|
Name |
Accession |
Description |
Interval |
E-value |
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
2-456 |
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: 793.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGqEGLHFALQQPQQGTGH 81
Cdd:COG1207 3 LAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD-LDVEFVLQEEQLGTGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLlegDGKDDVTLVLYGDVPLVQPDTLRRLLAAR---GDGAAVLTEVLDDSTGYGRIVRDAAGQVCRIVEHKD 158
Cdd:COG1207 82 AVQQALPAL---PGDDGTVLVLYGDVPLIRAETLKALLAAHraaGAAATVLTAELDDPTGYGRIVRDEDGRVLRIVEEKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 159 ASEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELER 238
Cdd:COG1207 159 ATEEQRAIREINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADGLKVAAVQPEDPWEVLGVNDRVQLAEAER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 239 RWQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEaYSHLQD 318
Cdd:COG1207 239 ILQRRIAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 319 AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVI 398
Cdd:COG1207 318 AVVGAGATVGPFARLRPGTVLGEGVKIGNFVEVKNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHRTVI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1337428519 399 EDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGWQRPTKK 456
Cdd:COG1207 398 GDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIEGWVRPKKK 455
|
|
| glmU |
TIGR01173 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
2-456 |
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: 688.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGgQEGLHFALQQPQQGTGH 81
Cdd:TIGR01173 1 LSVVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALA-NRDVNWVLQAEQLGTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLlegdGKDDVTLVLYGDVPLVQPDTLRRLLAA-RGDGAAVLTEVLDDSTGYGRIVRDAAGQVCRIVEHKDAS 160
Cdd:TIGR01173 80 AVLQALPFL----SDDGDVLVLYGDVPLISAETLERLLEAhRQNGITLLTAKLDDPTGYGRIIRENDGKVTAIVEDKDAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 161 EAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELERRW 240
Cdd:TIGR01173 156 AEQKAIKEINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRAVQVDDSDEVLGVNDRLQLAQLERIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 241 QAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQDAQ 320
Cdd:TIGR01173 236 QRRIAKKLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKVKIGDDVVIGPGCVIKNSVIGSNVVIKAYSVLEGSE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 321 VGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVIED 400
Cdd:TIGR01173 316 IGEGCDVGPFARLRPGSVLGAGVHIGNFVEVKNARIGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHKTIIGD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428519 401 DAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGWQRPTKK 456
Cdd:TIGR01173 396 GVFIGSNTQLVAPVKVGDGATIAAGSTVTKDVPEGALAISRARQRNIEGWVRPKKK 451
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-456 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 641.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGgQEGLHFALQQPQQGTGH 81
Cdd:PRK09451 6 MSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLA-DEPLNWVLQAEQLGTGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLlegdGKDDVTLVLYGDVPLVQPDTLRRLLAARGDGA-AVLTEVLDDSTGYGRIVRDAaGQVCRIVEHKDAS 160
Cdd:PRK09451 85 AMQQAAPFF----ADDEDILMLYGDVPLISVETLQRLRDAKPQGGiGLLTVKLDNPTGYGRITREN-GKVVGIVEQKDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 161 EAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELERRW 240
Cdd:PRK09451 160 DEQRQIQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGREIVAVHPQRLSEVEGVNNRLQLARLERVY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 241 QAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQDAQ 320
Cdd:PRK09451 240 QAEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDAN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 321 VGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVIED 400
Cdd:PRK09451 320 LGAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428519 401 DAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGWQRPTKK 456
Cdd:PRK09451 400 DVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGWQRPVKK 455
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-457 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 548.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQegLHFALQQPQQGTGH 81
Cdd:PRK14354 3 RYAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDR--SEFALQEEQLGTGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLlegDGKDDVTLVLYGDVPLVQPDTLRRLLA---ARGDGAAVLTEVLDDSTGYGRIVRDAAGQVCRIVEHKD 158
Cdd:PRK14354 81 AVMQAEEFL---ADKEGTTLVICGDTPLITAETLKNLIDfheEHKAAATILTAIAENPTGYGRIIRNENGEVEKIVEQKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 159 ASEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELER 238
Cdd:PRK14354 158 ATEEEKQIKEINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGEKVGAYQTEDFEESLGVNDRVALAEAEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 239 RWQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEaYSHLQD 318
Cdd:PRK14354 238 VMRRRINEKHMVNGVTIIDPESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVDSTIGDGVTIT-NSVIEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 319 AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVI 398
Cdd:PRK14354 317 SKVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVNYDGKNKFKTII 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1337428519 399 EDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGW--QRPTKKS 457
Cdd:PRK14354 397 GDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKEGYvkKLPHKKK 457
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-450 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 523.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEGLH-FALQQPQQGTGHAV 83
Cdd:PRK14353 9 IILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAeIFVQKERLGTAHAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 84 QQAVPLLleGDGKDDVtLVLYGDVPLVQPDTLRRLLAARGDGAAVLteVL----DDSTGYGRIVRDAaGQVCRIVEHKDA 159
Cdd:PRK14353 89 LAAREAL--AGGYGDV-LVLYGDTPLITAETLARLRERLADGADVV--VLgfraADPTGYGRLIVKG-GRLVAIVEEKDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 160 SEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQpAASWETLGVNSRVQQAELERR 239
Cdd:PRK14353 163 SDEERAITLCNSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIARAEGLRVAVVE-APEDEVRGINSRAELAEAEAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 240 WQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFegevtladgvrvGPhcvlrDVSVGAGTQIEAYSHLQDA 319
Cdd:PRK14353 242 WQARRRRAAMLAGVTLIAPETVFFSYDTVIGRDVVIEPNVVF------------GP-----GVTVASGAVIHAFSHLEGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 320 QVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVIE 399
Cdd:PRK14353 305 HVGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGAGANIGAGTITCNYDGFNKHRTEIG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1337428519 400 DDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGW 450
Cdd:PRK14353 385 AGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKPGW 435
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-450 |
5.41e-166 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 476.35 E-value: 5.41e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQ-EGLHFALQQPQQGTGHA 82
Cdd:PRK14352 7 VIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELaPEVDIAVQDEQPGTGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 83 VQQAVPLLleGDGKDDVTLVLYGDVPLVQPDTLRRLLA---ARGDGAAVLTEVLDDSTGYGRIVRDAAGQVCRIVEHKDA 159
Cdd:PRK14352 87 VQCALEAL--PADFDGTVVVTAGDVPLLDGETLADLVAthtAEGNAVTVLTTTLDDPTGYGRILRDQDGEVTAIVEQKDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 160 SEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELERR 239
Cdd:PRK14352 165 TPSQRAIREVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAIAREAGHRVGAHHADDSAEVAGVNDRVQLAALGAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 240 WQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAySHLQDA 319
Cdd:PRK14352 245 LNRRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVR-THGSES 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 320 QVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVIE 399
Cdd:PRK14352 324 EIGAGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVNKHRTTIG 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1337428519 400 DDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGW 450
Cdd:PRK14352 404 SHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSEGPQRNIEGW 454
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-450 |
6.14e-165 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 472.69 E-value: 6.14e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEGLHFALQQPQQGTGH 81
Cdd:PRK14355 4 LAAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFALQEEQLGTGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLLEGDGKddvTLVLYGDVPLVQPDTLRRLLAA-RGDGAA--VLTEVLDDSTGYGRIVRDAAGQVCRIVEHKD 158
Cdd:PRK14355 84 AVACAAPALDGFSGT---VLILCGDVPLLRAETLQGMLAAhRATGAAvtVLTARLENPFGYGRIVRDADGRVLRIVEEKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 159 ASEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELER 238
Cdd:PRK14355 161 ATPEERSIREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAAEGLRCLAFPVADPDEIMGVNDRAQLAEAAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 239 RWQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQD 318
