREDVPPGALAVSAGPQ 454
Cdd:cd03353 161 APVTIGDGATIAAGSTITKDVPPGALAIARARQ 193
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
11-438 |
3.13e-61 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 205.52 E-value: 3.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 11 VLAAGPGTRMR---SDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADtLGRTIDVALQDRPL 87
Cdd:TIGR03992 5 ILAAGKGTRMRpltETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSR-GGVPIEYVVQEEQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 88 GTGHAVLCglsaLPDDYAGNVVVTSGDTpLLDADTLADLIATHRAVSAAVTVltttlDDPFGYGrILRTQDHEVMAIVEQ 167
Cdd:TIGR03992 84 GTADALGS----AKEYVDDEFLVLNGDV-LLDSDLLERLIRAEAPAIAVVEV-----DDPSDYG-VVETDGGRVTGIVEK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 168 TDATPSQReireVNAGVYAFDiAALRSALSRLSSNnAQQELYLTDVIAILRSDGqtvhashvddsalvagvnnrvqlael 247
Cdd:TIGR03992 153 PENPPSNL----INAGIYLFS-PEIFELLEKTKLS-PRGEYELTDALQLLIDEG-------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 248 aselnrrvvaahqlaGVTVVDPATTWIDVdvtiGR--DtVIHPGTQLLG--RTQIGGrcVVGPDTTLT-DVAVGDGAsVV 322
Cdd:TIGR03992 201 ---------------KVKAVELDGFWLDV----GRpwD-LLDANEALLDnlEPRIEG--TVEENVTIKgPVVIGEGA-VI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 323 RthgsSSS-------IGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASS-- 393
Cdd:TIGR03992 258 R----SGTyiegpvyIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFGAGTkv 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 394 ---------VFVNYDG---TSKRR---TTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVV 438
Cdd:TIGR03992 334 anlrhddkpVKVTVKGkrvDTGRRklgAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
9-221 |
2.15e-40 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 144.65 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMR---SDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADtLGRTIDVALQDR 85
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSK-FGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PLGTGHAVLCGLSALPDDyagNVVVTSGDTpLLDADtLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIV 165
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDD---DFLVVNGDV-LTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489500362 166 EQtdatPSQREIREVNAGVYAFDiaalRSALSRLSSNNAQQELYLTDVIAILRSDG 221
Cdd:cd04181 155 EK----PTLPESNLANAGIYIFE----PEILDYIPEILPRGEDELTDAIPLLIEEG 202
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
9-231 |
1.61e-30 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 118.72 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMR---SDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADtLGRTIDVALQDR 85
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSR-FGVRITYVDEGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PLGTGHAVLCGLSALPDDyagNVVVTSGDTpLLDADtLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIV 165
Cdd:COG1208 81 PLGTGGALKRALPLLGDE---PFLVLNGDI-LTDLD-LAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489500362 166 EQTDATPSQReireVNAGVYAFDiaalRSALSRLSSNnaqQELYLTDVIAILRSDGQtVHASHVDD 231
Cdd:COG1208 156 EKPEEPPSNL----INAGIYVLE----PEIFDYIPEG---EPFDLEDLLPRLIAEGR-VYGYVHDG 209
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
297-439 |
2.10e-25 |
|
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100060 [Multi-domain] Cd Length: 163 Bit Score: 101.90 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 297 QIGGRCVVGPDTTLTDVAVGDGASVvrthgssssIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLT 376
Cdd:cd05636 13 TIKGPVWIGEGAIVRSGAYIEGPVI---------IGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 377 YVGDADIGEYSNIGASSVFVNY--DGTS-------KRRTT--------VGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVR 439
Cdd:cd05636 84 YVGDSVLGENVNLGAGTITANLrfDDKPvkvrlkgERVDTgrrklgaiIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
9-222 |
1.70e-22 |
|
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.
Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 95.70 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRS---DTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGElADTLGRTIDVALQDR 85
Cdd:cd06915 1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGD-GYRGGIRIYYVIEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PLGTGHAVLCGLSALPDDyagNVVVTSGDTpLLDADtLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIV 165
Cdd:cd06915 80 PLGTGGAIKNALPKLPED---QFLVLNGDT-YFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489500362 166 EqTDATPSQREIrevNAGVYAFDiaalRSALSRLSSNNAQQElylTDVIAILRSDGQ 222
Cdd:cd06915 155 E-KGPGAAPGLI---NGGVYLLR----KEILAEIPADAFSLE---ADVLPALVKRGR 200
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
7-139 |
1.96e-21 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 91.47 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMRSdtPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLgrtidVALQDRP 86
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVV-----VINPDWE 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489500362 87 LGTGHAVLCGLSALPDDYAGnVVVTSGDTPLLDADTLADLIATHRAVSAAVTV 139
Cdd:cd04182 74 EGMSSSLAAGLEALPADADA-VLILLADQPLVTAETLRALIDAFREDGAGIVA 125
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
7-139 |
2.03e-21 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 91.76 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMrsDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLgrtidVALQDRP 86
Cdd:COG2068 4 VAAIILAAGASSRM--GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRV-----VVNPDWE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489500362 87 LGTGHAVLCGLSALPDDYAGnVVVTSGDTPLLDADTLADLIATHRAVSAAVTV 139
Cdd:COG2068 77 EGMSSSLRAGLAALPADADA-VLVLLGDQPLVTAETLRRLLAAFRESPASIVA 128
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
9-187 |
2.18e-17 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 81.10 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDT---PKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLGRTIDVALQDR 85
Cdd:cd06425 3 ALILVGGYGTRLRPLTltvPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIETE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PLGTGhavlcGLSALPDDYagnvvVTSGDTP--LLDADT-----LADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQD 158
Cdd:cd06425 83 PLGTA-----GPLALARDL-----LGDDDEPffVLNSDVicdfpLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDEN 152
|
170 180 190
....*....|....*....|....*....|
gi 489500362 159 H-EVMAIVEQtdatPSQREIREVNAGVYAF 187
Cdd:cd06425 153 TgRIERFVEK----PKVFVGNKINAGIYIL 178
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
10-233 |
2.64e-17 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 82.45 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 10 LVLAAGPGTRMRSDT---PKVLHTLAGRSMLSHVLHAIAkLAPQR--LIVVLGHDHQRIAPLVGELADtLGRTIDVALQD 84
Cdd:COG1209 4 IILAGGSGTRLRPLTltvSKQLLPVYDKPMIYYPLSTLM-LAGIReiLIISTPEDGPQFERLLGDGSQ-LGIKISYAVQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 85 RPLGTGHAVLCGLSALPDDyagNVVVTSGDTpLLDADTLADLIATHRAVSAAVTVLTTTLDDP--FG------YGRILRt 156
Cdd:COG1209 82 EPLGLAHAFIIAEDFIGGD---PVALVLGDN-IFYGDGLSELLREAAARESGATIFGYKVEDPerYGvvefdeDGRVVS- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489500362 157 qdhevmaIVEQTDATPSQREIrevnAGVYAFDiAALRSALSRLsSNNAQQELYLTDVIAILRSDGQTVHASHVDDSA 233
Cdd:COG1209 157 -------LEEKPKEPKSNLAV----TGLYFYD-NDVVEIAKNL-KPSARGELEITDANQAYLERGKLVVELLGRGFA 220
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
10-225 |
1.88e-16 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 78.25 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 10 LVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAP-QRLIVVLGHDHQriaPLVGELADTLGRTIDVAL------ 82
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVPPDDI---EYFEELLAKYGIDKPVRVvaggat 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 83 -QDrplgtghAVLCGLSALPDDyAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVL--TTTL----DDpfgyGRILR 155
Cdd:COG1211 78 rQD-------SVRNGLEALPDD-DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALpvTDTIkrvdDD----GRVTE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 156 TQDHEVMAIVeQtdaTPsQreirevnagvyAFDIAALRSALSRLssnnAQQELYLTDVIAILRSDGQTVH 225
Cdd:COG1211 146 TVDRSGLWAA-Q---TP-Q-----------GFRLDLLLEAHEAA----AADGLEFTDDASLVERLGLPVR 195
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
9-142 |
2.25e-16 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 76.46 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDtpKVLHTLAGRSMLSHVLhAIAKLAPQRLIVVLGHDHQRiaplvgelADTLGRTIDVALQDRP-L 87
Cdd:pfam12804 1 AVILAGGRSSRMGGD--KALLPLGGKPLLERVL-ERLRPAGDEVVVVANDEEVL--------AALAGLGVPVVPDPDPgQ 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489500362 88 GTGHAVLCGLSALPDdyAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTT 142
Cdd:pfam12804 70 GPLAGLLAALRAAPG--ADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVY 122
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
9-231 |
1.53e-14 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 72.97 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMR---SDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLgRTIDVALQDR 85
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPDV-TFVYNPDYDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 pLGTGHAVLCGLSALPDDyagnVVVTSGDTpLLDADTLADLIATHRAVSAAVTVLTTTLDDpfgygrilrtqdhEVMAIV 165
