|
Name |
Accession |
Description |
Interval |
E-value |
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-454 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 834.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 4 RYAIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKYALQAEQLGTGHAV 83
Cdd:PRK14354 3 RYAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFALQEEQLGTGHAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 84 LQAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATPEE 163
Cdd:PRK14354 83 MQAEEFLADKEGTTLVICGDTPLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKIVEQKDATEEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 164 ALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANEIMRKR 243
Cdd:PRK14354 163 KQIKEINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGEKVGAYQTEDFEESLGVNDRVALAEAEKVMRRR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 244 INQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIENSVIESSHVKKH 323
Cdd:PRK14354 243 INEKHMVNGVTIIDPESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVDSTIGDGVTITNSVIEESKVGDN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 324 ADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFI 403
Cdd:PRK14354 323 VTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVNYDGKNKFKTIIGDNAFI 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488216138 404 GSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYAKKLP 454
Cdd:PRK14354 403 GCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKEGYVKKLP 453
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-452 |
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: 777.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 4 RYAIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGE-RSKYALQAEQLGTGHA 82
Cdd:COG1207 3 LAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADlDVEFVLQEEQLGTGHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 83 VLQAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATPE 162
Cdd:COG1207 83 VQQALPALPGDDGTVLVLYGDVPLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRIVEEKDATEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 163 EALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANEIMRK 242
Cdd:COG1207 163 QRAIREINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADGLKVAAVQPEDPWEVLGVNDRVQLAEAERILQR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 243 RINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIENSVIESSHVKK 322
Cdd:COG1207 243 RIAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSVIEDAVVGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 323 HADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSF 402
Cdd:COG1207 323 GATVGPFARLRPGTVLGEGVKIGNFVEVKNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDGAF 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 488216138 403 IGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYAKK 452
Cdd:COG1207 403 IGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIEGWVRP 452
|
|
| glmU |
TIGR01173 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
6-452 |
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: 621.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERS-KYALQAEQLGTGHAVL 84
Cdd:TIGR01173 3 VVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALANRDvNWVLQAEQLGTGHAVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 85 QAASFLEgKKGTTLVISGDTPLLTTETLNNLFEYHQgkNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATPEEA 164
Cdd:TIGR01173 83 QALPFLS-DDGDVLVLYGDVPLISAETLERLLEAHR--QNGITLLTAKLDDPTGYGRIIRENDGKVTAIVEDKDANAEQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 165 LVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANEIMRKRI 244
Cdd:TIGR01173 160 AIKEINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRAVQVDDSDEVLGVNDRLQLAQLERILQRRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 245 NQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIE-NSVIESSHVKKH 323
Cdd:TIGR01173 240 AKKLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKVKIGDDVVIGPGCVIKNSVIGSNVVIKaYSVLEGSEIGEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 324 ADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFI 403
Cdd:TIGR01173 320 CDVGPFARLRPGSVLGAGVHIGNFVEVKNARIGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHKTIIGDGVFI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 488216138 404 GSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYAKK 452
Cdd:TIGR01173 400 GSNTQLVAPVKVGDGATIAAGSTVTKDVPEGALAISRARQRNIEGWVRP 448
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-449 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 538.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 1 MDARYAIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERS--KYALQAEQLG 78
Cdd:PRK14355 1 MNNLAAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGdvSFALQEEQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 79 TGHAVLQAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKD 158
Cdd:PRK14355 81 TGHAVACAAPALDGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIVEEKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 159 ATPEEALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANE 238
Cdd:PRK14355 161 ATPEERSIREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAAEGLRCLAFPVADPDEIMGVNDRAQLAEAAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 239 IMRKRINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIE-NSVIES 317
Cdd:PRK14355 241 VLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKaGSVLED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 318 SHVKKHADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTV 397
Cdd:PRK14355 321 SVVGDDVAIGPMAHLRPGTELSAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHRTVI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488216138 398 GDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGY 449
Cdd:PRK14355 401 EDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKEGW 452
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-454 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 529.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKY---ALQAEQLGTGHA 82
Cdd:PRK14352 7 VIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEvdiAVQDEQPGTGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 83 VLQAASFLEGK-KGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATP 161
Cdd:PRK14352 87 VQCALEALPADfDGTVVVTAGDVPLLDGETLADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQDGEVTAIVEQKDATP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 162 EEALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANEIMR 241
Cdd:PRK14352 167 SQRAIREVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAIAREAGHRVGAHHADDSAEVAGVNDRVQLAALGAELN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 242 KRINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIENSVIESSHVK 321
Cdd:PRK14352 247 RRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVRTHGSESEIG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 322 KHADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHS 401
Cdd:PRK14352 327 AGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVNKHRTTIGSHV 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488216138 402 FIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGY-AKKLP 454
Cdd:PRK14352 407 RTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSEGPQRNIEGWvQRKRP 460
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-454 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 525.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 8 ILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSK--YALQAEQLGTGHAVLQ 85
Cdd:PRK14360 6 ILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPGleFVEQQPQLGTGHAVQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 86 AASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATPEEAL 165
Cdd:PRK14360 86 LLPVLKGFEGDLLVLNGDVPLLRPETLEALLNTHRSSNADVTLLTARLPNPKGYGRVFCDGNNLVEQIVEDRDCTPAQRQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 166 VQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKeeghTVAAYQTDDFEESMGVNDRIALAKANEIMRKRIN 245
Cdd:PRK14360 166 NNRINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTVSLLD----PVMAVEVEDYQEINGINDRKQLAQCEEILQNRIK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 246 QMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIENSVIESSHVKKHAD 325
Cdd:PRK14360 242 EKWMLAGVTFIDPASCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIENSQIGENVTVLYSVVSDSQIGDGVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 326 VGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFIGS 405
Cdd:PRK14360 322 IGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDGVKKHRTVIGDRSKTGA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 488216138 406 STNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYAKKLP 454
Cdd:PRK14360 402 NSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKENWKKKSS 450
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-453 |
1.25e-167 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 478.97 E-value: 1.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKYA---LQAEQLGTGHA 82
Cdd:PRK14353 8 AIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAeifVQKERLGTAHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 83 VLQAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKnASATILTAQAENPTGYGRIIRDHiGIVEKIVEQKDATPE 162
Cdd:PRK14353 88 VLAAREALAGGYGDVLVLYGDTPLITAETLARLRERLADG-ADVVVLGFRAADPTGYGRLIVKG-GRLVAIVEEKDASDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 163 EALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDdFEESMGVNDRIALAKANEIMRK 242
Cdd:PRK14353 166 ERAITLCNSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIARAEGLRVAVVEAP-EDEVRGINSRAELAEAEAVWQA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 243 RINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAgvqiqgNTVIGSDCvigshskivdsRIEDHVVIEN-SVIESSHVK 321
Cdd:PRK14353 245 RRRRAAMLAGVTLIAPETVFFSYDTVIGRDVVIEP------NVVFGPGV-----------TVASGAVIHAfSHLEGAHVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 322 KHADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHS 401
Cdd:PRK14353 308 EGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGAGANIGAGTITCNYDGFNKHRTEIGAGA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488216138 402 FIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYAKKL 453
Cdd:PRK14353 388 FIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKPGWAKKL 439
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-452 |
1.59e-166 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 476.56 E-value: 1.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKpDEVITIVGHGAEQVKAQLGERSKYALQAEQLGTGHAVLQ 85
Cdd:PRK14357 3 ALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEWVKIFLQEEQLGTAHAVMC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 86 AASFLEgKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIveKIVEQKDATPEEAL 165
Cdd:PRK14357 82 ARDFIE-PGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKY--RIVEDKDAPEEEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 166 VQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEeghtVAAYQTDDFEESMGVNDRIALAKANEIMRKRIN 245
Cdd:PRK14357 159 IKEINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAVNFAEK----VRVVKTEDLLEITGVNTRIQLAWLEKQLRMRIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 246 QMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIENSVIESSHVKKHAD 325
Cdd:PRK14357 235 EELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKIIRSECEKSVIEDDVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 326 VGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFIGS 405
Cdd:PRK14357 315 VGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTFIEDGAFIGS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 488216138 406 STNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYAKK 452
Cdd:PRK14357 395 NSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWVLK 441
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
7-456 |
6.43e-158 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 455.59 E-value: 6.43e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 7 IILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQL-GERSKYALQAEQLGTGHAVLQ 85
Cdd:PRK14358 11 VILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALqGSGVAFARQEQQLGTGDAFLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 86 AASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATPEEAL 165
Cdd:PRK14358 91 GASALTEGDADILVLYGDTPLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQKDATDAEKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 166 VQEINTGTYCFDNEALfDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANEIMRKRIN 245
Cdd:PRK14358 171 IGEFNSGVYVFDARAP-ELARRIGNDNKAGEYYLTDLLGLYRAGGAQVRAFKLSDPDEVLGANDRAGLAQLEATLRRRIN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 246 QMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIE-NSVIESSHVKKHA 324
Cdd:PRK14358 250 EAHMKAGVTLQDPGTILIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSVLHEGAVIKpHSVLEGAEVGAGS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 325 DVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFIG 404
Cdd:PRK14358 330 DVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNKHQSKVGAGVFIG 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488216138 405 SSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGYA------------KKLPYL 456
Cdd:PRK14358 410 SNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNLEGWSrrywagrhekvaKKLPWL 473
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-449 |
3.36e-149 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 432.53 E-value: 3.36e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 1 MDARYAIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERS-KYALQAEQLGT 79
Cdd:PRK09451 3 NSAMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEPlNWVLQAEQLGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 80 GHAVLQAASFLEGKKgTTLVISGDTPLLTTETLNNLFEYH-QGKNAsatILTAQAENPTGYGRIIRDHiGIVEKIVEQKD 158
Cdd:PRK09451 83 GHAMQQAAPFFADDE-DILMLYGDVPLISVETLQRLRDAKpQGGIG---LLTVKLDNPTGYGRITREN-GKVVGIVEQKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 159 ATPEEALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANE 238
Cdd:PRK09451 158 ATDEQRQIQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGREIVAVHPQRLSEVEGVNNRLQLARLER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 239 IMRKRINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIEN-SVIES 317
Cdd:PRK09451 238 VYQAEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPySVVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 318 SHVKKHADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTV 397
Cdd:PRK09451 318 ANLGAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTII 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488216138 398 GDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGY 449
Cdd:PRK09451 398 GDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGW 449
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-449 |
1.16e-139 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 407.45 E-value: 1.16e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 7 IILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDeVITIVGHGAEQVKAQLGERS---KYALQAEQ--LGTGH 81
Cdd:PRK14359 6 IILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAISDD-VHVVLHHQKERIKEAVLEYFpgvIFHTQDLEnyPGTGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 82 AVLQAAsfLEGKKgtTLVISGDTPLLTTETLNNLFEYHQGKNASATiltaQAENPTGYGRIIRDHiGIVEKIVEQKDATP 161
Cdd:PRK14359 85 ALMGIE--PKHER--VLILNGDMPLVEKDELEKLLENDADIVMSVF----HLADPKGYGRVVIEN-GQVKKIVEQKDANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 162 EEALVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDfEESMGVNDRIALAKANEIMR 241
Cdd:PRK14359 156 EELKIKSVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAVFVDE-ENFMGVNSKFELAKAEEIMQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 242 KRINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNtvigsdcvigshSKIVDSRIEDHVVIENSVIESShvk 321
Cdd:PRK14359 235 ERIKKNAMKQGVIMRLPETIYIESGVEFEGECELEEGVRILGK------------SKIENSHIKAHSVIEESIIENS--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 322 khaDVGPYAHLRPKAEIgENVHIGNFVEVKNAQIgKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHS 401
Cdd:PRK14359 300 ---DVGPLAHIRPKSEI-KNTHIGNFVETKNAKL-NGVKAGHLSYLGDCEIDEGTNIGAGTITCNYDGKKKHKTIIGKNV 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 488216138 402 FIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNKEGY 449
Cdd:PRK14359 375 FIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIKNF 422
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-446 |
4.39e-136 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 399.10 E-value: 4.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQL-GERSKYALQAEQLGTGHAVL 84
Cdd:PRK14356 8 ALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFpDEDARFVLQEQQLGTGHALQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 85 QAASFLEgKKGTT--LVISGDTPLLTTETLNNLFEyhQGKNASATILTAQAENPTGYGRIIRDHiGIVEKIVEQKDAtpE 162
Cdd:PRK14356 88 CAWPSLT-AAGLDrvLVVNGDTPLVTTDTIDDFLK--EAAGADLAFMTLTLPDPGAYGRVVRRN-GHVAAIVEAKDY--D 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 163 EAL----VQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANE 238
Cdd:PRK14356 162 EALhgpeTGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAVAEGMNVLGVNCGEDPNLLGVNTPAELVRSEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 239 IMRKRINQMHMVNGVsFVDSATTyidagVEIGPDTLIEAGVQIQG------NTVIGSDCVIGSHSKIVDSRIEDHVVIEN 312
Cdd:PRK14356 242 LLRARIVEKHLESGV-LIHAPES-----VRIGPRATIEPGAEIYGpceiygASRIARGAVIHSHCWLRDAVVSSGATIHS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 313 -SVIESSHVKKHADVGPYAHLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKN 391
Cdd:PRK14356 316 fSHLEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488216138 392 KHHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNK 446
Cdd:PRK14356 396 KHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQKNL 450
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-233 |
9.18e-123 |
|
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: 356.44 E-value: 9.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERS-KYALQAEQLGTGHAVL 84
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNvEFVLQEEQLGTGHAVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 85 QAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQKDATPEEA 164
Cdd:cd02540 81 QALPALKDFEGDVLVLYGDVPLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVEEKDATEEEK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488216138 165 LVQEINTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIAL 233
Cdd:cd02540 161 AIREVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVAAVLADDEEEVLGVNDRVQL 229
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
252-443 |
1.92e-107 |
|
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: 316.28 E-value: 1.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 252 GVSFVDSATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVDSRIEDHVVIE-NSVIESSHVKKHADVGPYA 330
Cdd:cd03353 1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKaSSVIEGAVIGNGATVGPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 331 HLRPKAEIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFIGSSTNII 410
Cdd:cd03353 81 HLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDNVFIGSNSQLV 160
|
170 180 190
....*....|....*....|....*....|...
gi 488216138 411 GPVEVAKNSSIAAGSTITDNIPEYALAIARARQ 443
Cdd:cd03353 161 APVTIGDGATIAAGSTITKDVPPGALAIARARQ 193
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-221 |
2.31e-50 |
|
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: 170.45 E-value: 2.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMK---SKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSK------YALQAEQ 76
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKfgvnieYVVQEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LGTGHAVLQAASFLegKKGTTLVISGDTplLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEq 156
Cdd:cd04181 81 LGTAGAVRNAEDFL--GDDDFLVVNGDV--LTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVE- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216138 157 KDATPEEALvqeINTGTYCFDNEaLFDALSKVGTNnaqGEYYLTDIIEILKEEGhTVAAYQTDDF 221
Cdd:cd04181 156 KPTLPESNL---ANAGIYIFEPE-ILDYIPEILPR---GEDELTDAIPLLIEEG-KVYGYPVDGY 212
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-236 |
5.19e-41 |
|
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: 146.45 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMK---SKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSK------YALQAEQ 76
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRfgvritYVDEGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LGTGHAVLQAASFLEGkkGTTLVISGDTplLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEQ 156
Cdd:COG1208 82 LGTGGALKRALPLLGD--EPFLVLNGDI--LTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 157 kdatPEEALVQEINTGTYCFDNEaLFDALSKvgtnnaQGEYYLTDIIEILKEEGhTVAAYQTDDFEESMGVNDRIALAKA 236
Cdd:COG1208 158 ----PEEPPSNLINAGIYVLEPE-IFDYIPE------GEPFDLEDLLPRLIAEG-RVYGYVHDGYWLDIGTPEDLLEANA 225
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-240 |
1.92e-31 |
|
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: 120.37 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLY---KVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSK------YALQAEQ 76
Cdd:cd04189 3 GLILAGGKGTRLRPLTYtrpKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRfgvritYILQEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LGTGHAVLQAASFLEGKKgtTLVISGDTplLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDhIGIVEKIVEq 156
Cdd:cd04189 83 LGLAHAVLAARDFLGDEP--FVVYLGDN--LIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 157 KDATPEE--ALVqeintGTYCFdNEALFDALSKVgTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRiaLA 234
Cdd:cd04189 157 KPKEPPSnlALV-----GVYAF-TPAIFDAISRL-KPSWRGELEITDAIQWLIDRGRRVGYSIVTGWWKDTGTPED--LL 227
|
....*.