Cdd:PRK14355 241 VLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 319 AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVI 398
Cdd:PRK14355 321 SVVGDDVAIGPMAHLRPGTELSAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHRTVI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1337428519 399 EDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGW 450
Cdd:PRK14355 401 EDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKEGW 452
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-455 |
7.18e-164 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 469.79 E-value: 7.18e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 1 MLNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEGLHFALQQPQQGTG 80
Cdd:PRK14360 1 MLAVAILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPGLEFVEQQPQLGTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 81 HAVQQAVPLL--LEGDgkddvTLVLYGDVPLVQPDTLRRLLAA-RGDGAAV--LTEVLDDSTGYGRIVRDAAGQVCRIVE 155
Cdd:PRK14360 81 HAVQQLLPVLkgFEGD-----LLVLNGDVPLLRPETLEALLNThRSSNADVtlLTARLPNPKGYGRVFCDGNNLVEQIVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 156 HKDASEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVtdgvPVGAAQPAASWETLGVNSRVQQAE 235
Cdd:PRK14360 156 DRDCTPAQRQNNRINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTVSLLD----PVMAVEVEDYQEINGINDRKQLAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 236 LERRWQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIeAYSH 315
Cdd:PRK14360 232 CEEILQNRIKEKWMLAGVTFIDPASCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIENSQIGENVTV-LYSV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 316 LQDAQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHR 395
Cdd:PRK14360 311 VSDSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDGVKKHR 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 396 TVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGWQRPTK 455
Cdd:PRK14360 391 TVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKENWKKKSS 450
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-444 |
3.99e-156 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 450.33 E-value: 3.99e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGqEGLHFALQQPQQGTGHAVQ 84
Cdd:PRK14356 9 LILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPD-EDARFVLQEQQLGTGHALQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 85 QAVPLLlEGDGKDDVtLVLYGDVPLVQPDTLRRLL-AARGDGAAVLTEVLDDSTGYGRIVRdAAGQVCRIVEHKDASEAE 163
Cdd:PRK14356 88 CAWPSL-TAAGLDRV-LVVNGDTPLVTTDTIDDFLkEAAGADLAFMTLTLPDPGAYGRVVR-RNGHVAAIVEAKDYDEAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 164 R--AIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELERRWQ 241
Cdd:PRK14356 165 HgpETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAVAEGMNVLGVNCGEDPNLLGVNTPAELVRSEELLR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 242 AEQARRQLEAGVTLADParfdlrGTLRCGRDVFIDVG------CVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSH 315
Cdd:PRK14356 245 ARIVEKHLESGVLIHAP------ESVRIGPRATIEPGaeiygpCEIYGASRIARGAVIHSHCWLRDAVVSSGATIHSFSH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 316 LQDAQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHR 395
Cdd:PRK14356 319 LEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNKHR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1337428519 396 TVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQ 444
Cdd:PRK14356 399 TVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQ 447
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-450 |
2.12e-142 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 414.93 E-value: 2.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPaRITVVVGHGADRVKQAFggQEGLHFALQQPQQGTGH 81
Cdd:PRK14357 1 MRALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKKVAQ-KVGVVLGHEAELVKKLL--PEWVKIFLQEEQLGTAH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLlegDGKDDVtLVLYGDVPLVQPDTLRRLLAA---RGDGAAVLTEVLDDSTGYGRIVRDAaGQVcRIVEHKD 158
Cdd:PRK14357 78 AVMCARDFI---EPGDDL-LILYGDVPLISENTLKRLIEEhnrKGADVTILVADLEDPTGYGRIIRDG-GKY-RIVEDKD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 159 ASEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTdgvpVGAAQPAASWETLGVNSRVQQAELER 238
Cdd:PRK14357 152 APEEEKKIKEINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAVNFAEK----VRVVKTEDLLEITGVNTRIQLAWLEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 239 RWQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIeAYSHLQD 318
Cdd:PRK14357 228 QLRMRILEELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKI-IRSECEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 319 AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVI 398
Cdd:PRK14357 307 SVIEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTFI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1337428519 399 EDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGW 450
Cdd:PRK14357 387 EDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGW 438
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
2-452 |
8.47e-139 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 407.06 E-value: 8.47e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGqEGLHFALQQPQQGTGH 81
Cdd:PRK14358 8 LDVVILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQG-SGVAFARQEQQLGTGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLLEGDGkdDVtLVLYGDVPLVQPDTLRRLLA---ARGDGAAVLTEVLDDSTGYGRIVRDAAGQVCRIVEHKD 158
Cdd:PRK14358 87 AFLSGASALTEGDA--DI-LVLYGDTPLLRPDTLRALVAdhrAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 159 ASEAERAIKEVNTGILAApTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQQAELER 238
Cdd:PRK14358 164 ATDAEKAIGEFNSGVYVF-DARAPELARRIGNDNKAGEYYLTDLLGLYRAGGAQVRAFKLSDPDEVLGANDRAGLAQLEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 239 RWQAEQARRQLEAGVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQD 318
Cdd:PRK14358 243 TLRRRINEAHMKAGVTLQDPGTILIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSVLHEGAVIKPHSVLEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 319 AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVI 398
Cdd:PRK14358 323 AEVGAGSDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNKHQSKV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1337428519 399 EDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEGWQR 452
Cdd:PRK14358 403 GAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNLEGWSR 456
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-449 |
1.85e-136 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 398.98 E-value: 1.85e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 1 MLNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPaRITVVVGHGADRVKQA----FggqEGLHFALQQPQ 76
Cdd:PRK14359 2 KLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAISD-DVHVVLHHQKERIKEAvleyF---PGVIFHTQDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 77 Q--GTGHAVQQAVPlllegdgKDDVTLVLYGDVPLVQPDTLRRLLAARGDGA-AVLTevLDDSTGYGRIVRDAaGQVCRI 153
Cdd:PRK14359 78 NypGTGGALMGIEP-------KHERVLILNGDMPLVEKDELEKLLENDADIVmSVFH--LADPKGYGRVVIEN-GQVKKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 154 VEHKDASEAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASwETLGVNSRVQQ 233
Cdd:PRK14359 148 VEQKDANEEELKIKSVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAVFVDEE-NFMGVNSKFEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 234 AELERRWQAEQARRQLEAGVTLADPArfdlrgtlrcgrDVFIDVGCVFEGEVTLADGVRVGPHCVLRDvsvgagTQIEAY 313
Cdd:PRK14359 227 AKAEEIMQERIKKNAMKQGVIMRLPE------------TIYIESGVEFEGECELEEGVRILGKSKIEN------SHIKAH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 314 SHLQDAQVgRDARVGPYARLRPGAELGDrSHVGNFVEIKKSVL-GAdsKANHLAYIGDAEIGARVNVGAGTITCNYDGVN 392
Cdd:PRK14359 289 SVIEESII-ENSDVGPLAHIRPKSEIKN-THIGNFVETKNAKLnGV--KAGHLSYLGDCEIDEGTNIGAGTITCNYDGKK 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1337428519 393 KHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTVEG 449
Cdd:PRK14359 365 KHKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIKN 421
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-232 |
6.13e-120 |
|
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: 349.51 E-value: 6.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGqEGLHFALQQPQQGTGHAV 83
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN-PNVEFVLQEEQLGTGHAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 84 QQAVPLLlegDGKDDVTLVLYGDVPLVQPDTLRRLLAAR---GDGAAVLTEVLDDSTGYGRIVRDAAGQVCRIVEHKDAS 160
Cdd:cd02540 80 KQALPAL---KDFEGDVLVLYGDVPLITPETLQRLLEAHreaGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVEEKDAT 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1337428519 161 EAERAIKEVNTGILAAPTARLKDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQPAASWETLGVNSRVQ 232
Cdd:cd02540 157 EEEKAIREVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVAAVLADDEEEVLGVNDRVQ 228
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
252-444 |
1.22e-117 |
|
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: 342.09 E-value: 1.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 252 GVTLADPARFDLRGTLRCGRDVFIDVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQDAQVGRDARVGPYA 331
Cdd:cd03353 1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 332 RLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCNYDGVNKHRTVIEDDAFIGSDTQLV 411
Cdd:cd03353 81 HLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDNVFIGSNSQLV 160
|
170 180 190
....*....|....*....|....*....|...
