|
Name |
Accession |
Description |
Interval |
E-value |
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
8-462 |
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: 746.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwpDVEVALQPERNGTGG 87
Cdd:COG1207 4 AVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL--DVEFVLQEEQLGTGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 88 AVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHKDATE 166
Cdd:COG1207 82 AVQQALPALPGDDGTVLVLYGDVPLIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDgRVLRIVEEKDATE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 167 EELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAMNAEVN 246
Cdd:COG1207 162 EQRAIREINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADGLKVAAVQPEDPWEVLGVNDRVQLAEAERILQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 247 RRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIRTHGELAVIG 326
Cdd:COG1207 242 RRIAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSVIEDAVVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 327 ENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGDEV 406
Cdd:COG1207 322 AGATVGPFARLRPGTVLGEGVKIGNFVEVKNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDGA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 567338369 407 FIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRTRPGS 462
Cdd:COG1207 402 FIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIEGWVRPKKKKK 457
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-478 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 693.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 7 SAVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDWPDVEVALQPERNGTG 86
Cdd:PRK14352 5 TAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEVDIAVQDEQPGTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 87 GAVQCGITSLGDA-TGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHKDA 164
Cdd:PRK14352 85 HAVQCALEALPADfDGTVVVTAGDVPLLDGETLADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQDgEVTAIVEQKDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 165 TEEELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAMNAE 244
Cdd:PRK14352 165 TPSQRAIREVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAIAREAGHRVGAHHADDSAEVAGVNDRVQLAALGAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 245 VNRRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIRTHGELAV 324
Cdd:PRK14352 245 LNRRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVRTHGSESE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 325 IGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGD 404
Cdd:PRK14352 325 IGAGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVNKHRTTIGS 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567338369 405 EVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRTRPGSKAAKAAEKSTKTEKAD 478
Cdd:PRK14352 405 HVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSEGPQRNIEGWVQRKRPGTPAAEAAEAASEAAAQQ 478
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-457 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 587.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwpdVEVALQPERNGTGG 87
Cdd:PRK14354 4 YAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDR---SEFALQEEQLGTGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 88 AVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHKDATE 166
Cdd:PRK14354 81 AVMQAEEFLADKEGTTLVICGDTPLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENgEVEKIVEQKDATE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 167 EELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAMNAEVN 246
Cdd:PRK14354 161 EEKQIKEINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGEKVGAYQTEDFEESLGVNDRVALAEAEKVMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 247 RRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIRTHGELAVIG 326
Cdd:PRK14354 241 RRINEKHMVNGVTIIDPESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVDSTIGDGVTITNSVIEESKVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 327 ENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGDEV 406
Cdd:PRK14354 321 DNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVNYDGKNKFKTIIGDNA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 567338369 407 FIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPR 457
Cdd:PRK14354 401 FIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKEGYVKK 451
|
|
| glmU |
TIGR01173 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
8-460 |
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: 577.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwpDVEVALQPERNGTGG 87
Cdd:TIGR01173 2 SVVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALANR--DVNWVLQAEQLGTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 88 AVQCGITSLGDAtGEIIVTYGDVPMLDSDTLSDLVDAHRAqhNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHKDATE 166
Cdd:TIGR01173 80 AVLQALPFLSDD-GDVLVLYGDVPLISAETLERLLEAHRQ--NGITLLTAKLDDPTGYGRIIRENDgKVTAIVEDKDANA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 167 EELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAMNAEVN 246
Cdd:TIGR01173 157 EQKAIKEINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRAVQVDDSDEVLGVNDRLQLAQLERILQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 247 RRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHV-IRTHGELAVI 325
Cdd:TIGR01173 237 RRIAKKLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKVKIGDDVVIGPGCVIKNSVIGSNVVIkAYSVLEGSEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 326 GENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGDE 405
Cdd:TIGR01173 317 GEGCDVGPFARLRPGSVLGAGVHIGNFVEVKNARIGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHKTIIGDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 406 VFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRTRP 460
Cdd:TIGR01173 397 VFIGSNTQLVAPVKVGDGATIAAGSTVTKDVPEGALAISRARQRNIEGWVRPKKK 451
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-459 |
6.00e-171 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 488.22 E-value: 6.00e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 7 SAVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDWPDVEVALQPERNGTG 86
Cdd:PRK14353 6 CLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAEIFVQKERLGTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 87 GAVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDaHRAQHNAVTVLTARVPNPTGYGRVVRVGEEVAKIVEHKDATE 166