gi 488216138 235 KANEIM 240
Cdd:cd04189 228 EANRLL 233
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-213 |
2.02e-31 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 122.12 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRmkskLY-------KVLHPVSGKPMVEHIINRVSETKPDEVITIVG-HGAEQVKAQLGERSK------YA 71
Cdd:COG1209 3 GIILAGGSGTR----LRpltltvsKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGSQlgikisYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 72 LQAEQLGTGHAVLQAASFLEGKKgtTLVISGDTpLLTTETLNNLFEYHQGKNASATILTAQAENPTGYG--------RII 143
Cdd:COG1209 79 VQPEPLGLAHAFIIAEDFIGGDP--VALVLGDN-IFYGDGLSELLREAAARESGATIFGYKVEDPERYGvvefdedgRVV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216138 144 RdhigIVEKiveqkdatPEE-----ALvqeinTGTYCFDNEaLFDALSKVgTNNAQGEYYLTDIIEILKEEGHTV 213
Cdd:COG1209 156 S----LEEK--------PKEpksnlAV-----TGLYFYDND-VVEIAKNL-KPSARGELEITDANQAYLERGKLV 211
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-222 |
2.42e-29 |
|
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: 115.04 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMK---SKLYKVLHPVSGK-PMVEHIINRVSETKPDEVITIVG-HGAEQVKAQLGERSK------YALQA 74
Cdd:pfam00483 2 AIILAGGSGTRLWpltRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGDGSKfgvqitYALQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 75 EQLGTGHAVLQAASFLEGKKGTTLVISGDtpLLTTETLNNLFEYHQGKNA--SATILTAQAENPTGYGRIIRDHIGIVEK 152
Cdd:pfam00483 82 EGKGTAPAVALAADFLGDEKSDVLVLGGD--HIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488216138 153 IVEQkdatPEEALVQE-INTGTYCFDNEAlFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFE 222
Cdd:pfam00483 160 FVEK----PKLPKASNyASMGIYIFNSGV-LDFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYA 225
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-181 |
8.83e-26 |
|
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: 104.56 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKS---KLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERS------KYALQAEQ 76
Cdd:cd06915 1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYrggiriYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LGTGHAVLQAASFLEGKKgtTLVISGDTpLLTTEtLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIVEKIVEq 156
Cdd:cd06915 81 LGTGGAIKNALPKLPEDQ--FLVLNGDT-YFDVD-LLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVE- 155
|
170 180
....*....|....*....|....*
gi 488216138 157 KDATPEEALvqeINTGTYCFDNEAL 181
Cdd:cd06915 156 KGPGAAPGL---INGGVYLLRKEIL 177
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
275-427 |
2.50e-24 |
|
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: 98.81 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 275 IEAGVQIQGNTVIGSDcvigshskivdSRIEDHVVIENSVIesshVKKHADVGPYAHLRPKAEIGENVHIGNFVEVKNAQ 354
Cdd:cd05636 8 VEEGVTIKGPVWIGEG-----------AIVRSGAYIEGPVI----IGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216138 355 IGKGTKVGHLTYVGDATLGEEINVGCGVVFVNY--DGKNKHHTTVGDHSFIGSST--NIIGP-VEVAKNSSIAAGSTI 427
Cdd:cd05636 73 IMDGTKVPHLNYVGDSVLGENVNLGAGTITANLrfDDKPVKVRLKGERVDTGRRKlgAIIGDgVKTGINVSLNPGVKI 150
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-216 |
5.01e-24 |
|
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: 99.51 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMK---SKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSK------YALQAEQ 76
Cdd:cd06426 1 VVIMAGGKGTRLRpltENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKfgvnisYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LGTGHAVlqaaSFLEGK-KGTTLVISGDtpLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRI-IRDH--IGIVEK 152
Cdd:cd06426 81 LGTAGAL----SLLPEKpTDPFLVMNGD--ILTNLNYEHLLDFHKENNADATVCVREYEVQVPYGVVeTEGGriTSIEEK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216138 153 iveqkdatPEEalVQEINTGTYCFDNEALfDALSKvgtnnaqGEYY-LTDIIEILKEEGHTVAAY 216
Cdd:cd06426 155 --------PTH--SFLVNAGIYVLEPEVL-DLIPK-------NEFFdMPDLIEKLIKEGKKVGVF 201
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
6-128 |
2.60e-17 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 79.82 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKS-KLykvLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKYALQAE--QLGTGHA 82
Cdd:COG2068 6 AIILAAGASSRMGRpKL---LLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPdwEEGMSSS 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488216138 83 VLQAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATI 128
Cdd:COG2068 83 LRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVA 128
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
6-147 |
3.31e-17 |
|
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: 78.78 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKS-KLykvLHPVSGKPMVEHIINRVSETkPDEVItIVGhGAEQVKAQLgERSKYAL---QAEQLGTGH 81
Cdd:pfam12804 1 AVILAGGRSSRMGGdKA---LLPLGGKPLLERVLERLRPA-GDEVV-VVA-NDEEVLAAL-AGLGVPVvpdPDPGQGPLA 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216138 82 AVLQAASFLEGKKGTtLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAE--NPTGYGRIIRDHI 147
Cdd:pfam12804 74 GLLAALRAAPGADAV-LVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGrgHPLLYRRRLLPAL 140
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-141 |
4.28e-17 |
|
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: 79.14 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKS-KLykvLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKYALQAE--QLGTGHA 82
Cdd:cd04182 3 AIILAAGRSSRMGGnKL---LLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPdwEEGMSSS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488216138 83 VLQAASFLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAE--NPTGYGR 141
Cdd:cd04182 80 LAAGLEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGRrgHPVLFPR 140
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
259-433 |
2.30e-16 |
|
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: 77.45 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 259 ATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIV-DSRIEDHVVIE-NSVI----------ESSHVKKHadv 326
Cdd:cd03352 12 PNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYeGCIIGDRVIIHsGAVIgsdgfgfapdGGGWVKIP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 327 gpyahlrpkaEIGeNVHIGNFVEV-----------KNAQIGKGTK------VGHLTYVGDATLgeeInVGCgvvfVNYDG 389
Cdd:cd03352 89 ----------QLG-GVIIGDDVEIganttidrgalGDTVIGDGTKidnlvqIAHNVRIGENCL---I-AAQ----VGIAG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488216138 390 knkhHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPE 433
Cdd:cd03352 150 ----STTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPP 189
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-181 |
3.09e-15 |
|
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: 74.94 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKS---KLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSK-------YALQAE 75
Cdd:cd06425 3 ALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKklgikitFSIETE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 76 QLGTGHAVLQAASFLEGKKGTTLVISGDtpLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHI-GIVEKIV 154
Cdd:cd06425 83 PLGTAGPLALARDLLGDDDEPFFVLNSD--VICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERFV 160
|
170 180
....*....|....*....|....*..
gi 488216138 155 EQkdatPEEALVQEINTGTYCFDNEAL 181
Cdd:cd06425 161 EK----PKVFVGNKINAGIYILNPSVL 183
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
261-433 |
3.52e-15 |
|
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: 76.21 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 261 TYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIV-DSRIEDHVVIE-NSVI-----------ESSHVKKHadvg 327
Cdd:COG1044 121 AVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYeRCVIGDRVIIHsGAVIgadgfgfapdeDGGWVKIP---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 328 pyahlrpkaEIGeNVHIGNFVEV-----------KNAQIGKGTK------VGHLTYVGDATLgeeInVGC----Gvvfvn 386
Cdd:COG1044 197 ---------QLG-RVVIGDDVEIganttidrgalGDTVIGDGTKidnlvqIAHNVRIGEHTA---I-AAQvgiaG----- 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488216138 387 ydgknkhHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPE 433
Cdd:COG1044 258 -------STKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPE 297
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
338-444 |
7.21e-15 |
|
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: 70.61 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 338 IGENVHIGNFVEV-KNAQIGKGTKVGHLTYVGD-ATLGEEINVGCGVVFVN--------YDGKNKHHTTVGDHSFIGSST 407
Cdd:cd03358 1 IGDNCIIGTNVFIeNDVKIGDNVKIQSNVSIYEgVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANA 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 488216138 408 NIIGPVEVAKNSSIAAGSTITDNIPEYALAIAR-ARQV 444
Cdd:cd03358 81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNpARII 118
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
262-433 |
9.39e-15 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 75.18 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 262 YIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIV-DSRIEDHVVIE-NSVI----------ESSHVKkhadvgpy 329
Cdd:PRK00892 126 VIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYhAVRIGNRVIIHsGAVIgsdgfgfandRGGWVK-------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 330 ahlrpKAEIGeNVHIGNFVEV-----------KNAQIGKGTK------VGHLTYVGDATLgeeINVGCGVVfvnydGKnk 392
Cdd:PRK00892 198 -----IPQLG-RVIIGDDVEIganttidrgalDDTVIGEGVKidnlvqIAHNVVIGRHTA---IAAQVGIA-----GS-- 261
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488216138 393 hhTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPE 433
Cdd:PRK00892 262 --TKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPE 300
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
263-448 |
9.53e-14 |
|
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: 70.92 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 263 IDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKI-VDSRIEDHVVIENsviESSHVKkhadvgpYAHLRPKAEIGEN 341
Cdd:cd03351 14 IGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIgKNNRIFPFASIGE---APQDLK-------YKGEPTRLEIGDN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 342 VHIGNFVevknaQIGKGTKVGH-LTYVGDATL-------GEEINVGCGVVFVNydgkNKH---HTTVGDHSFIGSSTNII 410
Cdd:cd03351 84 NTIREFV-----TIHRGTAQGGgVTRIGNNNLlmayvhvAHDCVIGNNVILAN----NATlagHVEIGDYAIIGGLSAVH 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488216138 411 GPVEVAKNSSIAAGSTITDNIPEYALAI---ARARQVNKEG 448
Cdd:cd03351 155 QFCRIGRHAMVGGGSGVVQDVPPYVIAAgnrARLRGLNLVG 195
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-186 |
1.17e-13 |
|
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: 69.91 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKS---KLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERsKYALQ-------AE 75
Cdd:cd06422 2 AMILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDS-RFGLRitisdepDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 76 QLGTGHAVLQAASFLEGkkGTTLVISGDTplLTTETLNNLFEYHQGKNASATILTAQAENP--TGYGRIIRDHIGIVEKI 153
Cdd:cd06422 81 LLETGGGIKKALPLLGD--EPFLVVNGDI--LWDGDLAPLLLLHAWRMDALLLLLPLVRNPghNGVGDFSLDADGRLRRG 156
|
170 180 190
....*....|....*....|....*....|...