gi 1337428519 412 APVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQ 444
Cdd:cd03353 161 APVTIGDGATIAAGSTITKDVPPGALAIARARQ 193
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
5-427 |
1.24e-63 |
|
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: 210.53 E-value: 1.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEGLH----FALQQPQQ 77
Cdd:TIGR03992 4 VILAAGKGTRMRpltETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGvpieYVVQEEQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 78 GTGHAVQQAVPLLlegdgkDDVTLVLYGDVpLVQPDTLRRLLAArgDGAAVLTEVLDDSTGYGRIVRDAaGQVCRIVEHK 157
Cdd:TIGR03992 84 GTADALGSAKEYV------DDEFLVLNGDV-LLDSDLLERLIRA--EAPAIAVVEVDDPSDYGVVETDG-GRVTGIVEKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 158 DASEAERAikevNTGILAAPtARLKDWLSRIDNNnAQGEYYLTDVIGLAVTDGvPVGAAQPAASWETLGvnsrvqqaele 237
Cdd:TIGR03992 154 ENPPSNLI----NAGIYLFS-PEIFELLEKTKLS-PRGEYELTDALQLLIDEG-KVKAVELDGFWLDVG----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 238 RRWQAeqarrqLEAGVTLADPARFDLRGTLrcgrdvfidvgcvfEGEVTLadgvrVGPhcvlrdVSVGAGTQIEAYSHLQ 317
Cdd:TIGR03992 216 RPWDL------LDANEALLDNLEPRIEGTV--------------EENVTI-----KGP------VVIGEGAVIRSGTYIE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 318 D-AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKANHLAYIGDAEIGARVNVGAGTITCN--YD----- 389
Cdd:TIGR03992 265 GpVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFGAGTKVANlrHDdkpvk 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1337428519 390 ----------GVNKHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTT 427
Cdd:TIGR03992 345 vtvkgkrvdtGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEV 392
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
4-226 |
2.57e-32 |
|
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: 122.30 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEG----LHFALQQPQ 76
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKfgvnIEYVVQEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 77 QGTGHAVQQAVPLLlegdgKDDVTLVLYGDVpLVQPDT---LRRLLAARGDGAAVLTEVlDDSTGYGRIVRDAAGQVCRI 153
Cdd:cd04181 81 LGTAGAVRNAEDFL-----GDDDFLVVNGDV-LTDLDLselLRFHREKGADATIAVKEV-EDPSRYGVVELDDDGRVTRF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1337428519 154 VEhKDASEaerAIKEVNTGILAAPtarlKDWLSRIDNNNAQGEYYLTDVIGLAVTDGvPVGAAQPAASWETLG 226
Cdd:cd04181 154 VE-KPTLP---ESNLANAGIYIFE----PEILDYIPEILPRGEDELTDAIPLLIEEG-KVYGYPVDGYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
4-210 |
1.73e-27 |
|
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: 109.86 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEG----LHFALQQPQ 76
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRfgvrITYVDEGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 77 QGTGHAVQQAVPLLlegdgKDDVTLVLYGDVpLVQPDtLRRLLAA----RGDGAAVLTEVlDDSTGYGRIVRDAAGQVCR 152
Cdd:COG1208 82 LGTGGALKRALPLL-----GDEPFLVLNGDI-LTDLD-LAALLAFhrekGADATLALVPV-PDPSRYGVVELDGDGRVTR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1337428519 153 IVEHKDASEAERaikeVNTGILAAPtarlKDWLSRIDNNNAqgeYYLTDVIGLAVTDG 210
Cdd:COG1208 154 FVEKPEEPPSNL----INAGIYVLE----PEIFDYIPEGEP---FDLEDLLPRLIAEG 200
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
284-429 |
4.66e-26 |
|
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: 103.44 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 284 EVTLADGVRVGPHcvlrdVSVGAGTQIEAYSHLQD-AQVGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLGADSKA 362
Cdd:cd05636 5 EGTVEEGVTIKGP-----VWIGEGAIVRSGAYIEGpVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 363 NHLAYIGDAEIGARVNVGAGTITCNY-----------------DGVNKHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAG 425
Cdd:cd05636 80 PHLNYVGDSVLGENVNLGAGTITANLrfddkpvkvrlkgervdTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPG 159
|
....
gi 1337428519 426 TTLT 429
Cdd:cd05636 160 CVVR 163
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
2-121 |
3.91e-20 |
|
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: 87.62 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSdlPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEGLHFALQQPQQGTGH 81
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEGMSS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLLEGdgkDDVTLVLYGDVPLVQPDTLRRLLAA 121
Cdd:cd04182 79 SLAAGLEALPAD---ADAVLILLADQPLVTAETLRALIDA 115
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-127 |
6.05e-20 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 87.52 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 1 MLNVVILAAGLGKRMQSdlPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGqEGLHFAL-QQPQQGT 79
Cdd:COG2068 3 KVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG-LGVRVVVnPDWEEGM 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1337428519 80 GHAVQQAVPLLLEGdgkDDVTLVLYGDVPLVQPDTLRRLLAARGDGAA 127
Cdd:COG2068 80 SSSLRAGLAALPAD---ADAVLVLLGDQPLVTAETLRRLLAAFRESPA 124
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
4-215 |
1.98e-18 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 84.14 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGG-QEGLHFAL-QQPQQ- 77
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARpGPDVTFVYnPDYDEt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 78 GTGHAVQQAVPLLLEGdgkddvTLVLYGDVpLVQPDTLRRLLAARGDGAAVL----TEVLDDSTgygRIVRDAAGQVCRI 153
Cdd:COG1213 82 NNIYSLWLAREALDED------FLLLNGDV-VFDPAILKRLLASDGDIVLLVdrkwEKPLDEEV---KVRVDEDGRIVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428519 154 VEHKDASEAE-RAIkevntGIL---AAPTARLKDWLSRIDNNNAQGEYYlTDVIGLAVTDGVPVGA 215
Cdd:COG1213 152 GKKLPPEEADgEYI-----GIFkfsAEGAAALREALEALIDEGGPNLYY-EDALQELIDEGGPVKA 211
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-214 |
4.94e-17 |
|
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: 79.90 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQS---DLPKVLHTLAGKPMLAHVLasaRELAPA---RITVVVGHGADRVKQAFG----GQEGLHFALQ 73
Cdd:cd06915 1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYLL---EYLARQgisRIVLSVGYLAEQIEEYFGdgyrGGIRIYYVIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 74 QPQQGTGHAVQQAVPLLLegdgkDDVTLVLYGD--VPLVQPDTLRRLLAARGDGAAVLTEVlDDSTGYGRIVRDAAGQVC 151
Cdd:cd06915 78 PEPLGTGGAIKNALPKLP-----EDQFLVLNGDtyFDVDLLALLAALRASGADATMALRRV-PDASRYGNVTVDGDGRVI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1337428519 152 RIVEhKDASEAERAIkevNTGILAAPtarlKDWLSRIDNNNAQGEyylTDVIGLAVTDGVPVG 214
Cdd:cd06915 152 AFVE-KGPGAAPGLI---NGGVYLLR----KEILAEIPADAFSLE---ADVLPALVKRGRLYG 203
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
4-130 |
1.85e-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: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDlpKVLHTLAGKPMLAHVLASARElAPARITVVVGHgaDRVKQAFGGQeGLHFAL-QQPQQGTGHA 82
Cdd:pfam12804 1 AVILAGGRSSRMGGD--KALLPLGGKPLLERVLERLRP-AGDEVVVVAND--EEVLAALAGL-GVPVVPdPDPGQGPLAG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1337428519 83 VQQAvpllLEGDGKDDVTLVLYGDVPLVQPDTLRRLLAAR---GDGAAVLT 130
Cdd:pfam12804 75 LLAA----LRAAPGADAVLVLACDMPFLTPELLRRLLAAAeesGADIVVPV 121
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-198 |
2.56e-15 |
|
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: 74.96 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQS---DLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEGLHFALQQ--PQQG 78
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFVYNPdyAETN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 79 TGHAVQQAVPLLlegdgKDDvTLVLYGDVpLVQPDTLRRLLAARGDGAAVLTEVLDdsTGYGRIVRDAAGQVCRIVEHKD 158
Cdd:cd02523 81 NIYSLYLARDFL-----DED-FLLLEGDV-VFDPSILERLLSSPADNAILVDKKTK--EWEDEYVKDLDDAGVLLGIISK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1337428519 159 ASEAERAIKEVnTGIL---AAPTARLKDWLSRIDNNNAQGEYY 198
Cdd:cd02523 152 AKNLEEIQGEY-VGISkfsPEDADRLAEALEELIEAGRVNLYY 193
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-203 |
7.60e-15 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 74.74 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRM----QSdLPKVLHTLAGKPMLAHVLASAReLAPAR-ITVVVG-HGADRVKQAF--GGQEG--LHFALQQ 74
Cdd:COG1209 4 IILAGGSGTRLrpltLT-VSKQLLPVYDKPMIYYPLSTLM-LAGIReILIISTpEDGPQFERLLgdGSQLGikISYAVQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 75 PQQGTGHAVQQAVPLLlegdGKDDVTLVLyGDVpLVQPDTLRRLL---AARGDGAAV-LTEVlDDSTGYGRIVRDAAGQV 150
Cdd:COG1209 82 EPLGLAHAFIIAEDFI----GGDPVALVL-GDN-IFYGDGLSELLreaAARESGATIfGYKV-EDPERYGVVEFDEDGRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1337428519 151 CRIVEHKDASEAERAIkevnTGI--LaapTARLKDWLSRIDnNNAQGEYYLTDVI 203
Cdd:COG1209 155 VSLEEKPKEPKSNLAV----TGLyfY---DNDVVEIAKNLK-PSARGELEITDAN 201
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-160 |
3.89e-14 |
|
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: 71.45 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 6 ILAAGLGKRMQS---DLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQE---GLHFALQQPQ-QG 78
Cdd:cd06422 4 ILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRfglRITISDEPDElLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 79 TGHAVQQAVPLLlegdgKDDVTLVLYGDV----PLvqPDTLRRLLAARGDG-AAVLTEVLDDSTGYGRIVRDAAGQVCRI 153
Cdd:cd06422 84 TGGGIKKALPLL-----GDEPFLVVNGDIlwdgDL--APLLLLHAWRMDALlLLLPLVRNPGHNGVGDFSLDADGRLRRG 156
|
....*..