Cdd:PRK14353 86 HAVLAAREALAGGYGDVLVLYGDTPLITAETLARLRE-RLADGADVVVLGFRAADPTGYGRLIVKGGRLVAIVEEKDASD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 167 EELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDvWQTEGVNDRVQLAAMNAEVN 246
Cdd:PRK14353 165 EERAITLCNSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIARAEGLRVAVVEAPE-DEVRGINSRAELAEAEAVWQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 247 RRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTqllgatkiesdaVVGPDttlrdVEIGKGShVIR--THGELAV 324
Cdd:PRK14353 244 ARRRRAAMLAGVTLIAPETVFFSYDTVIGRDVVIEPNV------------VFGPG-----VTVASGA-VIHafSHLEGAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 325 IGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGD 404
Cdd:PRK14353 306 VGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGAGANIGAGTITCNYDGFNKHRTEIGA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 405 EVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRTR 459
Cdd:PRK14353 386 GAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKPGWAKKLR 440
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-460 |
1.75e-162 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 467.30 E-value: 1.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 4 HQVSAVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwPDVEVALQPERN 83
Cdd:PRK14355 1 MNNLAAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGD-GDVSFALQEEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 84 GTGGAVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHK 162
Cdd:PRK14355 80 GTGHAVACAAPALDGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADgRVLRIVEEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 163 DATEEELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAMN 242
Cdd:PRK14355 160 DATPEERSIREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAAEGLRCLAFPVADPDEIMGVNDRAQLAEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 243 AEVNRRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGkgSHVIRTHG-- 320
Cdd:PRK14355 240 RVLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIG--DDVTVKAGsv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 321 -ELAVIGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSK 399
Cdd:PRK14355 318 lEDSVVGDDVAIGPMAHLRPGTELSAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567338369 400 TTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRTRP 460
Cdd:PRK14355 398 TVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKEGWKLRKKD 458
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-458 |
4.65e-162 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 465.94 E-value: 4.65e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKdWPDVEVALQPERNGTGG 87
Cdd:PRK14360 3 AVAILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAH-LPGLEFVEQQPQLGTGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 88 AVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHKDATE 166
Cdd:PRK14360 82 AVQQLLPVLKGFEGDLLVLNGDVPLLRPETLEALLNTHRSSNADVTLLTARLPNPKGYGRVFCDGNnLVEQIVEDRDCTP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 167 EELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIgyarSQGKRVGALVTDDVWQTEGVNDRVQLAAMNAEVN 246
Cdd:PRK14360 162 AQRQNNRINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTV----SLLDPVMAVEVEDYQEINGINDRKQLAQCEEILQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 247 RRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIRTHGELAVIG 326
Cdd:PRK14360 238 NRIKEKWMLAGVTFIDPASCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIENSQIGENVTVLYSVVSDSQIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 327 ENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGDEV 406
Cdd:PRK14360 318 DGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDGVKKHRTVIGDRS 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 567338369 407 FIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRT 458
Cdd:PRK14360 398 KTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKENWKKKS 449
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
9-464 |
1.54e-158 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 456.92 E-value: 1.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSpQHLVVVVGHLREQVEEILSKDwpdVEVALQPERNGTGGA 88
Cdd:PRK14357 3 ALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEW---VKIFLQEEQLGTAHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 89 VQCGITSLgDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGEEVaKIVEHKDATEEE 168
Cdd:PRK14357 79 VMCARDFI-EPGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKY-RIVEDKDAPEEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 169 LKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYArsqgKRVGALVTDDVWQTEGVNDRVQLAAMNAEVNRR 248
Cdd:PRK14357 157 KKIKEINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAVNFA----EKVRVVKTEDLLEITGVNTRIQLAWLEKQLRMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 249 ICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIRTHGELAVIGEN 328
Cdd:PRK14357 233 ILEELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKIIRSECEKSVIEDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 329 CEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGDEVFI 408
Cdd:PRK14357 313 VSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTFIEDGAFI 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 567338369 409 GSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPRTRPGSKA 464
Cdd:PRK14357 393 GSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWVLKKRKEEEN 448
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
9-457 |
6.90e-145 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 423.24 E-value: 6.90e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKdwPDVEVALQPERNGTGGA 88
Cdd:PRK14358 10 VVILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQG--SGVAFARQEQQLGTGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 89 VQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVR-VGEEVAKIVEHKDATEE 167
Cdd:PRK14358 88 FLSGASALTEGDADILVLYGDTPLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRgADGAVERIVEQKDATDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 168 ELKIDEINSGIYVFD--AVTLRDGLGSlkaDNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAMNAEV 245
Cdd:PRK14358 168 EKAIGEFNSGVYVFDarAPELARRIGN---DNKAGEYYLTDLLGLYRAGGAQVRAFKLSDPDEVLGANDRAGLAQLEATL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 246 NRRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGShVIRTHG--ELA 323