Cdd:COG1213 81 -TNNIYSLWLAREALDED----FLLLNGDV-VFDPAILKRLLASDGDIVLLVDRKWEKPLD-------------EEVKVR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489500362 166 EQTDATPSQ--REIREVNA-----GVYAF---DIAALRSALSRLSSNNAQQeLYLTDVIAILRSDGQTVHASHVDD 231
Cdd:COG1213 142 VDEDGRIVEigKKLPPEEAdgeyiGIFKFsaeGAAALREALEALIDEGGPN-LYYEDALQELIDEGGPVKAVDIGG 216
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
10-230 |
2.93e-14 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 72.22 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 10 LVLAAGPGTRMRSDT---PKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGElADTLGRTIDVALQDRP 86
Cdd:cd04189 4 LILAGGKGTRLRPLTytrPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGD-GSRFGVRITYILQEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 87 LGTGHAVLCGLSALPDD----YAGNVVVTSGDTPLLDAdtladliatHRAVSAAVTVLTTTLDDPFGYGrILRTQDHEVM 162
Cdd:cd04189 83 LGLAHAVLAARDFLGDEpfvvYLGDNLIQEGISPLVRD---------FLEEDADASILLAEVEDPRRFG-VAVVDDGRIV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 163 AIVEQTDATPSQREIrevnAGVYAF--DIAalrSALSRLSSnNAQQELYLTDVIAILRSDGQTVHASHVD 230
Cdd:cd04189 153 RLVEKPKEPPSNLAL----VGVYAFtpAIF---DAISRLKP-SWRGELEITDAIQWLIDRGRRVGYSIVT 214
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
274-460 |
8.88e-14 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 70.13 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 274 IDVDVTIGRDTVIHPGtqllgrTQIGGRCVVGPDTTLtdvavgdgasvvrthGSSSSIGDGAAVGPFTYLRPGTALGADG 353
Cdd:cd03352 16 IGEGVVIGDGVVIGPG------VVIGDGVVIGDDCVI---------------HPNVTIYEGCIIGDRVIIHSGAVIGSDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 354 -------------------KLGAFVEV-KNST----------IGTGTKVPHLTYVG-DADIGEYSNIGASSVFvnydGTS 402
Cdd:cd03352 75 fgfapdgggwvkipqlggvIIGDDVEIgANTTidrgalgdtvIGDGTKIDNLVQIAhNVRIGENCLIAAQVGI----AGS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 403 krrTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGAlAVSAGPQRNIENW 460
Cdd:cd03352 151 ---TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGE-YVSGTPAQPHREW 204
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
6-139 |
1.35e-13 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 69.07 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 6 DTAVLVLAAGPGTRMRSDtpKVLHTLAGRSMLSHVLHAIAKLAPQrlIVVLGHDHQRIA----PLVGELADTLGrtidva 81
Cdd:COG0746 4 PITGVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLRPQVDE--VVIVANRPERYAalgvPVVPDDPPGAG------ 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 82 lqdrPLGtghAVLCGLSALPDDYagnVVVTSGDTPLLDADTLADLIAtHRAVSAAVTV 139
Cdd:COG0746 74 ----PLA---GILAALEAAPAEW---VLVLACDMPFLPPDLVRRLLE-ALEEGADAVV 120
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
349-449 |
2.17e-13 |
|
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.
Pssm-ID: 100048 [Multi-domain] Cd Length: 119 Bit Score: 66.76 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 349 LGADGKLGAFVEV-KNSTIGTGTKVPHLTYVGD-ADIGEYSNIGASSVFVN--------YDGTSKRRTTVGSHVRTGSDT 418
Cdd:cd03358 1 IGDNCIIGTNVFIeNDVKIGDNVKIQSNVSIYEgVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANA 80
|
90 100 110
....*....|....*....|....*....|.
gi 489500362 419 MFVAPVTIGDGAYTGAGTVVREDVPPGALAV 449
Cdd:cd03358 81 TILPGVTIGEYALVGAGAVVTKDVPPYALVV 111
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
10-222 |
3.71e-13 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 69.20 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 10 LVLAAGPGTRMRSDT----PKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGhdhQRIAPLVGE-LADT--LGRTIDVAL 82
Cdd:pfam00483 3 IILAGGSGTRLWPLTrtlaKPLVPVGGKYPLIDYPLSRLANAGIREIIVILT---QEHRFMLNElLGDGskFGVQITYAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 83 QDRPLGTGHAVLCGLSALPDDYaGNVVVTSGDtpLLDADTLADLIATHRAVSAA--VTVLTTTLDDPFGYGRILRTQDHE 160
Cdd:pfam00483 80 QPEGKGTAPAVALAADFLGDEK-SDVLVLGGD--HIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFDDNGR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489500362 161 VMAIVEQtdatPSQREIRE-VNAGVYAFDIAALRSALSRLsSNNAQQELYLTDVIAILRSDGQ 222
Cdd:pfam00483 157 VIRFVEK----PKLPKASNyASMGIYIFNSGVLDFLAKYL-EELKRGEDEITDILPKALEDGK 214
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
330-449 |
5.28e-13 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 66.05 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 330 SIGDGAAVGPFTYLRPGTAlgadgKLGafvevKNSTIGTGTkvpHLTYVGDADIGEYSNIGASSVFVNY---------DG 400
Cdd:COG0110 10 RIGDGVVIGPGVRIYGGNI-----TIG-----DNVYIGPGV---TIDDPGGITIGDNVLIGPGVTILTGnhpiddpatFP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489500362 401 TSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAV 449
Cdd:COG0110 77 LRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVA 125
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
7-225 |
4.20e-11 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 62.54 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHqRIAPLVGELADTLGRTIDVAL---- 82
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPD-DIDLAKELAKYGLSKVVKIVEggat 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 83 -QDrplgtghAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVL--TTTL---DDPfgyGRILRT 156
Cdd:cd02516 80 rQD-------SVLNGLKALPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVpvTDTIkrvDDD---GVVVET 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489500362 157 QDHEVMAIVEqtdaTPsQreirevnagvyAFDIAALRSALSRLSSNNaqqeLYLTDVIAILRSDGQTVH 225
Cdd:cd02516 150 LDREKLWAAQ----TP-Q-----------AFRLDLLLKAHRQASEEG----EEFTDDASLVEAAGGKVA 198
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
8-129 |
5.15e-11 |
|
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.