gi 488216138 154 VEQKDAtpeealvQEINTGTYCFDNEaLFDALS 186
Cdd:cd06422 157 GGGAVA-------PFTFTGIQILSPE-LFAGIP 181
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
6-221 |
1.20e-13 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 70.75 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAG--KGTRMKS---KLYKVLHPVSGKPMVEHIINRVSETkPD--EVITIVGHGAEQ-------VKAQLGERSKYA 71
Cdd:cd06428 1 AVILVGGpqKGTRFRPlslDVPKPLFPVAGKPMIHHHIEACAKV-PDlkEVLLIGFYPESVfsdfisdAQQEFNVPIRYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 72 LQAEQLGTGHAVLqaaSF----LEGKKGTTLVISGDT----PllttetLNNLFEYHQGKNASATILT--AQAENPTGYGR 141
Cdd:cd06428 80 QEYKPLGTAGGLY---HFrdqiLAGNPSAFFVLNADVccdfP------LQELLEFHKKHGASGTILGteASREQASNYGC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 142 IIRD-HIGIVEKIVEQkdatPEEALVQEINTGTYCFDNEaLFDALSKV------------GTNNAQGEYYL---TDIIEI 205
Cdd:cd06428 151 IVEDpSTGEVLHYVEK----PETFVSDLINCGVYLFSPE-IFDTIKKAfqsrqqeaqlgdDNNREGRAEVIrleQDVLTP 225
|
250
....*....|....*.
gi 488216138 206 LKEEGHtVAAYQTDDF 221
Cdd:cd06428 226 LAGSGK-LYVYKTDDF 240
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-223 |
2.24e-13 |
|
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: 69.18 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLY---KVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGER--------SKYAlqa 74
Cdd:cd02523 1 AIILAAGRGSRLRPLTEdrpKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpnikfvynPDYA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 75 eQLGTGHAVLQAASFLEGKkgtTLVISGDTpLLTTETLNNLFEYhqGKNASATILTAQAENPTGYGRIIRDHIGIVEKIv 154
Cdd:cd02523 78 -ETNNIYSLYLARDFLDED---FLLLEGDV-VFDPSILERLLSS--PADNAILVDKKTKEWEDEYVKDLDDAGVLLGII- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488216138 155 eQKDATPEEALVQEIntGTYCFDNE---ALFDALSKVGTNNAQGEYYlTDIIE-ILKEEGHTVAAYQT------DDFEE 223
Cdd:cd02523 150 -SKAKNLEEIQGEYV--GISKFSPEdadRLAEALEELIEAGRVNLYY-EDALQrLISEEGVKVKDISDgfwyeiDDLED 224
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
6-163 |
1.35e-12 |
|
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.
Pssm-ID: 274516 Cd Length: 188 Bit Score: 66.21 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRM-KSKLykvLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKYAL----QAEQlGTG 80
Cdd:TIGR03310 2 AIILAAGLSSRMgQNKL---LLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANHSNITLvhnpQYAE-GQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 81 HAVLQAASFLEGKKGtTLVISGDTPLLTTETLNNLFEY------------HQGKNASATILTAQ-------AENPTGYGR 141
Cdd:TIGR03310 78 SSIKLGLELPVQSDG-YLFLLGDQPFVTPDIIQLLLEAfalkndeivvplYKGKRGHPVLFPRKlfpellaLTGDTGGRQ 156
|
170 180
....*....|....*....|....*....
gi 488216138 142 IIRDHIGIVeKIVEQKDA-------TPEE 163
Cdd:TIGR03310 157 ILRELPHEV-KYVEVKDPgilfdidTPED 184
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
198-438 |
3.01e-12 |
|
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: 65.20 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 198 YLTDIIEILKEEGHTVAAYQTDDFEESMGVNDRIALAKANEIMRKRINQMHMVNGVSFVdsatTYIDAGVEIGPDTLIEA 277
Cdd:cd03360 26 FLDDDPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLRRKLAEKLLAAGYRFA----TLIHPSAVVSPSAVIGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 278 GVQIQGNTVIGSDCVIGshskivdsrieDHVVIeNSvieSSHVKKHADVGPYAHLRPKAEIGENVHIGnfvevknaqigk 357
Cdd:cd03360 102 GCVIMAGAVINPDARIG-----------DNVII-NT---GAVIGHDCVIGDFVHIAPGVVLSGGVTIG------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 358 gtkvghltyvgdatlgeeinvgcgvvfvnydgknkhhttvgDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALA 437
Cdd:cd03360 155 -----------------------------------------EGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVV 193
|
.
gi 488216138 438 I 438
Cdd:cd03360 194 V 194
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
332-437 |
1.19e-11 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 62.20 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 332 LRPKAEIGENVHIGNFVEV--KNAQIGKGTKVG---HLTYVGDATLGEEINVGCGVVFVN----YDGKNKH-----HTTV 397
Cdd:COG0110 5 LLFGARIGDGVVIGPGVRIygGNITIGDNVYIGpgvTIDDPGGITIGDNVLIGPGVTILTgnhpIDDPATFplrtgPVTI 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488216138 398 GDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALA 437
Cdd:COG0110 85 GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIV 124
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-239 |
1.62e-11 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 64.11 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLY---KVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERS---KYAL--QAEQL 77
Cdd:COG1213 2 AVILAAGRGSRLGPLTDdipKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGpdvTFVYnpDYDET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 78 GTGHAVLQAASFLEGKkgtTLVISGDTpLLTTETLNNLFEYhqgKNASATILTAQAENPTGYG-RIIRDHIGIVEKIVeq 156
Cdd:COG1213 82 NNIYSLWLAREALDED---FLLLNGDV-VFDPAILKRLLAS---DGDIVLLVDRKWEKPLDEEvKVRVDEDGRIVEIG-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 157 KDATPEEALVQEIntGTYCF---DNEALFDALSKVGTNNAQGEYYlTDIIEILKEEGHTVAAYQTD-------DFEEsmg 226
Cdd:COG1213 153 KKLPPEEADGEYI--GIFKFsaeGAAALREALEALIDEGGPNLYY-EDALQELIDEGGPVKAVDIGglpwveiDTPE--- 226
|
250
....*....|...
gi 488216138 227 vndriALAKANEI 239
Cdd:COG1213 227 -----DLERAEEL 234
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
9-140 |
3.31e-11 |
|
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: 62.21 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 9 LAAGKGTRMKSKLyKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLGERSKYALQAEqlGTGHAV-LQAA 87
Cdd:COG2266 1 MAGGKGTRLGGGE-KPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKERGVEVIETP--GEGYVEdLNEA 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488216138 88 sfLEGKKGTTLVISGDTPLLTTETLNNLFEYHQGKNASATILTAQAENPTGYG 140
Cdd:COG2266 78 --LESISGPVLVVPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPAALKRELG 128
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-128 |
4.10e-11 |
|
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: 61.75 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 1 MDARY-AIILAAGKGTRMKSKlyKVLHPVSGKPMVEHIINRVSETkPDEVItIVGHGAEQVkAQLGERskyALQAEQLGT 79
Cdd:COG0746 1 MTMPItGVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLRPQ-VDEVV-IVANRPERY-AALGVP---VVPDDPPGA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488216138 80 G-----HAVLQAAsflegKKGTTLVISGDTPLLTTETLNNLFEYHQgKNASATI 128
Cdd:COG0746 73 GplagiLAALEAA-----PAEWVLVLACDMPFLPPDLVRRLLEALE-EGADAVV 120
|
|
| PRK05289 |
PRK05289 |
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
263-448 |
5.21e-11 |
|
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 62.81 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 263 IDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKI-VDSRIEDHVVIENsviESSHVKkhadvgpYAHLRPKAEIGEN 341
Cdd:PRK05289 17 IGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIgKNNRIFPFASIGE---DPQDLK-------YKGEPTRLVIGDN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 342 VHIGNFVevknaQIGKGT-KVGHLTYVGDATL-------GEEINVGCGVVFVNY---DGknkhHTTVGDHSFIGSSTNII 410
Cdd:PRK05289 87 NTIREFV-----TINRGTvQGGGVTRIGDNNLlmayvhvAHDCVVGNHVILANNatlAG----HVEVGDYAIIGGLTAVH 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488216138 411 GPVEVAKNSSIAAGSTITDNIPEYALAI---ARARQVNKEG 448
Cdd:PRK05289 158 QFVRIGAHAMVGGMSGVSQDVPPYVLAEgnpARLRGLNLVG 198
|
|
| LpxA |
COG1043 |
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
261-448 |
6.46e-11 |
|
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: 62.34 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 261 TYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHskivdsriedhvvienSVI--ESSHVKkhadvgpYAHLRPKAEI 338