Cdd:PRK14358 245 RRRINEAHMKAGVTLQDPGTILIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSVLHEGA-VIKPHSvlEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 324 VIGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLG 403
Cdd:PRK14358 324 EVGAGSDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNKHQSKVG 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 567338369 404 DEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWVPR 457
Cdd:PRK14358 404 AGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNLEGWSRR 457
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-463 |
8.14e-142 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 414.42 E-value: 8.14e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 1 MQDHQVSAVIvLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwpDVEVALQP 80
Cdd:PRK09451 1 MLNSAMSVVI-LAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADE--PLNWVLQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 81 ERNGTGGAVQCGITSLGDATgEIIVTYGDVPMLDSDTLSDLVDAHRAqhNAVTVLTARVPNPTGYGRVVRVGEEVAKIVE 160
Cdd:PRK09451 78 EQLGTGHAMQQAAPFFADDE-DILMLYGDVPLISVETLQRLRDAKPQ--GGIGLLTVKLDNPTGYGRITRENGKVVGIVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 161 HKDATEEELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAA 240
Cdd:PRK09451 155 QKDATDEQRQIQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGREIVAVHPQRLSEVEGVNNRLQLAR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 241 MNAEVNRRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGShVIRTHG 320
Cdd:PRK09451 235 LERVYQAEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCVIGDDC-EISPYS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 321 --ELAVIGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKS 398
Cdd:PRK09451 314 vvEDANLGAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 399 KTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEGWvprTRPGSK 463
Cdd:PRK09451 394 KTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGW---QRPVKK 455
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-448 |
4.55e-129 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 382.15 E-value: 4.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 5 QVSAVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKdwPDVEVALQPERNG 84
Cdd:PRK14356 4 STTGALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPD--EDARFVLQEQQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 85 TGGAVQCGITSLGDATGE-IIVTYGDVPMLDSDTLSDLVDAhrAQHNAVTVLTARVPNPTGYGRVVRVGEEVAKIVEHKD 163
Cdd:PRK14356 82 TGHALQCAWPSLTAAGLDrVLVVNGDTPLVTTDTIDDFLKE--AAGADLAFMTLTLPDPGAYGRVVRRNGHVAAIVEAKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 164 ATEEEL--KIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQLAAM 241
Cdd:PRK14356 160 YDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAVAEGMNVLGVNCGEDPNLLGVNTPAELVRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 242 NAEVNRRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIR-THG 320
Cdd:PRK14356 240 EELLRARIVEKHLESGVLIHAPESVRIGPRATIEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVVSSGATIHSfSHL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 321 ELAVIGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKT 400
Cdd:PRK14356 320 EGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNKHRT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 567338369 401 TLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSRE 448
Cdd:PRK14356 400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQ 447
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
9-453 |
7.48e-125 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 370.47 E-value: 7.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQhLVVVVGHLREQVEEILSKDWPDVEVALQPERN--GTG 86
Cdd:PRK14359 5 IIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAISDD-VHVVLHHQKERIKEAVLEYFPGVIFHTQDLENypGTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 87 GAVQcGITSLGDatgEIIVTYGDVPMLDSDTLSDLVDAHrAQHNaVTVLTARvpNPTGYGRVVRVGEEVAKIVEHKDATE 166
Cdd:PRK14359 84 GALM-GIEPKHE---RVLILNGDMPLVEKDELEKLLEND-ADIV-MSVFHLA--DPKGYGRVVIENGQVKKIVEQKDANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 167 EELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVwQTEGVNDRVQLAamNAEV- 245
Cdd:PRK14359 156 EELKIKSVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAVFVDEE-NFMGVNSKFELA--KAEEi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 246 -NRRICERWMREGVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVvgpdttlrdveigKGSHVIrthgELAV 324
Cdd:PRK14359 233 mQERIKKNAMKQGVIMRLPETIYIESGVEFEGECELEEGVRILGKSKIENSHI-------------KAHSVI----EESI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 325 IgENCEVGPFSRLRPGTTLGNGgKIGSFVETKNAHIgEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGD 404
Cdd:PRK14359 296 I-ENSDVGPLAHIRPKSEIKNT-HIGNFVETKNAKL-NGVKAGHLSYLGDCEIDEGTNIGAGTITCNYDGKKKHKTIIGK 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 567338369 405 EVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGALGIARSREHVSEG 453
Cdd:PRK14359 373 NVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIKN 421
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
9-238 |
7.29e-111 |
|
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: 327.16 E-value: 7.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKdwPDVEVALQPERNGTGGA 88
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN--PNVEFVLQEEQLGTGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 89 VQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEHKDATEE 167
Cdd:cd02540 79 VKQALPALKDFEGDVLVLYGDVPLITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNgKVLRIVEEKDATEE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567338369 168 ELKIDEINSGIYVFDAVTLRDGLGSLKADNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQL 238
Cdd:cd02540 159 EKAIREVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVAAVLADDEEEVLGVNDRVQL 229
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
257-447 |
3.82e-102 |
|
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: 303.57 E-value: 3.82e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 257 GVTIVDPLTTWIETDVELSEDVTILPNTQLLGATKIESDAVVGPDTTLRDVEIGKGSHVIR-THGELAVIGENCEVGPFS 335
Cdd:cd03353 1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKAsSVIEGAVIGNGATVGPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 336 RLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFANYDGFNKSKTTLGDEVFIGSNSVLV 415
Cdd:cd03353 81 HLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDNVFIGSNSQLV 160
|
170 180 190
....*....|....*....|....*....|..