gi 1337428519 154 VEHKDAS 160
Cdd:cd06422 157 GGGAVAP 163
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-216 |
1.47e-13 |
|
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: 69.91 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRMQS---DLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEG----LHFALQQPQQ 77
Cdd:cd04189 4 LILAGGKGTRLRPltyTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRfgvrITYILQEEPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 78 GTGHAVQQAVPLLlegdgKDDVTLVLYGDVPLVQPDT--LRRLLAARGDGAAVLTEVlDDSTGYGRIVRDaAGQVCRIVE 155
Cdd:cd04189 84 GLAHAVLAARDFL-----GDEPFVVYLGDNLIQEGISplVRDFLEEDADASILLAEV-EDPRRFGVAVVD-DGRIVRLVE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1337428519 156 -----------------HKDASEAERAIKevntgilaaPTARlkdwlsridnnnaqGEYYLTDVIGLAVTDGVPVGAA 216
Cdd:cd04189 157 kpkeppsnlalvgvyafTPAIFDAISRLK---------PSWR--------------GELEITDAIQWLIDRGRRVGYS 211
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
318-435 |
8.54e-13 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 65.28 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 318 DAQVGRDARVGPYARLRPG-AELGDRSHVGNFVeikksvlgadskanHLAYIGDAEIGARVNVGAGTITCNY-------- 388
Cdd:COG0110 8 GARIGDGVVIGPGVRIYGGnITIGDNVYIGPGV--------------TIDDPGGITIGDNVLIGPGVTILTGnhpiddpa 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1337428519 389 -DGVNKHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAG 435
Cdd:COG0110 74 tFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPY 121
|
|
| LbH_THP_succinylT |
cd03350 |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
325-447 |
2.34e-11 |
|
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.
Pssm-ID: 100041 [Multi-domain] Cd Length: 139 Bit Score: 61.24 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 325 ARVGPYARLRPGAELGDRSHV--GNFVEIKkSVLGADSKANHLAYIGD-AEIGARVNVGAGT-ITCNYDGVNKHRTVIED 400
Cdd:cd03350 2 RRVPPGAIIRDGAFIGPGAVLmmPSYVNIG-AYVDEGTMVDSWATVGScAQIGKNVHLSAGAvIGGVLEPLQATPVIIED 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1337428519 401 DAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLTV 447
Cdd:cd03350 81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRV 127
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
285-436 |
5.41e-11 |
|
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: 61.66 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 285 VTLADGVRVGPHCVLR-DVSVGAGTQIEAYSHlqdaqVGRDARVGPYARLRPGAELGDRSHVGNFVEIKK-SVLGAD--- 359
Cdd:cd03352 2 AKIGENVSIGPNAVIGeGVVIGDGVVIGPGVV-----IGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSgAVIGSDgfg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 360 ---SKANHLAY--IGDAEIGARVNVGAGTI--------TCNYDGV--------------NKH-----------RTVIEDD 401
Cdd:cd03352 77 fapDGGGWVKIpqLGGVIIGDDVEIGANTTidrgalgdTVIGDGTkidnlvqiahnvriGENcliaaqvgiagSTTIGDN 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1337428519 402 AFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGK 436
Cdd:cd03352 157 VIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGE 191
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
5-129 |
5.92e-11 |
|
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: 62.07 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGAD---------------RVKQAFGGQE--- 66
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDieyfeellakygidkPVRVVAGGATrqd 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 67 ----GLhfalqqpqqgtghavqQAVPlllegdgkDDVTLVLYGDV--PLVQPDTLRRLL-AARGDGAAVL 129
Cdd:COG1211 81 svrnGL----------------EALP--------DDDDWVLVHDAarPLVSPELIDRVIeAAREYGAAIP 126
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
2-129 |
1.45e-10 |
|
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: 60.21 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDlpKVLHTLAGKPMLAHVLASARELAPAriTVVVGHGADRVKQAfggqeGLHFAL-QQPQQG-- 78
Cdd:COG0746 5 ITGVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLRPQVDE--VVIVANRPERYAAL-----GVPVVPdDPPGAGpl 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1337428519 79 TG-HAVQQAVPlllegdgkDDVTLVLYGDVPLVQPDTLRRLLAARGDGAAVL 129
Cdd:COG0746 76 AGiLAALEAAP--------AEWVLVLACDMPFLPPDLVRRLLEALEEGADAV 119
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
275-433 |
1.92e-10 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 61.19 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 275 IDVGCVFEGEVTLADGVRVGPHCVL-RDVSVGAGTQIEAYSHLQD-AQVGRDARVGPYARLrpGAE-------------- 338
Cdd:PRK12461 2 IHPTAVIDPSAKLGSGVEIGPFAVIgANVEIGDGTWIGPHAVILGpTRIGKNNKIHQGAVV--GDEpqdftykgeesrle 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 339 LGDRSHVGNFVEIKK-------SVLGADS--KAN-HLAYigDAEIGARVNVGAGTITCNYdgvnkhrTVIEDDAFIGSDT 408
Cdd:PRK12461 80 IGDRNVIREGVTIHRgtkgggvTRIGNDNllMAYsHVAH--DCQIGNNVILVNGALLAGH-------VTVGDRAIISGNC 150
|
170 180
....*....|....*....|....*
gi 1337428519 409 QLVAPVRVGQGATLGAGTTLTRDAP 433
Cdd:PRK12461 151 LVHQFCRIGALAMMAGGSRISKDVP 175
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
339-439 |
2.13e-10 |
|
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: 57.90 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 339 LGDRSHVGNFVEIKKSV-LGADSKANHLAYIGD-AEIGARVNVGAGTITCN--------YDGVNKHRTVIEDDAFIGSDT 408
Cdd:cd03358 1 IGDNCIIGTNVFIENDVkIGDNVKIQSNVSIYEgVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANA 80
|
90 100 110
....*....|....*....|....*....|.