Cdd:COG1043 26 CVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPF----------------ASIgeEPQDLK-------YKGEPTRLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 339 GENVHIGNFVevknaQIGKGTKVGH-LTYVGDATL-------GEEINVGCGVVFVNY---DGknkhHTTVGDHSFIGSST 407
Cdd:COG1043 83 GDNNTIREFV-----TIHRGTVQGGgVTRIGDDNLlmayvhvAHDCVVGNNVILANNatlAG----HVEVGDHAIIGGLS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488216138 408 NIIGPVEVAKNSSIAAGSTITDNIPEYALAI---ARARQVNKEG 448
Cdd:COG1043 154 AVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAgnpARLRGLNLVG 197
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
219-438 |
1.12e-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: 60.97 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 219 DDFEESMGVNDRIALAKANEIMRKRINQMHMVNGVSFVdsatTYIDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGshsk 298
Cdd:TIGR03570 50 EDLLRYPPDEVDLVVAIGDNKLRRRLVEKLKAKGYRFA----TLIHPSAIVSPSASIGEGTVIMAGAVINPDVRIG---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 299 ivdsrieDHVVIeNSvieSSHVKKHADVGPYAHLRPKAEIGENVHIGnfvevknaqigkgtkvghltyvgdatlgeeinv 378
Cdd:TIGR03570 122 -------DNVII-NT---GAIVEHDCVIGDFVHIAPGVTLSGGVVIG--------------------------------- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 379 gcgvvfvnydgknkhhttvgDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAI 438
Cdd:TIGR03570 158 --------------------EGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVV 197
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
4-117 |
1.85e-10 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 59.90 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 4 RYAIILAAGKGTRMKSKlyKVLHPVSGKPMVEHIINRVSETkPDEVItIVGHGAEQVKAQLGERskyALQAEQLGTG--- 80
Cdd:cd02503 1 ITGVILAGGKSRRMGGD--KALLELGGKPLLEHVLERLKPL-VDEVV-ISANRDQERYALLGVP---VIPDEPPGKGpla 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 488216138 81 --HAVLQAAsflegKKGTTLVISGDTPLLTTETLNNLFE 117
Cdd:cd02503 74 giLAALRAA-----PADWVLVLACDMPFLPPELLERLLA 107
|
|
| LbH_SAT |
cd03354 |
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
353-438 |
3.97e-10 |
|
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: 56.68 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 353 AQIGKGTKVGHLTYV---GDATLGEEINVGCGVVF-VNYDGKNKHHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTIT 428
Cdd:cd03354 9 AKIGPGLFIDHGTGIvigETAVIGDNCTIYQGVTLgGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT 88
|
90
....*....|
gi 488216138 429 DNIPEYALAI 438
Cdd:cd03354 89 KDVPANSTVV 98
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
7-219 |
3.03e-09 |
|
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: 57.26 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 7 IILAAGKGTRMKSKLYKVLHP---VSGKPMVEHIINRVSETKPDEVITIVG-------HGAEQVKAQLGERSKYALQAEQ 76
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPlieVDGKPMIEWVIESLAKIFDSRFIFICRdehntkfHLDESLKLLAPNATVVELDGET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LGTGHAVLQAASFLEGKKgTTLVISGDTplLTTETLNNLFEYHQGKNASATILTAQAENPtGYGRIIRDHIGIVEKIVEq 156
Cdd:cd04183 82 LGAACTVLLAADLIDNDD-PLLIFNCDQ--IVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIETAE- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488216138 157 KDATPEEALVqeintGTYCFDNEALF-DALSKVGTNNAQ--GEYYLTDIIEILKEEGHTVAAYQTD 219
Cdd:cd04183 157 KEPISDLATA-----GLYYFKSGSLFvEAAKKMIRKDDSvnGEFYISPLYNELILDGKKVGIYLID 217
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
4-219 |
3.56e-09 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 57.54 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 4 RYAIILAAGKGTRM----KSkLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHG----------AEQVKAQLGERSK 69
Cdd:cd02541 1 RKAVIPAAGLGTRFlpatKA-IPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfdrSYELEETLEKKGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 70 YAL-----------------QAEQLGTGHAVLQAASFLEGKKGTTL----VISGDTPLLttETLNNLFEYHqGKNASATI 128
Cdd:cd02541 80 TDLleevriisdlanihyvrQKEPLGLGHAVLCAKPFIGDEPFAVLlgddLIDSKEPCL--KQLIEAYEKT-GASVIAVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 129 LTAqAENPTGYGRI----IRDHIGIVEKIVE---QKDATPEEALVqeintGTYCFDNEaLFDALSKVGTnNAQGEYYLTD 201
Cdd:cd02541 157 EVP-PEDVSKYGIVkgekIDGDVFKVKGLVEkpkPEEAPSNLAIV-----GRYVLTPD-IFDILENTKP-GKGGEIQLTD 228
|
250
....*....|....*...
gi 488216138 202 IIEILKEEGhTVAAYQTD 219
Cdd:cd02541 229 AIAKLLEEE-PVYAYVFE 245
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
269-345 |
9.95e-09 |
|
eIF-2B epsilon subunit, central 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 epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 51.81 E-value: 9.95e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216138 269 IGPDTLIEAGVQIQgNTVIGSDCVIGSHSKIVDSRIEDHVVIE-NSVIESSHVKKHADVGPYAHLRPKAEIGENVHIG 345
Cdd:cd05787 2 IGRGTSIGEGTTIK-NSVIGRNCKIGKNVVIDNSYIWDDVTIEdGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIG 78
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
263-434 |
1.02e-08 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 55.80 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 263 IDAGVEIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKIVdsriEDHVVIENSVIESSHVKKHADvGPYAHLrpkaEIGENV 342
Cdd:PRK12461 14 LGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIG----KNNKIHQGAVVGDEPQDFTYK-GEESRL----EIGDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 343 HIGNFVevknaQIGKGTKVGHLTYVGDATL-------GEEINVGCGVVFVNY---DGknkhHTTVGDHSFIGSSTNIIGP 412
Cdd:PRK12461 85 VIREGV-----TIHRGTKGGGVTRIGNDNLlmayshvAHDCQIGNNVILVNGallAG----HVTVGDRAIISGNCLVHQF 155
|
170 180
....*....|....*....|..
gi 488216138 413 VEVAKNSSIAAGSTITDNIPEY 434
Cdd:PRK12461 156 CRIGALAMMAGGSRISKDVPPY 177
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-215 |
4.39e-08 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 54.29 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 1 MDARYAIILAAGKGTRM---KSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITI-VGHGAEQVKAQLGERS------KY 70
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLypvTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIsTPQDTPRFQQLLGDGSqwglnlQY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 71 ALQAEQLGTGHAVLQAASFLeGKKGTTLVIsGDTpLLTTETLNNLFEYHQGKNASATILTAQAENPTGYGRIIRDHIGIV 150
Cdd:PRK15480 81 KVQPSPDGLAQAFIIGEEFI-GGDDCALVL-GDN-IFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216138 151 EKIVEQkdatPEEALVQEINTGTYCFDNEALfdALSKVGTNNAQGEYYLTDIIEILKEEGHTVAA 215
Cdd:PRK15480 158 ISLEEK----PLQPKSNYAVTGLYFYDNDVV--EMAKNLKPSARGELEITDINRIYMEQGRLSVA 216
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
6-219 |
8.37e-08 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 53.50 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRM--------KSKLykvlhPVSGKPMVEHIINRVSETKPDEVITIVGHG----------AEQVKAQLGER 67
Cdd:COG1210 6 AVIPVAGLGTRFlpatkaipKEML-----PIVDKPLIQYVVEEAVAAGIEEIIFVTGRGkraiedhfdrSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 68 SKYAL-----------------QAEQLGTGHAVLQAASFLegKKGTTLVISGD------TPLLttETLNNLFEYHQGkna 124
Cdd:COG1210 81 GKEELleevrsisplanihyvrQKEPLGLGHAVLCARPFV--GDEPFAVLLGDdlidseKPCL--KQMIEVYEETGG--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 125 saTILTAQ---AENPTGYGRI----IRDHIGIVEKIVEqKDAtPEEALVQEINTGTYCFDNEaLFDALSKVGTnNAQGEY 197
Cdd:COG1210 154 --SVIAVQevpPEEVSKYGIVdgeeIEGGVYRVTGLVE-KPA-PEEAPSNLAIVGRYILTPE-IFDILEKTKP-GAGGEI 227
|
250 260
....*....|....*....|..
gi 488216138 198 YLTDIIEILKEEgHTVAAYQTD 219
Cdd:COG1210 228 QLTDAIAALAKE-EPVYAYEFE 248
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
262-346 |
1.13e-07 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 49.16 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 262 YIDAGVEIGPDTLIeagvqiqGNTVIGSDCVIGSHSKIVDSRIEDHVVI-ENSVIESSHVKKHADVGPYAHLRPKAEIGE 340
Cdd:cd03356 1 LIGESTVIGENAII-------KNSVIGDNVRIGDGVTITNSILMDNVTIgANSVIVDSIIGDNAVIGENVRVVNLCIIGD 73
|
....*.