gi 567338369 416 APVTVGDGAFVAAGSAVTNDIPAGALGIARSR 447
Cdd:cd03353 161 APVTIGDGATIAAGSTITKDVPPGALAIARAR 192
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
10-432 |
1.60e-65 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 216.31 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 10 IVLAAGGGTRMK---SAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEIL---SKDWPDVEVALQPERN 83
Cdd:TIGR03992 4 VILAAGKGTRMRpltETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFgdgSRGGVPIEYVVQEEQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 84 GTGGAVQCGITSLgdaTGEIIVTYGDVpMLDSDTLSDLVDAHraqhnAVTVLTARVPNPTGYGRVVRVGEEVAKIVEhkd 163
Cdd:TIGR03992 84 GTADALGSAKEYV---DDEFLVLNGDV-LLDSDLLERLIRAE-----APAIAVVEVDDPSDYGVVETDGGRVTGIVE--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 164 aTEEELKIDEINSGIYVFDAvTLRDGLGSLKAdNAQGELYLTDVIGYARSQGKrVGALVTDDVWQTEGVNDRVqLAAMNA 243
Cdd:TIGR03992 152 -KPENPPSNLINAGIYLFSP-EIFELLEKTKL-SPRGEYELTDALQLLIDEGK-VKAVELDGFWLDVGRPWDL-LDANEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 244 EVNRRICErwmregvtivdplttwIETDVElsEDVTILPNTQLLGATKIESDAVV-GPdttlrdveigkgshvirthgel 322
Cdd:TIGR03992 227 LLDNLEPR----------------IEGTVE--ENVTIKGPVVIGEGAVIRSGTYIeGP---------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 323 AVIGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTIFAN--YD------- 393
Cdd:TIGR03992 267 VYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFGAGTKVANlrHDdkpvkvt 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 567338369 394 --------GFNKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAV 432
Cdd:TIGR03992 347 vkgkrvdtGRRKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
9-227 |
2.13e-37 |
|
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: 136.56 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMK---SAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEIL---SKDWPDVEVALQPER 82
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFgdgSKFGVNIEYVVQEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 83 NGTGGAVQCGITSLGDatGEIIVTYGDVpMLDSDtLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGE-EVAKIVEh 161
Cdd:cd04181 81 LGTAGAVRNAEDFLGD--DDFLVVNGDV-LTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDgRVTRFVE- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567338369 162 KDATEEelkIDEINSGIYVFDavtlRDGLGSLKADNAQGELYLTDVIGYARSQGKrVGALVTDDVW 227
Cdd:cd04181 156 KPTLPE---SNLANAGIYIFE----PEILDYIPEILPRGEDELTDAIPLLIEEGK-VYGYPVDGYW 213
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
9-228 |
1.78e-31 |
|
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: 121.03 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMK---SAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEIL--SKDWP-DVEVALQPER 82
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFgdGSRFGvRITYVDEGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 83 NGTGGAVQCGITSLGDATgeIIVTYGDVpMLDSDtLSDLVDAHRAQHNAVTVLTARVPNPTGYGrVVRVGEE--VAKIVE 160
Cdd:COG1208 82 LGTGGALKRALPLLGDEP--FLVLNGDI-LTDLD-LAALLAFHREKGADATLALVPVPDPSRYG-VVELDGDgrVTRFVE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567338369 161 HKDATEEELkideINSGIYVFDavtlRDGLGSLKADNAqgeLYLTDVIGYARSQGkRVGALVTDDVWQ 228
Cdd:COG1208 157 KPEEPPSNL----INAGIYVLE----PEIFDYIPEGEP---FDLEDLLPRLIAEG-RVYGYVHDGYWL 212
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
291-433 |
2.95e-28 |
|
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: 109.60 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 291 KIESDAVVGPDTTLR-DVEIGKGShVIRTHGEL---AVIGENCEVGPFSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKV 366
Cdd:cd05636 1 KDEIEGTVEEGVTIKgPVWIGEGA-IVRSGAYIegpVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 367 PHLTYCGDANIGSGVNIGAGTIFANY-----------------DGFNKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAG 429
Cdd:cd05636 80 PHLNYVGDSVLGENVNLGAGTITANLrfddkpvkvrlkgervdTGRRKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPG 159
|
....