Pssm-ID: 274516 Cd Length: 188 Bit Score: 61.59 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 8 AVLVLAAGPGTRMRsdTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLvgeLADTLGRTIDVALQDRpL 87
Cdd:TIGR03310 1 DAIILAAGLSSRMG--QNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVAL---LANHSNITLVHNPQYA-E 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489500362 88 GTGHAVLCGLsALPDDYAGnVVVTSGDTPLLDADTLADLIAT 129
Cdd:TIGR03310 75 GQSSSIKLGL-ELPVQSDG-YLFLLGDQPFVTPDIIQLLLEA 114
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
9-212 |
1.61e-10 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 60.92 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRiaPLVGELADTLGRTIDVAlqdrplg 88
Cdd:PRK00155 6 AIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDR--PDFAELLLAKDPKVTVV------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 89 TG-----HAVLCGLSALPDDyaGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVL--TTTL---DDPfgyGRILRTQD 158
Cdd:PRK00155 77 AGgaerqDSVLNGLQALPDD--DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVpvKDTIkrsDDG---GGIVDTPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489500362 159 HEVMAIVeQtdaTPsQreirevnagvyAFDIAALRSALSRLSsnnaQQELYLTD 212
Cdd:PRK00155 152 RSGLWAA-Q---TP-Q-----------GFRIELLREALARAL----AEGKTITD 185
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
362-449 |
1.83e-10 |
|
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 57.85 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 362 KNSTIGTGTkvpHLTYVGDADIGEYSNIGASSVFVNYD------------GTSKRRTTVGSHVRTGSDTMFVAPVTIGDG 429
Cdd:cd04647 6 DNVYIGPGC---VISAGGGITIGDNVLIGPNVTIYDHNhdiddperpieqGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82
|
90 100
....*....|....*....|
gi 489500362 430 AYTGAGTVVREDVPPGALAV 449
Cdd:cd04647 83 AVVGAGSVVTKDVPPNSIVA 102
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
7-128 |
1.98e-10 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 59.90 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 7 TAVLVLAAGPGTRMrsDTPKVLHTLAGRSMLSHVlhaIAKLAPQ--RLIVVLGHDHQRIA----PLVGELADTLGrtidv 80
Cdd:cd02503 1 ITGVILAGGKSRRM--GGDKALLELGGKPLLEHV---LERLKPLvdEVVISANRDQERYAllgvPVIPDEPPGKG----- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489500362 81 alqdrPLGtghAVLCGLSALPDDYagnVVVTSGDTPLLDADTLADLIA 128
Cdd:cd02503 71 -----PLA---GILAALRAAPADW---VLVLACDMPFLPPELLERLLA 107
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
8-168 |
2.09e-10 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 213532 Cd Length: 217 Bit Score: 60.38 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 8 AVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAP-QRLIVVLGHDHQRIAPLvgELADTLGRTIDVALQDRp 86
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAiDEVVVVVSPDDTEFFQK--YLVARAVPKIVAGGDTR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 87 lgtGHAVLCGLSALPDdyAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVL--TTTLDDPFGYGRILRTQDHEVMAI 164
Cdd:TIGR00453 78 ---QDSVRNGLKALKD--AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALpvADTLKRVEADGFVVETVDREGLWA 152
|
....