gi 488216138 341 NVHIGN 346
Cdd:cd03356 74 DVVVED 79
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
78-427 |
1.21e-07 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 53.71 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 78 GTGHAVLQAASFLEGKKGTT----LVISGDTplLTTETLNNLFEYHQGKNASATI--LTAQAENPTGYGRIIRDHIGIVE 151
Cdd:PLN02241 102 GTADAVRQFLWLFEDAKNKNveevLILSGDH--LYRMDYMDFVQKHRESGADITIacLPVDESRASDFGLMKIDDTGRII 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 152 KIVE----------QKDAT-----PEEALVQEI--NTGTYCFDNEALFDALskvgtnnaqGEYYLT------DIIEILKE 208
Cdd:PLN02241 180 EFSEkpkgdelkamQVDTTvlglsPEEAKEKPYiaSMGIYVFKKDVLLKLL---------RWRFPTandfgsEIIPGAIK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 209 EGHTVAAYQTDDFEESMGV-----NDRIALAKaneimrkrinqmhMVNGVSFVDSA------------TTYIDAGVEigp 271
Cdd:PLN02241 251 EGYNVQAYLFDGYWEDIGTiksfyEANLALTK-------------QPPKFSFYDPDapiytsprflppSKIEDCRIT--- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 272 DTLIEAGVQIQGNTVIGSdcVIGshskiVDSRIEDHVVIENSVIE-SSHVKKHADV-GPYAHLRPKAEIGENVHIGNFVE 349
Cdd:PLN02241 315 DSIISHGCFLRECKIEHS--VVG-----LRSRIGEGVEIEDTVMMgADYYETEEEIaSLLAEGKVPIGIGENTKIRNAII 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216138 350 VKNAQIGKgtkvghltyvgdatlgeeinvgcGVVFVNYDGKNKHhtTVGDHSFIGSStniiGPVEVAKNSSIAAGSTI 427
Cdd:PLN02241 388 DKNARIGK-----------------------NVVIINKDGVQEA--DREEEGYYIRS----GIVVILKNAVIPDGTVI 436
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-163 |
3.35e-07 |
|
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: 50.71 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMK---SKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQVKAQLgERSKYALQ--------- 73
Cdd:cd02507 3 AVVLADGFGSRFLpltSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHL-LKSKWSSLsskmivdvi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 74 ----AEQLGTGHAVLQAASFLegkKGTTLVISGDT----PLLttETLNNLFEYHQGKNASATILTAQAENPTGYGR--II 143
Cdd:cd02507 82 tsdlCESAGDALRLRDIRGLI---RSDFLLLSCDLvsniPLS--ELLEERRKKDKNAIATLTVLLASPPVSTEQSKktEE 156
|
170 180
....*....|....*....|
gi 488216138 144 RDHIGIVEKIVEQKDATPEE 163
Cdd:cd02507 157 EDVIAVDSKTQRLLLLHYEE 176
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-55 |
7.09e-07 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 50.13 E-value: 7.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488216138 1 MDARYAIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKP-DEVItIVGH 55
Cdd:PRK00155 1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRiDEII-VVVP 55
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
337-437 |
1.13e-06 |
|
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: 47.07 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 337 EIGENVHIGNFVEV---KNAQIGKGTKVGHLTYVGDATLGEEInvgcgVVFVNYDGKNKHHTTVGDHSFIGSSTNIIGPV 413
Cdd:cd04647 3 SIGDNVYIGPGCVIsagGGITIGDNVLIGPNVTIYDHNHDIDD-----PERPIEQGVTSAPIVIGDDVWIGANVVILPGV 77
|
90 100
....*....|....*....|....
gi 488216138 414 EVAKNSSIAAGSTITDNIPEYALA 437
Cdd:cd04647 78 TIGDGAVVGAGSVVTKDVPPNSIV 101
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
5-53 |
1.43e-06 |
|
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: 49.06 E-value: 1.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488216138 5 YAIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKP-DEVITIV 53
Cdd:cd02516 2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVV 51
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
7-55 |
1.62e-06 |
|
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: 48.97 E-value: 1.62e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488216138 7 IILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGH 55
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVP 49
|
|
| LbH_Dynactin_5 |
cd03359 |
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
269-361 |
1.97e-06 |
|
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100049 [Multi-domain] Cd Length: 161 Bit Score: 47.59 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 269 IGPDTLIEAGVQIQGN--TV-IGSDCVIGSHSKIVDS-------------RIEDHVVI-ENSVIESshvkkhADVGPYAH 331
Cdd:cd03359 24 LNGKTIIQSDVIIRGDlaTVsIGRYCILSEGCVIRPPfkkfskgvaffplHIGDYVFIgENCVVNA------AQIGSYVH 97
|
90 100 110
....*....|....*....|....*....|.
gi 488216138 332 lrpkaeIGENVHIGNFVEVK-NAQIGKGTKV 361
Cdd:cd03359 98 ------IGKNCVIGRRCIIKdCVKILDGTVV 122
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
6-185 |
2.25e-06 |
|
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: 48.44 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEHIINRVSETKP-DEVItIVGHGAEQVKAQLGERSKYALQ-----AEQLGT 79
Cdd:TIGR00453 2 AVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAiDEVV-VVVSPDDTEFFQKYLVARAVPKivaggDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 80 ghaVLQAASFLEGKKgTTLVISGDTPLLTTETLNNLFEyhQGKNASATILTAQAenptgygriiRDHIgiveKIVEQK-- 157
Cdd:TIGR00453 81 ---VRNGLKALKDAE-FVLVHDAARPFVPKELLDRLLE--ALRKAGAAILALPV----------ADTL----KRVEADgf 140
|
170 180
....*....|....*....|....*....
gi 488216138 158 -DATPEEALVQEINTgTYCFDNEALFDAL 185
Cdd:TIGR00453 141 vVETVDREGLWAAQT-PQAFRTELLKKAL 168
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
6-210 |
4.00e-06 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short 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 homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. 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.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 47.95 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMkSKLYKV----LHPVSGKPMVEHIINRVSETKPDEVITIVGHG-AEQVK------AQLGERSKYALQA 74
Cdd:cd02538 3 GIILAGGSGTRL-YPLTKVvskqLLPVYDKPMIYYPLSTLMLAGIREILIISTPEdLPLFKellgdgSDLGIRITYAVQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 75 EQLGTGHAVLQAASFLEGKKgtTLVISGDtpllttetlnNLFeYHQG----------KNASATILTAQAENPTGYGRIIR 144
Cdd:cd02538 82 KPGGLAQAFIIGEEFIGDDP--VCLILGD----------NIF-YGQGlspilqraaaQKEGATVFGYEVNDPERYGVVEF 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488216138 145 DHIGIVEKIVEQkdatPEEALVQEINTGTYCFDNEAlFDaLSKVGTNNAQGEYYLTDIIEILKEEG 210
Cdd:cd02538 149 DENGRVLSIEEK----PKKPKSNYAVTGLYFYDNDV-FE-IAKQLKPSARGELEITDVNNEYLEKG 208
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
269-344 |
7.06e-06 |
|
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: 44.11 E-value: 7.06e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216138 269 IGPDTLIEAGVQIQgNTVIGSDCVIGSHSKIVDSRIEDHVVIENSV-IESSHVKKHADVGPYAHLRpKAEIGENVHI 344
Cdd:cd04652 2 VGENTQVGEKTSIK-RSVIGANCKIGKRVKITNCVIMDNVTIEDGCtLENCIIGNGAVIGEKCKLK-DCLVGSGYRV 76
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
5-225 |
1.11e-05 |
|
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: 46.80 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 5 YAIILAAGKGTRM----KSKLYKVLHPV-SGKPMVEHIINRVSETKPDEVITIVGHGA--EQVKAQLGER-SKYALQAEQ 76
Cdd:cd02509 2 YPVILAGGSGTRLwplsRESYPKQFLKLfGDKSLLQQTLDRLKGLVPPDRILVVTNEEyrFLVREQLPEGlPEENIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 77 LG--TGHAVLQAASFLEGKKG--TTLVISGDtPLLTT-----ETLNNLFEYHQgKNASAT--ILTAQAEnpTGYGRI--- 142
Cdd:cd02509 82 EGrnTAPAIALAALYLAKRDPdaVLLVLPSD-HLIEDveaflKAVKKAVEAAE-EGYLVTfgIKPTRPE--TGYGYIeag 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 143 --IRDHIGIVEKIVEQKD-ATPEEALVQE---INTGTYCFDNEALFDALSKvgtnnaqgeyYLTDIIEILKEeghTVAAY 216
Cdd:cd02509 158 ekLGGGVYRVKRFVEKPDlETAKEYLESGnylWNSGIFLFRAKTFLEELKK----------HAPDIYEALEK---ALAAA 224
|
....*....
gi 488216138 217 QTDDFEESM 225
Cdd:cd02509 225 GTDDFLRLL 233
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
328-411 |
1.16e-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: 47.32 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 328 PYAHLRPKAEIGENVHIGNFVEV-KNAQIGKGTKVGHLTYVGD-ATLGEEINVGCGVVFVnydgknkHHTTVGDHSFIGS 405
Cdd:COG1044 101 PSAVIDPSAKIGEGVSIGPFAVIgAGVVIGDGVVIGPGVVIGDgVVIGDDCVLHPNVTIY-------ERCVIGDRVIIHS 173
|
....*.
gi 488216138 406 STnIIG 411
Cdd:COG1044 174 GA-VIG 178
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-163 |
1.92e-05 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 45.73 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRM---KSKLYKVLHPVSGKPMVEHIINRVSETKPDEVITIV---------GHGAEQVKAQLGERSKYALQ 73
Cdd:cd04198 3 AVILAGGGGSRLyplTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqaeisTYLRSFPLNLKQKLDEVTIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 74 -AEQLGTGhAVLQAasFLEGKKGTTLVISGDtpLLTTETLNNLFEYHQGKNASATILTAQA--ENPTGYGRII------R 144
Cdd:cd04198 83 lDEDMGTA-DSLRH--IRKKIKKDFLVLSCD--LITDLPLIELVDLHRSHDASLTVLLYPPpvSSEQKGGKGKskkadeR 157
|
170
....*....|....*....