gi 567338369 430 SAVT 433
Cdd:cd05636 160 CVVR 163
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
10-227 |
9.04e-23 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 97.85 E-value: 9.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 10 IVLAAGGGTRMK---SAKSK-LLHeVAGRPMLSYAVSAAKALSPQHLVVVVG-HLREQVEEILsKDWPD----VEVALQP 80
Cdd:COG1209 4 IILAGGSGTRLRpltLTVSKqLLP-VYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLL-GDGSQlgikISYAVQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 81 ERNGTGGAVQCGITSLGDAtgEIIVTYGDVpMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGrVVRVGEE--VAKI 158
Cdd:COG1209 82 EPLGLAHAFIIAEDFIGGD--PVALVLGDN-IFYGDGLSELLREAAARESGATIFGYKVEDPERYG-VVEFDEDgrVVSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 159 VEhkdateeelKIDEINS-----GIYVFDAvTLRDGLGSLKAdNAQGELYLTDVIGYARSQGKRVGA-LVTDDVW 227
Cdd:COG1209 158 EE---------KPKEPKSnlavtGLYFYDN-DVVEIAKNLKP-SARGELEITDANQAYLERGKLVVElLGRGFAW 221
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
8-134 |
2.97e-22 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 94.07 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSakSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKdwPDVEVALQPE-RNGTG 86
Cdd:COG2068 5 AAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG--LGVRVVVNPDwEEGMS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 567338369 87 GAVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTV 134
Cdd:COG2068 81 SSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVA 128
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
8-147 |
4.75e-21 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 90.31 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSakSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDWPDVEVALQPERnGTGG 87
Cdd:cd04182 2 AAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE-GMSS 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567338369 88 AVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTA--RVPNPTGYGR 147
Cdd:cd04182 79 SLAAGLEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYqgRRGHPVLFPR 140
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
9-181 |
2.17e-20 |
|
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: 89.53 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKS---KLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDWP---DVEVALQPER 82
Cdd:cd06915 1 AVILAGGLGTRLRSVVKdlpKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRggiRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 83 NGTGGAVQCGITSLGDAtgEIIVTYGDVpMLDSDtLSDLVDAHRAQHNAVTVLTARVPNPTGYGRV-VRVGEEVAKIVEh 161
Cdd:cd06915 81 LGTGGAIKNALPKLPED--QFLVLNGDT-YFDVD-LLALLAALRASGADATMALRRVPDASRYGNVtVDGDGRVIAFVE- 155
|
170 180
....*....|....*....|
gi 567338369 162 KDATEEElkiDEINSGIYVF 181
Cdd:cd06915 156 KGPGAAP---GLINGGVYLL 172
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
10-252 |
2.49e-20 |
|
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: 89.55 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 10 IVLAAGGGTRMKS---AKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILsKDWPD----VEVALQPER 82
Cdd:cd04189 4 LILAGGKGTRLRPltyTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL-GDGSRfgvrITYILQEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 83 NGTGGAVQCGITSLGDatGEIIVTYGDvpMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRVGEEVAKIVEHK 162
Cdd:cd04189 83 LGLAHAVLAARDFLGD--EPFVVYLGD--NLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDGRIVRLVEKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 163 DATEEELKIdeinSGIYVFDAVTLrDGLGSLKAdNAQGELYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVqlaamn 242
Cdd:cd04189 159 KEPPSNLAL----VGVYAFTPAIF-DAISRLKP-SWRGELEITDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDL------ 226
|
250
....*....|
gi 567338369 243 AEVNRRICER 252
Cdd:cd04189 227 LEANRLLLDK 236
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
10-225 |
7.17e-20 |
|
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: 88.46 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 10 IVLAAGGGTR-----MKSAKsKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVG-HLREQVEEILS--KDWP-DVEVALQP 80
Cdd:pfam00483 3 IILAGGSGTRlwpltRTLAK-PLVPVGGKYPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGdgSKFGvQITYALQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 81 ERNGTGGAVQCGITSLGDATGEIIVTYGDVpmLDSDTLSDLVDAHRAQHNAVTVLTARVP--NPTGYGrVVRVGEE--VA 156