gi 1337428519 409 QLVAPVRVGQGATLGAGTTLTRDAPAGKLTV 439
Cdd:cd03358 81 TILPGVTIGEYALVGAGAVVTKDVPPYALVV 111
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-129 |
2.16e-10 |
|
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: 60.23 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGAD--------------RVKQAFGGQEGlh 69
Cdd:cd02516 3 AIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDidlakelakyglskVVKIVEGGATR-- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1337428519 70 falqqpQQGTGHAVqQAVPlllegdgKDDVTLVLYGDV--PLVQPDTLRRLL-AARGDGAAVL 129
Cdd:cd02516 81 ------QDSVLNGL-KALP-------DADPDIVLIHDAarPFVSPELIDRLIdALKEYGAAIP 129
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-129 |
2.19e-10 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 60.53 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 1 MLNVVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASArELAPA--RItVVVGHGAD-------------RVKQAFGGQ 65
Cdd:PRK00155 3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAF-LAHPRidEI-IVVVPPDDrpdfaelllakdpKVTVVAGGA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1337428519 66 E-------GLhfalqqpqqgtghavqQAVPlllegdgKDDVTLVLYGDVPLVQPDTLRRLL-AARGDGAAVL 129
Cdd:PRK00155 81 ErqdsvlnGL----------------QALP-------DDDWVLVHDAARPFLTPDDIDRLIeAAEETGAAIL 129
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
4-129 |
7.03e-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: 58.84 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADrvkQAFGGQEGLHFALQQPQQGtGHAV 83
Cdd:TIGR00453 2 AVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDD---TEFFQKYLVARAVPKIVAG-GDTR 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1337428519 84 QQAVPLLLEgdGKDDVTLVLYGDV--PLVQPDTLRRLL-AARGDGAAVL 129
Cdd:TIGR00453 78 QDSVRNGLK--ALKDAEFVLVHDAarPFVPKELLDRLLeALRKAGAAIL 124
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
321-437 |
7.37e-10 |
|
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: 58.27 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 321 VGRDARVGPYARLRPGAELGDRSHVGNFVEIKKSVLgadskANHLAYIG-DAEIGARVNVGAGTITCNYdgvnkhrTVIE 399
Cdd:TIGR03570 90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVI-----INTGAIVEhDCVIGDFVHIAPGVTLSGG-------VVIG 157
|
90 100 110
....*....|....*....|....*....|....*...
gi 1337428519 400 DDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKL 437
Cdd:TIGR03570 158 EGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGV 195
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-226 |
1.14e-09 |
|
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: 58.42 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRM---QSDLPKVLHTLAGK-PMLAHVLASARELAPARITVVVG----HGADRVKQA---FGGQEGlhFALQ 73
Cdd:pfam00483 3 IILAGGSGTRLwplTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqehrFMLNELLGDgskFGVQIT--YALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 74 QPQQGTGHAVQQAVPLLleGDGKDDVtLVLYGDVplVQPDTLRRLLA-ARGDGAAVLTEVL----DDSTGYGRIVRDAAG 148
Cdd:pfam00483 81 PEGKGTAPAVALAADFL--GDEKSDV-LVLGGDH--IYRMDLEQAVKfHIEKAADATVTFGivpvEPPTGYGVVEFDDNG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337428519 149 QVCRIVEhKdaSEAERAIKEVNTGILAAPTARLkDWLSRIDNNNAQGEYYLTDVIGLAVTDGVPVGAAQ-PAASWETLG 226
Cdd:pfam00483 156 RVIRFVE-K--PKLPKASNYASMGIYIFNSGVL-DFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIfKGYAWLDVG 230
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
324-435 |
1.51e-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: 57.49 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 324 DARVGPYARLRPGAELGDRSHVGNFVEIKKSVLgadskANHLAYIG-DAEIGARVNVGAGTITCnydGvnkhRTVIEDDA 402
Cdd:cd03360 90 SAVVSPSAVIGEGCVIMAGAVINPDARIGDNVI-----INTGAVIGhDCVIGDFVHIAPGVVLS---G----GVTIGEGA 157
|
90 100 110
....*....|....*....|....*....|...
gi 1337428519 403 FIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAG 435
Cdd:cd03360 158 FIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDG 190
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
2-128 |
1.61e-09 |
|
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: 57.20 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDlpKVLHTLAGKPMLAHVLASARELApARITVVVGHgadrvKQAFGGQEGLHFAL-QQPQQG-- 78
Cdd:cd02503 1 ITGVILAGGKSRRMGGD--KALLELGGKPLLEHVLERLKPLV-DEVVISANR-----DQERYALLGVPVIPdEPPGKGpl 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1337428519 79 TG-HAVQQAVPlllegdgkDDVTLVLYGDVPLVQPDTLRRLLAARGDGAAV 128
Cdd:cd02503 73 AGiLAALRAAP--------ADWVLVLACDMPFLPPELLERLLAAAEEGADA 115
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
354-429 |
1.79e-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: 54.18 E-value: 1.79e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1337428519 354 SVLGADSKANHLAYIGD-AEIGARVNVGAGTITCNYDGVNKHR-TVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLT 429
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGPNEKNpTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
285-436 |
2.51e-09 |
|
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: 58.49 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 285 VTLADGVRVGPHCVL-RDVSVGAGTQIEAYSHlqdaqVGRDARVGPYARLRPGAELGDRSHVGNFVEIK-KSVLGAD--- 359
Cdd:COG1044 109 AKIGEGVSIGPFAVIgAGVVIGDGVVIGPGVV-----IGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHsGAVIGADgfg 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 360 ----SKANHL--AYIGDAEIGARVNVGA------GTITcnydgvnkhRTVIEDDA------------FIGSDTQLVAPV- 414
Cdd:COG1044 184 fapdEDGGWVkiPQLGRVVIGDDVEIGAnttidrGALG---------DTVIGDGTkidnlvqiahnvRIGEHTAIAAQVg 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1337428519 415 -----------------------RVGQGATLGAGTTLTRDAPAGK 436
Cdd:COG1044 255 iagstkigdnvviggqvgiaghlTIGDGVIIGAQSGVTKSIPEGG 299
|
|
| DapD |
COG2171 |
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ... |
326-430 |
1.13e-08 |
|
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441774 [Multi-domain] Cd Length: 268 Bit Score: 55.89 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 326 RVGPYARLRPGAELGDRS-HVGNFVEIkksvlGAdskanhlaYIGD-------------AEIGARVNVGAGT-ITCNYDG 390
Cdd:COG2171 99 RIVPGARVRLGAYLAPGVvLMPSFVNI-----GA--------YVDEgtmvdtwatvgscAQIGKNVHLSGGAgIGGVLEP 165
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1337428519 391 VNKHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTR 430
Cdd:COG2171 166 LQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTA 205
|
|
| LbH_XAT |
cd03349 |
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
338-434 |
9.59e-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: 51.01 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 338 ELGDRSHVGNFVEI---KKSVLGADSKANHLAYIGDAEIGARVNVGAGTItcnyDGVNKHRTVIEDDAFIGSDTQLVAPV 414
Cdd:cd03349 17 VGGDKLSIGKFCSIapgVKIGLGGNHPTDWVSTYPFYIFGGEWEDDAKFD----DWPSKGDVIIGNDVWIGHGATILPGV 92
|
90 100
....*....|....*....|
gi 1337428519 415 RVGQGATLGAGTTLTRDAPA 434
Cdd:cd03349 93 TIGDGAVIAAGAVVTKDVPP 112
|
|
| LpxA |
COG1043 |
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
287-433 |
4.24e-07 |
|
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: 51.17 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 287 LADGVRVGPHCVL-RDVSVGAGTQIEAYSHLQD-AQVGRDARVGPYARL------------RPGAELGDRSHVGNFVEIK 352
Cdd:COG1043 16 LGENVEIGPFCVIgPDVEIGDGTVIGSHVVIEGpTTIGKNNRIFPFASIgeepqdlkykgePTRLEIGDNNTIREFVTIH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 353 KSVLGADSK---ANH---LAY--IG-DAEIGARV----NVG-AGtitcnydgvnkHrTVIEDDAFIGSdtqLVAP---VR 415
Cdd:COG1043 96 RGTVQGGGVtriGDDnllMAYvhVAhDCVVGNNVilanNATlAG-----------H-VEVGDHAIIGG---LSAVhqfVR 160
|
170
....*....|....*...
gi 1337428519 416 VGQGATLGAGTTLTRDAP 433
Cdd:COG1043 161 IGAHAMVGGGSGVVKDVP 178
|
|
| LbH_unknown |
cd05635 |
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
295-387 |
5.85e-07 |
|
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain] Cd Length: 101 Bit Score: 47.66 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 295 PHCVL--RD--VSVGAGTQIEAYSHLQ-DAQVGRDARVGPYARLRPGAELGDRSHVGNfvEIKKSVLGADSKANHLAYIG 369
Cdd:cd05635 1 PGAVLdaEDgpIYIGKDAVIEPFAVIEgPVYIGPGSRVKMGARIYGNTTIGPTCKIGG--EVEDSIIEGYSNKQHDGFLG 78
|
90
....*....|....*...