gi 489500362 165 VeQT 168
Cdd:TIGR00453 153 A-QT 155
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
9-205 |
5.48e-10 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 59.96 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGP--GTRMRS---DTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLG-HDHQRIAPLVGELADTLGRTIDVAL 82
Cdd:cd06428 1 AVILVGGPqkGTRFRPlslDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGfYPESVFSDFISDAQQEFNVPIRYLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 83 QDRPLGTGHavlcGLSALPDD-YAGN---VVVTSGDT----PlldadtLADLIATHRAVSAAVTVLTT--TLDDPFGYGR 152
Cdd:cd06428 81 EYKPLGTAG----GLYHFRDQiLAGNpsaFFVLNADVccdfP------LQELLEFHKKHGASGTILGTeaSREQASNYGC 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489500362 153 ILR-TQDHEVMAIVEQtdatPSQREIREVNAGVYAFDIAALRsALSRLSSNNAQ 205
Cdd:cd06428 151 IVEdPSTGEVLHYVEK----PETFVSDLINCGVYLFSPEIFD-TIKKAFQSRQQ 199
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
10-147 |
7.40e-10 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 59.12 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 10 LVLAAGPGTRMRS---DTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHdhqriapLVGELADTLGRT---IDVALQ 83
Cdd:cd06422 3 MILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHH-------LADQIEAHLGDSrfgLRITIS 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 84 D---RPLGTGHavlcGLS-ALPDDYAGNVVVTSGDTpLLDADtLADLIATHRAVSAAVTVLTTTLDDP 147
Cdd:cd06422 76 DepdELLETGG----GIKkALPLLGDEPFLVVNGDI-LWDGD-LAPLLLLHAWRMDALLLLLPLVRNP 137
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
4-139 |
2.57e-09 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 56.73 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 4 PGDTAVLVLAAGPGTRMR-SDtpKVLHTLAGRSMLSHVlhaIAKLAPQ--RLIVVLGHDHQRIA----PLVG-ELADTLG 75
Cdd:PRK00317 1 MPPITGVILAGGRSRRMGgVD--KGLQELNGKPLIQHV---IERLAPQvdEIVINANRNLARYAafglPVIPdSLADFPG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489500362 76 rtidvalqdrPLGtGhaVLCGLSALPDDYagnVVVTSGDTPLLDADTLADLIATHRAVSAAVTV 139
Cdd:PRK00317 76 ----------PLA-G--ILAGLKQARTEW---VLVVPCDTPFIPPDLVARLAQAAGKDDADVAW 123
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
364-438 |
5.22e-09 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 53.02 E-value: 5.22e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489500362 364 STIGTGTKVPHLTYVGD-ADIGEYSNIGASSVFVNYDG-TSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVV 438
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGpNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
326-449 |
8.56e-09 |
|
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.
Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 55.18 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 326 GSSSSIGDGAAVGPFTYLRPGTALGadgklgafvevKNSTIGTGTKVPHltyvgDADIGEYSNIgASSVFVNydGtskrR 405
Cdd:cd03360 94 SPSAVIGEGCVIMAGAVINPDARIG-----------DNVIINTGAVIGH-----DCVIGDFVHI-APGVVLS--G----G 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489500362 406 TTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAV 449
Cdd:cd03360 151 VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVV 194
|
|
| alt_bact_glmU |
TIGR03991 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
264-455 |
1.06e-08 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Homologs of this enzyme are identified in a number of bacterial organisms and modeled here. A number of these are observed in proximity to the GlmS and GlmM genes, and phylogenetic profiling by PPP identifies the LEPBI_I0518 gene in Leptospira biflexa as a likely Glm-system candidate. Multiple sequence alignments of these bacterial homologs with their archaeal counterparts reveals significant structural differences, necessitating the construction of separate models. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 274907 [Multi-domain] Cd Length: 337 Bit Score: 56.93 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 264 VTVVDPAttwidvDVTIGRDTVIHPGTQLLGRtqiGGRCVVGPDTTLTDVAVGDGASVVrthGSSSSIGDGAAVgpftyl 343
Cdd:TIGR03991 116 VVVVNPS------HVFIEEGATVRPGAVLDAS---DGPIYIGKDARIEPFSFLEGPVYI---GPGARVKAGARI------ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 344 RPGTALGADGKLGAfvEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGA----SSVFVNYdGTSKRRTT------------ 407
Cdd:TIGR03991 178 YGGTSIGPTCKIGG--EVENSIIEGYSNKHHDGFLGHSYLGSWCNLGAgtntSDLKNNY-GEVKIREGdgfvdtglqflg 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489500362 408 --VGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQR 455
Cdd:TIGR03991 255 lfMGDHSKCGIGTMFNTGTVVGVGSNIFGSGFPPKYVPSFTWGGSGGFTE 304
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
9-225 |
1.16e-08 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Pssm-ID: 460075 Cd Length: 219 Bit Score: 55.53 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRiaplvGELADTLGRTiDVALQDRPLG 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDT-----PEFRQLLGDP-SIQLVAGGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 89 TGHAVLCGLSALPDDyAGNVVVTSGDTPLLDADTLADLIA---THRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIV 165
Cdd:pfam01128 75 RQDSVLNGLKALAGT-AKFVLVHDGARPCLPHADLARLLAaleTGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 166 EqtdaTPSqreirevnagvyAFDIAALRSALSRlssnNAQQELYLTDVIAILRSDGQTVH 225
Cdd:pfam01128 154 Q----TPQ------------GFRVDLLLAAHQR----GDQPGAEITDDASLVEHAGGSVQ 193
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
293-449 |
1.87e-08 |
|
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.