Cdd:pfam00483 82 EGKGTAPAVALAADFLGDEKSDVLVLGGDH--IYRMDLEQAVKFHIEKAADATVTFGIVPvePPTGYG-VVEFDDNgrVI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567338369 157 KIVEhKdaTEEELKIDEINSGIYVFDAVTLRDGLGSLKADnAQGELYLTDVIGYARSQGKRVGALVTDD 225
Cdd:pfam00483 159 RFVE-K--PKLPKASNYASMGIYIFNSGVLDFLAKYLEEL-KRGEDEITDILPKALEDGKLAYAFIFKG 223
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
325-441 |
5.74e-19 |
|
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: 82.55 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 325 IGENCEVGPFSRLRPGTTLGNGGKIGSfvetkNAHIGEGSKvphltycgdanIGSGVNIGAGTIFAN--------YDGFN 396
Cdd:cd03358 1 IGDNCIIGTNVFIENDVKIGDNVKIQS-----NVSIYEGVT-----------IEDDVFIGPNVVFTNdlyprskiYRKWE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 567338369 397 KSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:cd03358 65 LKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYAL 109
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
323-441 |
1.46e-18 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 81.84 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 323 AVIGENCEVGPFSRLRPGTTlgnggKIGsfvetKNAHIGEGSkvpHLTYCGDANIGSGVNIGAGTIFANY---------D 393
Cdd:COG0110 9 ARIGDGVVIGPGVRIYGGNI-----TIG-----DNVYIGPGV---TIDDPGGITIGDNVLIGPGVTILTGnhpiddpatF 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 567338369 394 GFNKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:COG0110 76 PLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAI 123
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
9-147 |
7.07e-18 |
|
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: 80.70 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSakSKLLHEVAGRPMLSYAVSAAKALsPQHLVVVVGHlrEQVEEILSKdwPDVEVALQPERN-GTGG 87
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRPA-GDEVVVVAND--EEVLAALAG--LGVPVVPDPDPGqGPLA 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567338369 88 AVQCGITSLGDATGeIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTA--RVPNPTGYGR 147
Cdd:pfam12804 74 GLLAALRAAPGADA-VLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYdgGRGHPLLYRR 134
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
11-188 |
3.66e-17 |
|
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: 80.31 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 11 VLAAGGGTRMKS---AKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDWPDVEVALQPERN---G 84
Cdd:cd06422 4 ILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLRITISDEPDellE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 85 TGGAVQCGITSLGDATgeIIVTYGDVPMLDSdtLSDLVDAHRAQHNAVTVLTARVPNPtGYGRVVRVGEEVAKIVEHKDA 164
Cdd:cd06422 84 TGGGIKKALPLLGDEP--FLVVNGDILWDGD--LAPLLLLHAWRMDALLLLLPLVRNP-GHNGVGDFSLDADGRLRRGGG 158
|
170 180
....*....|....*....|....
gi 567338369 165 TEeelKIDEINSGIYVFDAVTLRD 188
Cdd:cd06422 159 GA---VAPFTFTGIQILSPELFAG 179
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
9-227 |
5.60e-16 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 77.20 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMK---SAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDWPDVEVALQP--ERN 83
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPDVTFVYNPdyDET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 84 GTGGAVQCGITSLGDatgEIIVTYGDVpMLDSDTLSDLVDAHRAqhNAVTVlTARVPNPTGYGRVVRVGEEvAKIVEH-K 162
Cdd:COG1213 82 NNIYSLWLAREALDE---DFLLLNGDV-VFDPAILKRLLASDGD--IVLLV-DRKWEKPLDEEVKVRVDED-GRIVEIgK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567338369 163 DATEEElkIDEINSGIYVF---DAVTLRDGLGSLKaDNAQGELYLTDVIGYARSQGKRVGAL-VTDDVW 227
Cdd:COG1213 154 KLPPEE--ADGEYIGIFKFsaeGAAALREALEALI-DEGGPNLYYEDALQELIDEGGPVKAVdIGGLPW 219
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
271-440 |
1.33e-15 |
|
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: 75.14 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 271 DVELSEDVTILPNTQllgatkIESDAVVGPDTTL-------RDVEIGKGShVIRTHgelAVIGENCEVGPFSRLRPGTTL 343
Cdd:cd03352 1 SAKIGENVSIGPNAV------IGEGVVIGDGVVIgpgvvigDGVVIGDDC-VIHPN---VTIYEGCIIGDRVIIHSGAVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 344 GNGG-------------------KIGSFVE-----------TKNAHIGEGSKVPHLTYcgdanIGSGVNIGAGTIFANYD 393
Cdd:cd03352 71 GSDGfgfapdgggwvkipqlggvIIGDDVEiganttidrgaLGDTVIGDGTKIDNLVQ-----IAHNVRIGENCLIAAQV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 567338369 394 GFNKSkTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGA 440