gi 1337428519 370 DAEIGARVNVGAGTITCN 387
Cdd:cd05635 79 HSYLGSWCNLGAGTNNSD 96
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
282-433 |
6.85e-07 |
|
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: 50.51 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 282 EGEVTLADGVRVGPHCVLR-DVSVGAGTQIEAYSHLQD-AQVGRDARVGPYARL------------RPGAELGDRSHVGN 347
Cdd:cd03351 9 DPGAKIGENVEIGPFCVIGpNVEIGDGTVIGSHVVIDGpTTIGKNNRIFPFASIgeapqdlkykgePTRLEIGDNNTIRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 348 FVEIKKSVLGADSKanhlAYIGD-------AEIGARVNVGAGTITCNYDGVNKHrTVIEDDAFIGSDTQLVAPVRVGQGA 420
Cdd:cd03351 89 FVTIHRGTAQGGGV----TRIGNnnllmayVHVAHDCVIGNNVILANNATLAGH-VEIGDYAIIGGLSAVHQFCRIGRHA 163
|
170
....*....|...
gi 1337428519 421 TLGAGTTLTRDAP 433
Cdd:cd03351 164 MVGGGSGVVQDVP 176
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
338-435 |
8.04e-07 |
|
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: 47.45 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 338 ELGDRSHVGNFVeikksvlgadskanHLAYIGDAEIGARVNVGAGT--ITCNYD----------GVNKHRTVIEDDAFIG 405
Cdd:cd04647 3 SIGDNVYIGPGC--------------VISAGGGITIGDNVLIGPNVtiYDHNHDiddperpieqGVTSAPIVIGDDVWIG 68
|
90 100 110
....*....|....*....|....*....|
gi 1337428519 406 SDTQLVAPVRVGQGATLGAGTTLTRDAPAG 435
Cdd:cd04647 69 ANVVILPGVTIGDGAVVGAGSVVTKDVPPN 98
|
|
| LbH_SAT |
cd03354 |
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
369-439 |
1.21e-06 |
|
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: 46.66 E-value: 1.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1337428519 369 GDAEIGARVNVGAG-TITCNYDGVNKHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTV 439
Cdd:cd03354 27 ETAVIGDNCTIYQGvTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVV 98
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
246-346 |
1.27e-06 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 47.56 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 246 RRQLEAGVTLADPARFDLrGTLRCGRDVFIDVGCVFE--GEVTLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQDAQVGR 323
Cdd:COG0110 8 GARIGDGVVIGPGVRIYG-GNITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIGD 86
|
90 100
....*....|....*....|...
gi 1337428519 324 DARVGPYARLRPGAELGDRSHVG 346
Cdd:COG0110 87 DVWIGAGATILPGVTIGDGAVVG 109
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
4-155 |
1.87e-06 |
|
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: 48.60 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRvkqAFGGQEGLHFALQQPQQGTGHav 83
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDT---PEFRQLLGDPSIQLVAGGDTR-- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428519 84 QQAVPLLLEG-DGKDDVTLVLYGDVPLVQPDTLRRLLAA--RGDGAAVLTEVLDDSTGYGrivrDAAGQVCRIVE 155
Cdd:pfam01128 76 QDSVLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAAleTGTQGAILALPVTDTIKRV----EADGVVAGTPD 146
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
270-437 |
2.38e-06 |
|
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.
Pssm-ID: 100051 [Multi-domain] Cd Length: 153 Bit Score: 47.02 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 270 GRDVFIDVGCVFEGEVTLADGVRVGPHCVLRdvsvGAGTQIeayshlqdaqvgrdarvgpyarlrpgaELGDRSHVGNFv 349
Cdd:cd04645 3 DPSAFIAPNATVIGDVTLGEGSSVWFGAVLR----GDVNPI---------------------------RIGERTNIQDG- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 350 eikkSVLgadskanHLAYIGDAEIGARVNVGAGTITcnydgvnkHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTLT 429
Cdd:cd04645 51 ----SVL-------HVDPGYPTIIGDNVTVGHGAVL--------HGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVP 111
|
170
....*....|
gi 1337428519 430 RDA--PAGKL 437
Cdd:cd04645 112 PGKviPPGSL 121
|
|
| PRK05289 |
PRK05289 |
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
280-433 |
3.79e-06 |
|
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 48.17 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 280 VFEGEVTLADGVRVGPHCVL-RDVSVGAGTQIEAYSHLQ-DAQVGRDARVGPYARLrpGA--------------ELGDRS 343
Cdd:PRK05289 10 IVEPGAKIGENVEIGPFCVIgPNVVIGDGTVIGSHVVIDgHTTIGKNNRIFPFASI--GEdpqdlkykgeptrlVIGDNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 344 --------HVGNFVEIKKSVLGADS--KAN-HLAYigDAEIGARV----NVG-AGtitcnydgvnkHrTVIEDDAFIGSD 407
Cdd:PRK05289 88 tirefvtiNRGTVQGGGVTRIGDNNllMAYvHVAH--DCVVGNHVilanNATlAG-----------H-VEVGDYAIIGGL 153
|
170 180
....*....|....*....|....*....
gi 1337428519 408 T---QLvapVRVGQGATLGAGTTLTRDAP 433
Cdd:PRK05289 154 TavhQF---VRIGAHAMVGGMSGVSQDVP 179
|
|
| dapD |
PRK11830 |
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional |
366-429 |
5.20e-06 |
|
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
Pssm-ID: 236996 [Multi-domain] Cd Length: 272 Bit Score: 47.88 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 366 AYIGD-------------AEIGARVNVGAGT-ItcnyDGV----NKHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGTT 427
Cdd:PRK11830 133 AYVDEgtmvdtwatvgscAQIGKNVHLSGGVgI----GGVleplQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVF 208
|
..
gi 1337428519 428 LT 429
Cdd:PRK11830 209 LG 210
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
285-383 |
9.66e-06 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 47.44 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 285 VTLADGVRVGPHCVL-RDVSVGAGTQIEAYSHL-QDAQVGRDARVGPYARLRPGAELGDRSHV--GnfveikkSVLGAD- 359
Cdd:PRK00892 113 AKIGEGVSIGPNAVIgAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIYHAVRIGNRVIIhsG-------AVIGSDg 185
|
90 100 110
....*....|....*....|....*....|.
gi 1337428519 360 -----SKANH--LAYIGDAEIGARVNVGAGT 383
Cdd:PRK00892 186 fgfanDRGGWvkIPQLGRVIIGDDVEIGANT 216
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
4-129 |
1.73e-05 |
|
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: 46.76 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRV--KQAFGgqeglHFALQQPQQGtGH 81
Cdd:PRK09382 8 LVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAymKKALP-----EIKFVTLVTG-GA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1337428519 82 AVQQAVPLLLEgdgKDDVTLVLYGDV--PLVQPDTLRRLLAARGDGAAVL 129
Cdd:PRK09382 82 TRQESVRNALE---ALDSEYVLIHDAarPFVPKELIDRLIEALDKADCVL 128
|
|
| PRK10502 |
PRK10502 |
putative acyl transferase; Provisional |
325-437 |
2.52e-05 |
|
putative acyl transferase; Provisional
Pssm-ID: 236703 [Multi-domain] Cd Length: 182 Bit Score: 44.94 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 325 ARVGPYARLRPGA--------ELGDRSHVGNFVEIkksvlgaDSkanhlayIGDAEIGARVNVGAGTITC----NYD--- 389
Cdd:PRK10502 52 AKIGKGVVIRPSVritypwklTIGDYAWIGDDVWL-------YN-------LGEITIGAHCVISQKSYLCtgshDYSdph 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1337428519 390 -GVNKHRTVIEDDAFIGSDTqLVAP-VRVGQGATLGAGTTLTRDAPAGKL 437
Cdd:PRK10502 118 fDLNTAPIVIGEGCWLAADV-FVAPgVTIGSGAVVGARSSVFKSLPANTI 166
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
1-135 |
2.99e-05 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 44.79 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 1 MLNVVILAAGLGKRMQ-SDlpKVLHTLAGKPMLAHVLasaRELAP--ARITVVVGHGADRVkQAFGGQE----------- 66
Cdd:PRK00317 3 PITGVILAGGRSRRMGgVD--KGLQELNGKPLIQHVI---ERLAPqvDEIVINANRNLARY-AAFGLPVipdsladfpgp 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1337428519 67 --GLHFALQQPqqGTGHAvqqavplllegdgkddvtLVLYGDVPLVQPDTLRRLLAARGDGAAVLTEVLDD 135
Cdd:PRK00317 77 laGILAGLKQA--RTEWV------------------LVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDG 127
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
318-408 |
4.51e-05 |
|
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: 45.39 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 318 DAQVGRDARVGPYARLRPGAELGDRSHVGNFVEI-KKSVLGADSK--ANhlAYIG-DAEIGARVNVGAGTI--------T 385
Cdd:COG1044 108 SAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIgDGVVIGDDCVlhPN--VTIYeRCVIGDRVIIHSGAVigadgfgfA 185
|
90 100
....*....|....*....|....*...