Pssm-ID: 274656 [Multi-domain] Cd Length: 201 Bit Score: 54.42 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 293 LGRTQIGGRCVVGPDTTLTD---------VAVGD--------------GASVVRTHGSSSSIGDGAAVGPFTYLRPGTAL 349
Cdd:TIGR03570 35 LQGTEVDGLPVLGGDEDLLRyppdevdlvVAIGDnklrrrlveklkakGYRFATLIHPSAIVSPSASIGEGTVIMAGAVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 350 GADGKLGAFVevknsTIGTGTKVPHltyvgDADIGEYSNIgASSVFVNydgtskRRTTVGSHVRTGSDTMFVAPVTIGDG 429
Cdd:TIGR03570 115 NPDVRIGDNV-----IINTGAIVEH-----DCVIGDFVHI-APGVTLS------GGVVIGEGVFIGAGATIIQGVTIGAG 177
|
170 180
....*....|....*....|
gi 489500362 430 AYTGAGTVVREDVPPGALAV 449
Cdd:TIGR03570 178 AIVGAGAVVTKDIPDGGVVV 197
|
|
| LbH_XAT |
cd03349 |
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
337-465 |
9.23e-08 |
|
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.
Pssm-ID: 100040 [Multi-domain] Cd Length: 145 Bit Score: 51.39 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 337 VGPFTYL-RPGTALGADG-KLGAFVEV-KNSTIGTGTKVP--HLTYVGDADIGEYSNIGASSvfvnYDGTSKRRTTVGSH 411
Cdd:cd03349 4 VGDYSYGsGPDCDVGGDKlSIGKFCSIaPGVKIGLGGNHPtdWVSTYPFYIFGGEWEDDAKF----DDWPSKGDVIIGND 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489500362 412 VRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPgaLAVSAG-PQRNIenwvqRKR 465
Cdd:cd03349 80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPP--YAIVGGnPAKVI-----RYR 127
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
274-460 |
1.61e-07 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 53.22 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 274 IDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLT-DVAVGDGasvVRTHgssssigdgaavgpftylrPGTALGAD 352
Cdd:PRK00892 127 IGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYhAVRIGNR---VIIH-------------------SGAVIGSD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 353 G-------------------KLGAFVEV-KNSTIGTGTkvphltyVGDADIGEYS---N---------IGASSVFVNYDG 400
Cdd:PRK00892 185 GfgfandrggwvkipqlgrvIIGDDVEIgANTTIDRGA-------LDDTVIGEGVkidNlvqiahnvvIGRHTAIAAQVG 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 401 TSKrRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENW 460
Cdd:PRK00892 258 IAG-STKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEW 316
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
274-460 |
1.77e-07 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 53.10 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 274 IDVDVTIGRDTVIHPGtqllgrTQIGGRCVVGPDTTLtdvavgdGASVVrthgssssIGDGAAVGPFTYLRPGTALGADG 353
Cdd:COG1044 123 IGAGVVIGDGVVIGPG------VVIGDGVVIGDDCVL-------HPNVT--------IYERCVIGDRVIIHSGAVIGADG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 354 --------------------KLGAFVEV-KNST----------IGTGTKVPHLTYVG-DADIGEYSNIGASSVFvnydGT 401
Cdd:COG1044 182 fgfapdedggwvkipqlgrvVIGDDVEIgANTTidrgalgdtvIGDGTKIDNLVQIAhNVRIGEHTAIAAQVGI----AG 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489500362 402 SkrrTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGAlAVSAGPQRNIENW 460
Cdd:COG1044 258 S---TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGG-VYSGSPAQPHREW 312
|
|
| LbH_SAT |
cd03354 |
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
365-449 |
5.41e-07 |
|
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.
Pssm-ID: 100045 [Multi-domain] Cd Length: 101 Bit Score: 47.82 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 365 TIGTGTKVPHLTYV---GDADIGEYSNIGASSVF-VNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVRE 440
Cdd:cd03354 10 KIGPGLFIDHGTGIvigETAVIGDNCTIYQGVTLgGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTK 89
|
....*....
gi 489500362 441 DVPPGALAV 449
Cdd:cd03354 90 DVPANSTVV 98
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
9-217 |
9.35e-07 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 49.92 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRMRS---DTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLvgeladtLGRTIDVALQDR 85
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEEL-------LKKYPNIKFVYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 86 PL----GTGHAVLCGLSALPDDyagnVVVTSGDTpLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGygriLRTQDHEV 161
Cdd:cd02523 74 PDyaetNNIYSLYLARDFLDED----FLLLEGDV-VFDPSILERLLSSPADNAILVDKKTKEWEDEYV----KDLDDAGV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489500362 162 MAIVEQTDATPSQREIREVnaGVYAF---DIAALRSALSRLSSNNAQQeLYLTDVIAIL 217
Cdd:cd02523 145 LLGIISKAKNLEEIQGEYV--GISKFspeDADRLAEALEELIEAGRVN-LYYEDALQRL 200
|
|
| lacA |
PRK09527 |
galactoside O-acetyltransferase; Reviewed |
407-465 |
7.93e-06 |
|
galactoside O-acetyltransferase; Reviewed
Pssm-ID: 181930 [Multi-domain] Cd Length: 203 Bit Score: 46.92 E-value: 7.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 407 TVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGalAVSAG-PQRNIENWVQRKR 465
Cdd:PRK09527 133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPN--VVAAGvPCRVIREINDRDK 190
|
|
| PLN02357 |
PLN02357 |
serine acetyltransferase |
366-457 |
7.96e-06 |
|
serine acetyltransferase
Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 47.95 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 366 IGTGTKVPHLTYVgdaDIGEYSNIGAS-SVF--VNYDGTSK----RRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVV 438
Cdd:PLN02357 235 IGQGILLDHATGV---VIGETAVVGNNvSILhnVTLGGTGKqsgdRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVV 311
|
90
....*....|....*....