Cdd:cd03352 146 GIAGS-TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGE 191
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
265-440 |
1.67e-14 |
|
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: 74.28 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 265 TTWIETDVELSEDVTILPNTQllgatkIESDAVVGPDTTlrdveIGKGSHVirthGELAVIGENCEVGPFSRLRPGTTLG 344
Cdd:COG1044 102 SAVIDPSAKIGEGVSIGPFAV------IGAGVVIGDGVV-----IGPGVVI----GDGVVIGDDCVLHPNVTIYERCVIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 345 N------GGKIGS----FVETKNahiGEGSKVPHLTYC--GD-----AN------------IGSGV---N---------I 383
Cdd:COG1044 167 DrviihsGAVIGAdgfgFAPDED---GGWVKIPQLGRVviGDdveigANttidrgalgdtvIGDGTkidNlvqiahnvrI 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 567338369 384 GAGTIFANYDGFNKSkTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGA 440
Cdd:COG1044 244 GEHTAIAAQVGIAGS-TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGG 299
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
323-440 |
2.80e-14 |
|
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: 71.36 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 323 AVIGENCEVGPFSRLRPGTTLGNGGKIGSfvetkNAHIGegskvpHltycgDANIGSGVNIGAGTIFANYdgfnkskTTL 402
Cdd:cd03360 97 AVIGEGCVIMAGAVINPDARIGDNVIINT-----GAVIG------H-----DCVIGDFVHIAPGVVLSGG-------VTI 153
|
90 100 110
....*....|....*....|....*....|....*...
gi 567338369 403 GDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGA 440
Cdd:cd03360 154 GEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGS 191
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
9-227 |
2.62e-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: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKS---AKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKdWPDVEVALQP--ERN 83
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK-YPNIKFVYNPdyAET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 84 GTGGAVQCGITSLGDatgEIIVTYGDVpMLDSDTLSDLVDahraqHNAVTVLTARVPNPTGYGRVVRVGEEVAKIVEHKD 163
Cdd:cd02523 80 NNIYSLYLARDFLDE---DFLLLEGDV-VFDPSILERLLS-----SPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIIS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567338369 164 ATEEELKIDEINSGIYVFDAVTLRDGLGSLKA--DNAQGELYLTDVIGYARSQGKRVGALVTDDVW 227
Cdd:cd02523 151 KAKNLEEIQGEYVGISKFSPEDADRLAEALEEliEAGRVNLYYEDALQRLISEEGVKVKDISDGFW 216
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
254-438 |
2.90e-13 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 70.94 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 254 MREGVTIVDPlTTWIETDVELSEDVTILPNtqllgatkiesdAVVGPDttlrdVEIGKGShVIRTHgelAVIGENCEVGP 333
Cdd:PRK00892 96 TPSPAAGIHP-SAVIDPSAKIGEGVSIGPN------------AVIGAG-----VVIGDGV-VIGAG---AVIGDGVKIGA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 334 FSRLRPGTTLGNGGKIGS----------------FVETKNAHIgegsKVPHLTYC--GD-----AN-------------- 376
Cdd:PRK00892 154 DCRLHANVTIYHAVRIGNrviihsgavigsdgfgFANDRGGWV----KIPQLGRViiGDdveigANttidrgalddtvig 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567338369 377 ----------IGSGVNIGAGTIFANYDGFNKSkTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPA 438
Cdd:PRK00892 230 egvkidnlvqIAHNVVIGRHTAIAAQVGIAGS-TKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPE 300
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
10-135 |
6.29e-13 |
|
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: 67.85 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 10 IVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGH--LREQVEEILSKDWPDVEVALQPerngtGG 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPpdDIEYFEELLAKYGIDKPVRVVA-----GG 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 88 A-----VQCGITSLGDATGEIIVTygDV--PMLDSDTLSDLVDAHRAQHNAVTVL 135
Cdd:COG1211 76 AtrqdsVRNGLEALPDDDDWVLVH--DAarPLVSPELIDRVIEAAREYGAAIPAL 128
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
356-441 |
7.03e-13 |
|
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: 64.79 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 356 KNAHIGEGSkvpHLTYCGDANIGSGVNIGAGTIF------------ANYDGFNKSKTTLGDEVFIGSNSVLVAPVTVGDG 423
Cdd:cd04647 6 DNVYIGPGC---VISAGGGITIGDNVLIGPNVTIydhnhdiddperPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82
|
90
....*....|....*...