gi 1337428519 386 CNYDGVNKH-----RTVIEDDAFIGSDT 408
Cdd:COG1044 186 PDEDGGWVKipqlgRVVIGDDVEIGANT 213
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
318-430 |
5.85e-05 |
|
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: 43.94 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 318 DAQVGRDARVGPYARLRPGAELGDRSHVGNFVeikksVLGADSKanhlayIG-DAEIGARVNVGAGTITCNydgvnkhRT 396
Cdd:cd03352 1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGV-----VIGDGVV------IGdDCVIHPNVTIYEGCIIGD-------RV 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1337428519 397 VIEDDAFIGSDTQLVAP-------------VRVGQGATLGAGTTLTR 430
Cdd:cd03352 63 IIHSGAVIGSDGFGFAPdgggwvkipqlggVIIGDDVEIGANTTIDR 109
|
|
| LbH_wcaF_like |
cd05825 |
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
338-435 |
6.55e-05 |
|
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: 41.82 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 338 ELGDRSHVGNFVEIkksvlgadskanhlaY-IGDAEIGARVNVGAGTITCNydGVNKHRT----------VIEDDAFIGS 406
Cdd:cd05825 5 TIGDNSWIGEGVWI---------------YnLAPVTIGSDACISQGAYLCT--GSHDYRSpafplitapiVIGDGAWVAA 67
|
90 100 110
....*....|....*....|....*....|
gi 1337428519 407 DTqLVAP-VRVGQGATLGAGTTLTRDAPAG 435
Cdd:cd05825 68 EA-FVGPgVTIGEGAVVGARSVVVRDLPAW 96
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
272-384 |
1.15e-04 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 42.71 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 272 DVFIDVGCVFEGEVTLADGVRVGPHCVLR-DVS---VGAGTQIeayshlQD-----------AQVGRDARVGPYARLRpG 336
Cdd:COG0663 16 SAFVAPTAVVIGDVTIGEDVSVWPGAVLRgDVGpirIGEGSNI------QDgvvlhvdpgypLTIGDDVTIGHGAILH-G 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1337428519 337 AELGDRShvgnFVEIKKSVLgadskanhlayiGDAEIGARVNVGAGTI 384
Cdd:COG0663 89 CTIGDNV----LIGMGAIVL------------DGAVIGDGSIVGAGAL 120
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
270-346 |
1.82e-04 |
|
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: 42.48 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 270 GRDVFIDVGCVFEGEVTLADGVRVGPHCVLR-DVSVGAGTQIEAYSHLQ-------DAQVGRDARVGPYARLRPGAELGD 341
Cdd:TIGR03570 97 SPSASIGEGTVIMAGAVINPDVRIGDNVIINtGAIVEHDCVIGDFVHIApgvtlsgGVVIGEGVFIGAGATIIQGVTIGA 176
|
....*
gi 1337428519 342 RSHVG 346
Cdd:TIGR03570 177 GAIVG 181
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-120 |
1.83e-04 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 43.03 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 1 MLNVVILAAglgkRMQSD-LP-KVLHTLAGKPMLAHVLASARElAPARITVVVGHGADRVKQA---FGGQeglhfAL--- 72
Cdd:PRK13368 1 MKVVVVIPA----RYGSSrLPgKPLLDILGKPMIQHVYERAAQ-AAGVEEVYVATDDQRIEDAveaFGGK-----VVmts 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1337428519 73 QQPQQGTGHAVQQAVPLllegdgKDDVTLVLYGDVPLVQPDTLRRLLA 120
Cdd:PRK13368 71 DDHLSGTDRLAEVMLKI------EADIYINVQGDEPMIRPRDIDTLIQ 112
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
267-346 |
2.45e-04 |
|
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: 40.52 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 267 LRCGRDVFIDVGCVF--EGEVTLADGVRVGPHCVLRDVSVG---AGTQIEAYSHLQDAQVGRDARVGPYARLRPGAELGD 341
Cdd:cd04647 2 ISIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDHNHDiddPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81
|
....*
gi 1337428519 342 RSHVG 346
Cdd:cd04647 82 GAVVG 86
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-63 |
3.12e-04 |
|
NTP_trnasferase_like_2 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: 133048 [Multi-domain] Cd Length: 220 Bit Score: 42.11 E-value: 3.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1337428519 4 VVILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFG 63
Cdd:cd06426 1 VVIMAGGKGTRLRpltENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFG 63
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
270-327 |
3.96e-04 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 42.51 E-value: 3.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428519 270 GRDVFIDVGCVFEGEVtLADGVRVGPHCVLR------DVSVGAGTQIeAYSHLQDAQ-----------VGRDARV 327
Cdd:PRK00844 335 SPNVVVESGAEVEDSV-LMDGVRIGRGAVVRraildkNVVVPPGATI-GVDLEEDRRrftvseggivvVPKGQRV 407
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
4-51 |
4.80e-04 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 41.64 E-value: 4.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1337428519 4 VVILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASARELAPARITVVV 51
Cdd:PLN02728 27 VILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVV 74
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
366-428 |
6.94e-04 |
|
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: 41.54 E-value: 6.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337428519 366 AYIG-DAEIGARVNVGAGTitcnydgvnkhrtVIEDDAFIGSDTQLVAPVRVGQGATLGAGTTL 428
Cdd:COG1044 103 AVIDpSAKIGEGVSIGPFA-------------VIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVL 153
|
|
| PLN02296 |
PLN02296 |
carbonate dehydratase |
271-437 |
8.18e-04 |
|
carbonate dehydratase
Pssm-ID: 215167 [Multi-domain] Cd Length: 269 Bit Score: 41.26 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 271 RDVFIDVGCVFEGEVTLADGVRVGPHCVLR----DVSVGAGTQIeayshlQDAQVgrdarvgpyarlrpgaelgdrshvg 346
Cdd:PLN02296 57 KDAFVAPSASVIGDVQVGRGSSIWYGCVLRgdvnSISVGSGTNI------QDNSL------------------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 347 nfVEIKKSVLGAdskaNHLAYIgdaeIGARVNVGAGTITcnydgvnkHRTVIEDDAFIGSDTQLVAPVRVGQGATLGAGT 426
Cdd:PLN02296 106 --VHVAKTNLSG----KVLPTI----IGDNVTIGHSAVL--------HGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGA 167
|
170
....*....|...
gi 1337428519 427 TLTRDA--PAGKL 437
Cdd:PLN02296 168 LVRQNTriPSGEV 180
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
318-407 |
8.77e-04 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 41.28 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 318 DAQVGRDARVGPYARLRPGAELGDRSHVGnfveikksvlgadskANhlAYIGD-AEIGARVNVGAG-TITcnydgvnkHR 395
Cdd:PRK00892 112 SAKIGEGVSIGPNAVIGAGVVIGDGVVIG---------------AG--AVIGDgVKIGADCRLHANvTIY--------HA 166
|
90
....*....|....*...
gi 1337428519 396 TVIEDD------AFIGSD 407
Cdd:PRK00892 167 VRIGNRviihsgAVIGSD 184
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
4-61 |
9.65e-04 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. 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 epsilon shares sequence similarity with gamma 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: 133001 [Multi-domain] Cd Length: 216 Bit Score: 40.31 E-value: 9.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337428519 4 VVILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHVLASareLAPARIT---VVVGHGADRVKQA 61
Cdd:cd02507 3 AVVLADGFGSRFLpltSDIPKALLPVANVPLIDYTLEW---LEKAGVEevfVVCCEHSQAIIEH 63
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
258-339 |
1.68e-03 |
|
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.