gi 489500362 439 REDVPPGALAVsAGPQRNI 457
Cdd:PLN02357 312 LKDVPPRTTAV-GNPARLI 329
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
12-141 |
1.14e-05 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 46.03 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 12 LAAGPGTRMRsDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHqriaPLVGELADTLG-RTIDVAlqdrplGTG 90
Cdd:COG2266 1 MAGGKGTRLG-GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNT----PKTREYLKERGvEVIETP------GEG 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489500362 91 -----HAVLCGLSalpddyaGNVVVTSGDTPLLDADTLADLIATHRAV-SAAVTVLT 141
Cdd:COG2266 70 yvedlNEALESIS-------GPVLVVPADLPLLTPEIIDDIIDAYLESgKPSLTVVV 119
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
278-361 |
2.98e-05 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 42.24 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 278 VTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLtdvavgdGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGA 357
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVI-------GAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73
|
....
gi 489500362 358 FVEV 361
Cdd:cd00208 74 GAVV 77
|
|
| LpxA |
COG1043 |
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
274-444 |
3.08e-05 |
|
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440665 [Multi-domain] Cd Length: 258 Bit Score: 45.39 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 274 IDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPdttltdvavgdGASVvrthgssssigdGAA------VGPFTYLRpgt 347
Cdd:COG1043 28 IGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFP-----------FASI------------GEEpqdlkyKGEPTRLE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 348 aLGADGKLGAFVevknsTIGTGTKVPH-LTYVGD-------ADIGEYSNIGASSVFVNYdgtskrrTTVGSHVRTGSDTM 419
Cdd:COG1043 82 -IGDNNTIREFV-----TIHRGTVQGGgVTRIGDdnllmayVHVAHDCVVGNNVILANN-------ATLAGHVEVGDHAI 148
|
170 180 190
....*....|....*....|....*....|.
gi 489500362 420 F--VAPV----TIGDGAYTGAGTVVREDVPP 444
Cdd:COG1043 149 IggLSAVhqfvRIGAHAMVGGGSGVVKDVPP 179
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
274-444 |
3.82e-05 |
|
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.
Pssm-ID: 100042 [Multi-domain] Cd Length: 254 Bit Score: 45.12 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 274 IDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPdttltdvavgdGASV------VRTHGSSSS--IGDGAAVGPFTYLRP 345
Cdd:cd03351 26 IGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFP-----------FASIgeapqdLKYKGEPTRleIGDNNTIREFVTIHR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 346 GTALGaDGKlgafvevknSTIG------TGTKVPHLTYVGDadigeysNIgassVFVNYdgtskrrTTVGSHVRTGSDTM 419
Cdd:cd03351 95 GTAQG-GGV---------TRIGnnnllmAYVHVAHDCVIGN-------NV----ILANN-------ATLAGHVEIGDYAI 146
|
170 180 190
....*....|....*....|....*....|.
gi 489500362 420 F--VAPV----TIGDGAYTGAGTVVREDVPP 444
Cdd:cd03351 147 IggLSAVhqfcRIGRHAMVGGGSGVVQDVPP 177
|
|
| CysE |
COG1045 |
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
389-449 |
7.16e-05 |
|
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440667 [Multi-domain] Cd Length: 174 Bit Score: 43.53 E-value: 7.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489500362 389 IGASSVfvnydGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAV 449
Cdd:COG1045 106 LGGTGK-----EKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVV 161
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
2-140 |
1.05e-04 |
|
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional
Pssm-ID: 236492 [Multi-domain] Cd Length: 378 Bit Score: 44.45 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 2 TFPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGH--DHQRIAPLVGELADTLGRTID 79
Cdd:PRK09382 1 TLMSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHpdDIAYMKKALPEIKFVTLVTGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489500362 80 VALQDrplgtghAVLCGLSALPDDYagnVVVTSGDTPLLDADTLADLIATHRAVSAAVTVL 140
Cdd:PRK09382 81 ATRQE-------SVRNALEALDSEY---VLIHDAARPFVPKELIDRLIEALDKADCVLPAL 131
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
9-140 |
1.37e-04 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 43.03 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 9 VLVLAAGPGTRM---RSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQR-IAPLVGELADTLGRTIDVAL-- 82
Cdd:cd04198 3 AVILAGGGGSRLyplTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAeISTYLRSFPLNLKQKLDEVTiv 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489500362 83 QDRPLGTGHAvlcgLSALPDDYAGNVVVTSGDTpLLDADtLADLIATHRAVSAAVTVL 140
Cdd:cd04198 83 LDEDMGTADS----LRHIRKKIKKDFLVLSCDL-ITDLP-LIELVDLHRSHDASLTVL 134
|
|
| PLN02694 |
PLN02694 |
serine O-acetyltransferase |
366-455 |
2.31e-04 |
|
serine O-acetyltransferase
Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 43.09 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 366 IGTGTKVPHLTYVGdadIGEYSNIGAS-SVF--VNYDGTSK----RRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVV 438
Cdd:PLN02694 169 IGKGILFDHATGVV---IGETAVIGNNvSILhhVTLGGTGKacgdRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVV 245
|
90
....*....|....*..