gi 488216138 145 DHIGIVEKIVEQKDATPEE 163
Cdd:cd04198 158 DVIGLDEKTQRLLFITSEE 176
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
353-428 |
2.80e-05 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 42.24 E-value: 2.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216138 353 AQIGKGTKVGHLTYVGD-ATLGEEINVGCGVVFVNYDGKN-KHHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTIT 428
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGPNeKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
98-427 |
4.29e-05 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 45.65 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 98 LVISGDTplLTTETLNNLFEYHQGKNASATI--LTAQAENPTGYGRIIRDHIGIVEKIVE---------------QKDAT 160
Cdd:PRK02862 120 LILSGDQ--LYRMDYRLFVQHHRETGADITLavLPVDEKDASGFGLMKTDDDGRITEFSEkpkgdelkamavdtsRLGLS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 161 PEEALVQEI--NTGTYCFDNEALFDALSKVGTNNAQGEyyltdiiEILKE--EGHTVAAYQTDDFEESMGVndrI-ALAK 235
Cdd:PRK02862 198 PEEAKGKPYlaSMGIYVFSRDVLFDLLNKNPEYTDFGK-------EIIPEaiRDYKVQSYLFDGYWEDIGT---IeAFYE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 236 ANEIMRKRINQmhmvnGVSFVDSA------------TTYIDAGVEigpDTLIEAGVQIQgNTVIgSDCVIGshskiVDSR 303
Cdd:PRK02862 268 ANLALTQQPNP-----PFSFYDEKapiytrarylppSKLLDATIT---ESIIAEGCIIK-NCSI-HHSVLG-----IRSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 304 IEDHVVIENSVI------ESSHVKKHADVGPyahlRPKAEIGENVHIGNFVEVKNAQIGKGTKVghltyvgdatlgeein 377
Cdd:PRK02862 333 IESGCTIEDTLVmgadfyESSEEREELRKEG----KPPLGIGEGTTIKRAIIDKNARIGNNVRI---------------- 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 488216138 378 vgcgvvfvnydgKNKHHTTVGDHSFIGSStniI--GPVEVAKNSSIAAGSTI 427
Cdd:PRK02862 393 ------------VNKDNVEEADREDQGFY---IrdGIVVVVKNAVIPDGTVI 429
|
|
| lacA |
PRK09527 |
galactoside O-acetyltransferase; Reviewed |
324-453 |
4.80e-05 |
|
galactoside O-acetyltransferase; Reviewed
Pssm-ID: 181930 [Multi-domain] Cd Length: 203 Bit Score: 44.22 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 324 ADVGPYAHLRPKAEI--GENVHIG-NFVEVKNaqigkgtkvghLTYVGD--ATLGEEINVGCGVVfVNYDGKNKHHT--- 395
Cdd:PRK09527 56 ATVGENAWVEPPVYFsyGSNIHIGrNFYANFN-----------LTIVDDytVTIGDNVLIAPNVT-LSVTGHPVHHElrk 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488216138 396 ---------TVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALA-------IARARQVNKEGYAKKL 453
Cdd:PRK09527 124 ngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAagvpcrvIREINDRDKQYYFKDY 197
|
|
| PLN02694 |
PLN02694 |
serine O-acetyltransferase |
353-451 |
5.76e-05 |
|
serine O-acetyltransferase
Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 45.02 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 353 AQIGKGTKVGHLTYVgdaTLGEEINVGCGVVF---VNYDGKNK----HHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGS 425
Cdd:PLN02694 167 AKIGKGILFDHATGV---VIGETAVIGNNVSIlhhVTLGGTGKacgdRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGS 243
|
90 100
....*....|....*....|....*...
gi 488216138 426 TITDNIPEYALAIAR-ARQV-NKEGYAK 451
Cdd:PLN02694 244 VVLIDVPPRTTAVGNpARLVgGKEKPAK 271
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
6-127 |
6.92e-05 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 43.64 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRM--KSKLykvLHPVSGKPMVEHIINRVsetKP--DEVItIVghgaeqVKAQLGERSKYALQ------AE 75
Cdd:PRK00317 6 GVILAGGRSRRMggVDKG---LQELNGKPLIQHVIERL---APqvDEIV-IN------ANRNLARYAAFGLPvipdslAD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488216138 76 QLG--TG-HAVLQAASFlegkkGTTLVISGDTPLLTTETLNNLFEYHQGKNASAT 127
Cdd:PRK00317 73 FPGplAGiLAGLKQART-----EWVLVVPCDTPFIPPDLVARLAQAAGKDDADVA 122
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
268-444 |
9.08e-05 |
|
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: 42.40 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 268 EIGPDTLIEAGVQIQGNTVIGSDCVIGshskivdsrieDHVVIEnsviesshvkkhADVGPyahlrpkAEIGENVHIGNF 347
Cdd:cd04645 1 EIDPSAFIAPNATVIGDVTLGEGSSVW-----------FGAVLR------------GDVNP-------IRIGERTNIQDG 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 348 VevknaqigkgtkVGHLTYVGDATLGEEINVGCGVVFvnydgknkHHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTI 427
Cdd:cd04645 51 S------------VLHVDPGYPTIIGDNVTVGHGAVL--------HGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLV 110
|
170 180
....*....|....*....|
gi 488216138 428 TDN--IPEYALAIAR-ARQV 444
Cdd:cd04645 111 PPGkvIPPGSLVAGSpAKVV 130
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
4-50 |
9.08e-05 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 44.04 E-value: 9.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488216138 4 RYAIILAAgkgtRMKS-KLY-KVLHPVSGKPMVEHIINRVSETK-PDEVI 50
Cdd:COG1861 3 KIVAIIQA----RMGStRLPgKVLKPLGGKPVLEHVIERLKRSKlIDEVV 48
|
|
| LicC |
COG4750 |
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ... |
6-59 |
1.26e-04 |
|
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 443784 [Multi-domain] Cd Length: 228 Bit Score: 43.28 E-value: 1.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488216138 6 AIILAAGKGTRMKSKLY---KVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAEQ 59
Cdd:COG4750 3 AIILAAGLGSRFAPITYetpKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQ 59
|
|
| PLN02739 |
PLN02739 |
serine acetyltransferase |
353-436 |
1.51e-04 |
|
serine acetyltransferase
Pssm-ID: 215394 [Multi-domain] Cd Length: 355 Bit Score: 43.87 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 353 AQIGKGTKVGHLTYVgdaTLGEEINVGCGVVF---VNYDGKNKH----HTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGS 425
Cdd:PLN02739 212 ARIGKGILLDHGTGV---VIGETAVIGDRVSIlhgVTLGGTGKEtgdrHPKIGDGALLGACVTILGNISIGAGAMVAAGS 288
|
90
....*....|.
gi 488216138 426 TITDNIPEYAL 436
Cdd:PLN02739 289 LVLKDVPSHSM 299
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
255-341 |
2.15e-04 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 43.28 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 255 FVDSattyiDAGVEIGPDTLIEAGVQIQG----NTVIGSDCVIGSHSKIVDSRIEDHVVI-ENSVIESSHVKKHADVGPy 329
Cdd:PRK00844 303 FVDG-----GGRVGSAQDSLVSAGSIISGatvrNSVLSPNVVVESGAEVEDSVLMDGVRIgRGAVVRRAILDKNVVVPP- 376
|
90
....*....|..
gi 488216138 330 ahlrpKAEIGEN 341
Cdd:PRK00844 377 -----GATIGVD 383
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
266-362 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 266 GVEIGPDTLIEAGVQIQ--GNTVIGSDCVIGSHSKIVDSrieDHVVIENSVIESSHVKKhADVgpyahlrpkaEIGENVH 343
Cdd:cd04647 1 NISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDH---NHDIDDPERPIEQGVTS-API----------VIGDDVW 66
|
90 100
....*....|....*....|
gi 488216138 344 IG-NFVEVKNAQIGKGTKVG 362
Cdd:cd04647 67 IGaNVVILPGVTIGDGAVVG 86
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
272-346 |
2.54e-04 |
|
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: 40.14 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 272 DTLIEAGVQIQG----NTVIGSDCVIGSHSKIVDSRIEDHVVI-ENSVIESSHVKKHadvgpyahlrpkAEIGENVHIGN 346
Cdd:cd04651 12 NSLVSEGCIISGgtveNSVLFRGVRVGSGSVVEDSVIMPNVGIgRNAVIRRAIIDKN------------VVIPDGVVIGG 79
|
|
| PRK09677 |
PRK09677 |
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional |
333-446 |
2.84e-04 |
|
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
Pssm-ID: 137467 [Multi-domain] Cd Length: 192 Bit Score: 41.78 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 333 RPKAEIGENVHIGNFVEVKNAQ---IGKGTKVGHLTYVGD---ATLGEEINVGCGVVFVNYDGKNKHHTTVGDHSFIGSS 406
Cdd:PRK09677 63 RGKLFFGDNVQVNDYVHIACIEsitIGRDTLIASKVFITDhnhGSFKHSDDFSSPNLPPDMRTLESSAVVIGQRVWIGEN 142
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488216138 407 TNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQVNK 446
Cdd:PRK09677 143 VTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
266-295 |
3.21e-04 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 37.70 E-value: 3.21e-04
10 20 30
....*....|....*....|....*....|
gi 488216138 266 GVEIGPDTLIEAGVQIQGNTVIGSDCVIGS 295
Cdd:pfam00132 1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
317-409 |
4.65e-04 |
|
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: 41.24 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 317 SSHVKKHADVGPYAHLRPKAEIGENVHIGNFVEV-KNAQIGKGTKVG-HLTYVGDATLGEEINVGCGVV-------FVNY 387
Cdd:cd03352 1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHpNVTIYEGCIIGDRVIIHSGAVigsdgfgFAPD 80
|
90 100
....*....|....*....|....*..