Pssm-ID: 100056 [Multi-domain] Cd Length: 104 Bit Score: 37.83 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 258 PARFDLRGTLRcgrDVFIDVGCVFE-GEVT---LADGVRVGPHCVLRDVSVGAGTQIEAYSHLQDAQVGRDARVGPYARL 333
Cdd:cd04651 1 PPYIGRRGEVK---NSLVSEGCIISgGTVEnsvLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVI 77
|
....*.
gi 1337428519 334 RPGAEL 339
Cdd:cd04651 78 GGDPEE 83
|
|
| PRK02726 |
PRK02726 |
molybdenum cofactor guanylyltransferase; |
2-121 |
2.32e-03 |
|
molybdenum cofactor guanylyltransferase;
Pssm-ID: 235063 Cd Length: 200 Bit Score: 39.25 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 2 LNVVILAAGLGKRMQSDlpKVLHTLAGKPMLAHVLASARELAPAriTVVVGHGADRVKQAFggQEGLHFaLQQPQQGTGH 81
Cdd:PRK02726 8 LVALILAGGKSSRMGQD--KALLPWQGVPLLQRVARIAAACADE--VYIITPWPERYQSLL--PPGCHW-LREPPPSQGP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1337428519 82 --AVQQAVPLLlegdgKDDVTLVLYGDVPLVQPDTLRRLLAA 121
Cdd:PRK02726 81 lvAFAQGLPQI-----KTEWVLLLACDLPRLTVDVLQEWLQQ 117
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
5-132 |
2.87e-03 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 39.08 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 5 VILAAGLGKRMQSDLPKVLHTLAGKPMLAHVLASAreLAPARIT-VVVGHGADRVKQAFGGQEGLHFALQQPQ-QGTGHA 82
Cdd:PRK13385 6 IFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPF--LADNRCSkIIIVTQAQERKHVQDLMKQLNVADQRVEvVKGGTE 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1337428519 83 VQQAVPLLLEGDGKDDVTLVLYGDVPLVQPDTLRRLLAARGDGAAVLTEV 132
Cdd:PRK13385 84 RQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAV 133
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
7-130 |
3.24e-03 |
|
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: 38.72 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 7 LAAGLGKRMQSDLpKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKqAFGGQEGLHFaLQQPqqGTG--HAVQ 84
Cdd:COG2266 1 MAGGKGTRLGGGE-KPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTR-EYLKERGVEV-IETP--GEGyvEDLN 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1337428519 85 QAVPLLlegdgkDDVTLVLYGDVPLVQPDTLRRLL-AARGDGAAVLT 130
Cdd:COG2266 76 EALESI------SGPVLVVPADLPLLTPEIIDDIIdAYLESGKPSLT 116
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
4-35 |
4.67e-03 |
|
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.
Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 38.71 E-value: 4.67e-03
10 20 30
....*....|....*....|....*....|....*
gi 1337428519 4 VVILAAGLGKRMQ---SDLPKVLHTLAGKPMLAHV 35
Cdd:cd02524 1 VVILAGGLGTRLSeetELKPKPMVEIGGRPILWHI 35
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
4-130 |
4.74e-03 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 38.39 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRMQS---DLPKVLHTLAGKPMLAHVLASARELAPARITVVVghGADRVKQAFGGQE---GLHFA----LQ 73
Cdd:cd04183 1 IIIPMAGLGSRFKKagyTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLDESlklLAPNAtvveLD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1337428519 74 QPQQGTGHAVQQAVPLLlegdGKDDVTLVLYGDVpLVQPDTLRRLLAA--RGDGAAVLT 130
Cdd:cd04183 79 GETLGAACTVLLAADLI----DNDDPLLIFNCDQ-IVESDLLAFLAAFreRDLDGGVLT 132
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
277-329 |
4.82e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.02 E-value: 4.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1337428519 277 VGCVfegevtLADGVRVGPHCVLRDVSVGAGTQIEAYSHLQDAQVGRDARVGP 329
Cdd:cd04652 32 TNCV------IMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEA 78
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
318-347 |
5.33e-03 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 34.23 E-value: 5.33e-03
10 20 30
....*....|....*....|....*....|
gi 1337428519 318 DAQVGRDARVGPYARLRPGAELGDRSHVGN 347
Cdd:pfam00132 1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
|
|
| F420_cofC |
TIGR03552 |
2-phospho-L-lactate guanylyltransferase; Members of this protein family are the CofC enzyme of ... |
31-129 |
5.80e-03 |
|
2-phospho-L-lactate guanylyltransferase; Members of this protein family are the CofC enzyme of coenzyme F420 biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274643 [Multi-domain] Cd Length: 195 Bit Score: 38.04 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 31 MLAHVLASARELAPARITVVVghgADRVKQAFGGQEGLHfALQQPQQGTGHAVQQAvplLLEGDGKDDVTLVLYGDVPLV 110
Cdd:TIGR03552 32 MLRDVITALRGAGAGAVLVVS---PDPALLEAARNLGAP-VLRDPGPGLNNALNAA---LAEAREPGGAVLILMADLPLL 104
|
90
....*....|....*....
gi 1337428519 111 QPDTLRRLLAARGDGAAVL 129
Cdd:TIGR03552 105 TPRELKRLLAAATEGDVVI 123
|
|
| PLN02694 |
PLN02694 |
serine O-acetyltransferase |
398-455 |
5.99e-03 |
|
serine O-acetyltransferase
Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 38.47 E-value: 5.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1337428519 398 IEDDAFIGSDTQLVAPVRVGQGATLGAGTTLTRDAPAGKLTVSRAKQLtVEGWQRPTK 455
Cdd:PLN02694 215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARL-VGGKEKPAK 271
|
|
| NRPS_term_dom |
TIGR02353 |
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
268-346 |
6.74e-03 |
|
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.
Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 38.96 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 268 RCGRDVFI-DVGCVFEGEVTLADGVRVGPHCVLRDVSVGAGtqieaYSHLQDAQVGRDARVGPYARLRPGAELGDRSHVG 346
Cdd:TIGR02353 114 KIGKGVDIgSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERG-----RLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLG 188
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
4-188 |
7.77e-03 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 37.94 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 4 VVILAAGLGKRM----QSDLPKVLHTLAG-KPMLAHVLASARELAP-ARITVVVGH-GADRVK-QAFGGQEGLHFALQQP 75
Cdd:cd02509 3 PVILAGGSGTRLwplsRESYPKQFLKLFGdKSLLQQTLDRLKGLVPpDRILVVTNEeYRFLVReQLPEGLPEENIILEPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 76 QQGTGHAVQQAVpLLLEGDGKDDVTLVLYGDvPLVQP-----DTLRRLLAARGDGAAVLTEVLDD--STGYGRI-----V 143
Cdd:cd02509 83 GRNTAPAIALAA-LYLAKRDPDAVLLVLPSD-HLIEDveaflKAVKKAVEAAEEGYLVTFGIKPTrpETGYGYIeagekL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1337428519 144 RDAAGQVCRIVEHKDASEAERAIKEV----NTGILAaptARLKDWLSRI 188
Cdd:cd02509 161 GGGVYRVKRFVEKPDLETAKEYLESGnylwNSGIFL---FRAKTFLEEL 206
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
270-351 |
8.59e-03 |
|
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: 35.30 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428519 270 GRDVFIDVGCVFEGEVTLADGVRVGPHCVLrdvsvGAGTQIEaysHLQDAQVGRDARVGPYARLRPGAELGDRSHVGNFV 349
Cdd:cd00208 4 GEGVKIHPKAVIRGPVVIGDNVNIGPGAVI-----GAATGPN---EKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGA 75
|
..
gi 1337428519 350 EI 351
Cdd:cd00208 76 VV 77
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
2-155 |
8.65e-03 |
|
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: 37.58 E-value: 8.65e-03
10 20 30 40 50 60 70 80
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gi 1337428519 2 LNVVILAAGLGKRMQS---DLPKVLHTLAGKPMLAHVLASARELAPARITVVVGHGADRVKQAFGGQEG-----LHFALQ 73
Cdd:cd06425 1 MKALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKklgikITFSIE 80
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90 100 110 120 130 140 150 160
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gi 1337428519 74 QPQQGTGHAVQQAVPLLLEGdgkDDVTLVLYGDVPLVQPdtLRRLLAAR----GDGAAVLTEVlDDSTGYGRIVRDAA-G 148
Cdd:cd06425 81 TEPLGTAGPLALARDLLGDD---DEPFFVLNSDVICDFP--LAELLDFHkkhgAEGTILVTKV-EDPSKYGVVVHDENtG 154
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....*..
gi 1337428519 149 QVCRIVE 155
Cdd:cd06425 155 RIERFVE 161
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