gi 489500362 439 REDVPPGALAVsAGPQR 455
Cdd:PLN02694 246 LIDVPPRTTAV-GNPAR 261
|
|
| PRK05289 |
PRK05289 |
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
274-448 |
2.85e-04 |
|
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 42.78 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 274 IDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPdttltdvavgdGASV------VRTHGSSSS--IGDGAAVGPFTYLRP 345
Cdd:PRK05289 29 IGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFP-----------FASIgedpqdLKYKGEPTRlvIGDNNTIREFVTINR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 346 GTAlGADGKlgafvevknSTIG------TGTKVPHltyvgDADIGeySNIgassVFVNYdgtskrrTTVGSHVRTGSDTM 419
Cdd:PRK05289 98 GTV-QGGGV---------TRIGdnnllmAYVHVAH-----DCVVG--NHV----ILANN-------ATLAGHVEVGDYAI 149
|
170 180 190
....*....|....*....|....*....|....*
gi 489500362 420 F--VAPV----TIGDGAYTGAGTVVREDVPPGALA 448
Cdd:PRK05289 150 IggLTAVhqfvRIGAHAMVGGMSGVSQDVPPYVLA 184
|
|
| LbH_MAT_GAT |
cd03357 |
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
424-449 |
6.22e-04 |
|
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100047 [Multi-domain] Cd Length: 169 Bit Score: 40.48 E-value: 6.22e-04
10 20
....*....|....*....|....*.
gi 489500362 424 VTIGDGAYTGAGTVVREDVPPGALAV 449
Cdd:cd03357 137 VTIGDNSVIGAGSVVTKDIPANVVAA 162
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
327-433 |
7.67e-04 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 41.16 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 327 SSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNST-IGTGTKVPHLTYVGDA--DI---GEYSN--IGASSVFVNY 398
Cdd:PRK12461 10 PSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTrIGKNNKIHQGAVVGDEpqDFtykGEESRleIGDRNVIREG 89
|
90 100 110
....*....|....*....|....*....|....*
gi 489500362 399 dGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTG 433
Cdd:PRK12461 90 -VTIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIG 123
|
|
| LbH_paaY_like |
cd04745 |
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
286-420 |
9.87e-04 |
|
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.
Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 39.66 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 286 IHPGTQLLGRTQIGGRCVVGPDTTLTdvavGDGASVVrthgssssIGDGAAV--GPFTYLRPG--TALGADGKLGAFVEV 361
Cdd:cd04745 9 VHPTAVLIGDVIIGKNCYIGPHASLR----GDFGRIV--------IRDGANVqdNCVIHGFPGqdTVLEENGHIGHGAIL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489500362 362 KNSTIGTGTKVPHLTYVGD-ADIGEYSNIGASSvFVNYDGTSKRRTTV----GSHVRTGSDTMF 420
Cdd:cd04745 77 HGCTIGRNALVGMNAVVMDgAVIGEESIVGAMA-FVKAGTVIPPRSLIagspAKVIRELSDEEV 139
|
|
| LbH_wcaF_like |
cd05825 |
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
420-447 |
1.43e-03 |
|
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.
Pssm-ID: 100063 [Multi-domain] Cd Length: 107 Bit Score: 38.36 E-value: 1.43e-03
10 20
....*....|....*....|....*....
gi 489500362 420 FVAP-VTIGDGAYTGAGTVVREDVPPGAL 447
Cdd:cd05825 70 FVGPgVTIGEGAVVGARSVVVRDLPAWTV 98
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
5-55 |
1.82e-03 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 40.10 E-value: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489500362 5 GDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVV 55
Cdd:PLN02728 23 KSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVV 73
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
26-132 |
2.19e-03 |
|
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.
Pssm-ID: 133011 Cd Length: 233 Bit Score: 39.86 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489500362 26 KVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLV------------GELADTLGRTIDVALQdrplgtghav 93
Cdd:cd02518 16 KVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATSTNEEDDPLEalakklgvkvfrGSEEDVLGRYYQAAEE---------- 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489500362 94 lcglsalpddYAGNVVV-TSGDTPLLDADTLADLIATHRA 132
Cdd:cd02518 86 ----------YNADVVVrITGDCPLIDPEIIDAVIRLFLK 115
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
277-306 |
3.60e-03 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 35.01 E-value: 3.60e-03
10 20 30
....*....|....*....|....*....|
gi 489500362 277 DVTIGRDTVIHPGTQLLGRTQIGGRCVVGP 306
Cdd:pfam00132 1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
|
|
| |