gi 488216138 388 DGKNK--HHT---TVGDHSFIGSSTNI 409
Cdd:cd03352 81 GGGWVkiPQLggvIIGDDVEIGANTTI 107
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
6-117 |
5.45e-04 |
|
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: 41.28 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 6 AIILAAGKGTRMKSKLYKVLHPVSGKPMVEH-------------IINRVSETKPDEVITIVGHGAEQVKAQLGERSkyal 72
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHtvdaflaspvvdrIVVAVSPDDTPEFRQLLGDPSIQLVAGGDTRQ---- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488216138 73 qaeqlgtgHAVLQAASFLEGKKGTTLVISGDTPLLTTETLNNLFE 117
Cdd:pfam01128 77 --------DSVLNGLKALAGTAKFVLVHDGARPCLPHADLARLLA 113
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
1-58 |
5.46e-04 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 42.05 E-value: 5.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488216138 1 MDARYAIILAAGKGTRMKSKlYKVLHPVSGKPMVEHIINRVSETKPDEVITIVGHGAE 58
Cdd:PRK14489 3 ISQIAGVILAGGLSRRMNGR-DKALILLGGKPLIERVVDRLRPQFARIHLNINRDPAR 59
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
268-444 |
5.84e-04 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 40.40 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 268 EIGPDTLIEAGVQIQGNTVIGSDCVIGSHSKI---VDS-RIEDHVVI-ENSVIessHVKKHADVgpyahlrpkaEIGENV 342
Cdd:COG0663 12 QIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLrgdVGPiRIGEGSNIqDGVVL---HVDPGYPL----------TIGDDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 343 HIGNfvevkNAQIgkgtkvgHltyvgdatlgeeinvGCgvvfvnydgknkhhtTVGDHSFIGSSTNIIGPVEVAKNSSIA 422
Cdd:COG0663 79 TIGH-----GAIL-------H---------------GC---------------TIGDNVLIGMGAIVLDGAVIGDGSIVG 116
|
170 180
....*....|....*....|....*
gi 488216138 423 AGSTITDN--IPEYALAIAR-ARQV 444
Cdd:COG0663 117 AGALVTEGkvVPPGSLVVGSpAKVV 141
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
6-41 |
9.58e-04 |
|
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 274249 Cd Length: 186 Bit Score: 39.96 E-value: 9.58e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488216138 6 AIILAAGKGTRMKSKlYKVLHPVSGKPMVEHIINRV 41
Cdd:TIGR02665 3 GVILAGGRARRMGGR-DKGLVELGGKPLIEHVLARL 37
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
293-409 |
1.28e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 41.01 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 293 IGSHSKIVDSRIEDHVVIENSVIESShvkkhadvgpyahlrpkaeIGENVHIGNFVEVKNAQIGKGTKVGHLTYVGDATL 372
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVVYGTVEHSV-------------------LFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAII 345
|
90 100 110
....*....|....*....|....*....|....*..
gi 488216138 373 GEEINVGCGVVFvnyDGKNKHHTTVGDHSFIGSSTNI 409
Cdd:PRK05293 346 GENAVIGDGVII---GGGKEVITVIGENEVIGVGTVI 379
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
241-330 |
1.40e-03 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 39.08 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 241 RKRINQMHMVNGVSFVDSATTYIDAGVEIGPDTLIEAGVQI----------------QGNTVIGSDCVIGSHSKIVD-SR 303
Cdd:COG0110 22 RIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDDVWIGAGATILPgVT 101
|
90 100
....*....|....*....|....*...
gi 488216138 304 IEDHVVIE-NSViesshVKKhaDVGPYA 330
Cdd:COG0110 102 IGDGAVVGaGSV-----VTK--DVPPYA 122
|
|
| LbH_gamma_CA |
cd00710 |
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
258-363 |
1.94e-03 |
|
Gamma carbonic anhydrases (CA): Carbonic anhydrases 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 distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.
Pssm-ID: 100039 [Multi-domain] Cd Length: 167 Bit Score: 39.15 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 258 SATTYIDAGVEIGPDTLIEAGVQIQGNTVIGSD----CVIGShskivDSRIEDHVVIensviessHVKKHADV--GPYAH 331
Cdd:cd00710 6 DPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADegtpIIIGA-----NVNIQDGVVI--------HALEGYSVwiGKNVS 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 488216138 332 LRPKA------EIGENVHIGNFVEVKNAQIGKGTKVGH 363
Cdd:cd00710 73 IAHGAivhgpaYIGDNCFIGFRSVVFNAKVGDNCVIGH 110
|
|
| PLN02296 |
PLN02296 |
carbonate dehydratase |
307-432 |
2.72e-03 |
|
carbonate dehydratase
Pssm-ID: 215167 [Multi-domain] Cd Length: 269 Bit Score: 39.34 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 307 HVVIENSVIESSHVKKHADVGPYAHLRPKAEIGENVHI--GNFV--EVKNAQIGKGTKVGHLTYVGDA-----------T 371
Cdd:PLN02296 42 HRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIwyGCVLrgDVNSISVGSGTNIQDNSLVHVAktnlsgkvlptI 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488216138 372 LGEEINVGCGVVFvnydgknkHHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDN--IP 432
Cdd:PLN02296 122 IGDNVTIGHSAVL--------HGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIP 176
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
6-50 |
3.79e-03 |
|
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.
Pssm-ID: 133011 Cd Length: 233 Bit Score: 38.71 E-value: 3.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488216138 6 AIILAagkgtRMKSKLY--KVLHPVSGKPMVEHIINRVSETKP-DEVI 50
Cdd:cd02518 2 AIIQA-----RMGSTRLpgKVLKPLGGKPLLEHLLDRLKRSKLiDEIV 44
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
78-368 |
3.93e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 39.47 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 78 GTGHAVLQAASFLEGKKGT-TLVISGDTplLTTETLNNLFEYHQGKNASATIltAQAENP----TGYGRIIRDHIG-IVE 151
Cdd:PRK05293 100 GTAHAIYQNIDYIDQYDPEyVLILSGDH--IYKMDYDKMLDYHKEKEADVTI--AVIEVPweeaSRFGIMNTDENMrIVE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 152 kiVEQKDATPEEALVqeiNTGTYCFDNEALFDALSKVGTNNAQGEYYLTDIIEILKEEGHTVAAYQTDDFEESMGVNDri 231
Cdd:PRK05293 176 --FEEKPKNPKSNLA---SMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGEKLYAYPFKGYWKDVGTIE-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 232 ALAKANEIMRKRINQMHM------VNGVSFVDSATtYIDAGVEIgPDTLIEAGVQIQG---NTVIGSDCVIGSHSKIVDS 302
Cdd:PRK05293 249 SLWEANMELLRPENPLNLfdrnwrIYSVNPNLPPQ-YIAENAKV-KNSLVVEGCVVYGtveHSVLFQGVQVGEGSVVKDS 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488216138 303 RIEDHVVI-ENSVIEsshvkkhadvgpyahlrpKAEIGENVHIGNFVEV---KNAQ--IGKGTKVGHLTYVG 368
Cdd:PRK05293 327 VIMPGAKIgENVVIE------------------RAIIGENAVIGDGVIIgggKEVItvIGENEVIGVGTVIG 380
|
|
| LbH_Dynactin_5 |
cd03359 |
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
281-369 |
5.12e-03 |
|
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100049 [Multi-domain] Cd Length: 161 Bit Score: 37.58 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216138 281 IQGNTVIGSDCVIgsHSKIVDSRIEDHVVI-ENSVIESShVKKHADVGPYAHLRpkaeIGENVHIGNFVEVKNAQIG--- 356
Cdd:cd03359 24 LNGKTIIQSDVII--RGDLATVSIGRYCILsEGCVIRPP-FKKFSKGVAFFPLH----IGDYVFIGENCVVNAAQIGsyv 96
|
90
....*....|....*.
gi 488216138 357 ---KGTKVGHLTYVGD 369
Cdd:cd03359 97 higKNCVIGRRCIIKD 112
|
|
| PRK10191 |
PRK10191 |
putative acyl transferase; Provisional |
373-444 |
5.24e-03 |
|
putative acyl transferase; Provisional
Pssm-ID: 182295 [Multi-domain] Cd Length: 146 Bit Score: 37.56 E-value: 5.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488216138 373 GEEINVGCGVVFVNYDGKNKHHTTVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALAIARARQV 444
Cdd:PRK10191 71 GDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
|
|
| LbH_MAT_GAT |
cd03357 |
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
396-437 |
7.37e-03 |
|
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100047 [Multi-domain] Cd Length: 169 Bit Score: 37.40 E-value: 7.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488216138 396 TVGDHSFIGSSTNIIGPVEVAKNSSIAAGSTITDNIPEYALA 437
Cdd:cd03357 120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVA 161
|
|
| |