gi 567338369 424 AFVAAGSAVTNDIPAGAL 441
Cdd:cd04647 83 AVVGAGSVVTKDVPPNSI 100
|
|
| LbH_SAT |
cd03354 |
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
358-440 |
2.54e-12 |
|
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: 62.84 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 358 AHIGEGSKVPHLTYC---GDANIGSGVNIGAG-TIFANYDGFNKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVT 433
Cdd:cd03354 9 AKIGPGLFIDHGTGIvigETAVIGDNCTIYQGvTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT 88
|
....*..
gi 567338369 434 NDIPAGA 440
Cdd:cd03354 89 KDVPANS 95
|
|
| LpxA |
COG1043 |
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
292-437 |
7.86e-12 |
|
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: 65.42 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 292 IESDAVVGPDttlrdVEIGKGSHVirthGELAVIGENCEVGPFSRLRPGTTLGNGGKIGSFvetknAHIGEgskVP-HLT 370
Cdd:COG1043 10 VDPGAKLGEN-----VEIGPFCVI----GPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPF-----ASIGE---EPqDLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 371 YC--------GDAN--------------------IGSG------------VNIGAGTIFANYdgfnkskTTL------GD 404
Cdd:COG1043 73 YKgeptrleiGDNNtirefvtihrgtvqgggvtrIGDDnllmayvhvahdCVVGNNVILANN-------ATLaghvevGD 145
|
170 180 190
....*....|....*....|....*....|...
gi 567338369 405 EVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIP 437
Cdd:COG1043 146 HAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVP 178
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
289-441 |
1.00e-11 |
|
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: 64.05 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 289 ATKIESDAVVGPDttlrdVEIGKGShvirthgelaVIGENCEVGPFSRlrpgttlgnggkIGSFVetknaHIGEGSKVPH 368
Cdd:TIGR03570 87 ATLIHPSAIVSPS-----ASIGEGT----------VIMAGAVINPDVR------------IGDNV-----IINTGAIVEH 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567338369 369 LTYCGD-ANIGSGVNIGAGTifanydgfnksktTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:TIGR03570 135 DCVIGDfVHIAPGVTLSGGV-------------VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGV 195
|
|
| LbH_XAT |
cd03349 |
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
307-438 |
1.78e-11 |
|
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.
Pssm-ID: 100040 [Multi-domain] Cd Length: 145 Bit Score: 61.79 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 307 VEIGKGSHVIRTHgeLAVIGENCEVGPFSRLRPGTTLGNGGkigsfvetkNAHIGEGSkvphlTYcgdaniGSGVNIGAG 386
Cdd:cd03349 2 ISVGDYSYGSGPD--CDVGGDKLSIGKFCSIAPGVKIGLGG---------NHPTDWVS-----TY------PFYIFGGEW 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 567338369 387 TIFANYDGFNKSK-TTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPA 438
Cdd:cd03349 60 EDDAKFDDWPSKGdVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPP 112
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
9-181 |
2.93e-11 |
|
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: 63.38 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKS---AKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSK--DWPDVEV--ALQPE 81
Cdd:cd06425 3 ALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyeKKLGIKItfSIETE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 82 RNGTGGAVQCGITSLGDATGEIIVtygdvpmLDSDT-----LSDLVDAHRAQHNAVTVLTARVPNPTGYGRVVRvgEEVA 156
Cdd:cd06425 83 PLGTAGPLALARDLLGDDDEPFFV-------LNSDVicdfpLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVH--DENT 153
|
170 180
....*....|....*....|....*
gi 567338369 157 KIVEHKDATEEELKIDEINSGIYVF 181
Cdd:cd06425 154 GRIERFVEKPKVFVGNKINAGIYIL 178
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-134 |
4.60e-11 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 62.54 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGH--LREQVEEILSKDWPD-VEVAlqperng 84
Cdd:cd02516 2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPpdDIDLAKELAKYGLSKvVKIV------- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 567338369 85 TGGA-----VQCGITSLGDATGEIIVTYgDV--PMLDSDTLSDLVDAhRAQHNAVTV 134
Cdd:cd02516 75 EGGAtrqdsVLNGLKALPDADPDIVLIH-DAarPFVSPELIDRLIDA-LKEYGAAIP 129
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
358-433 |
4.91e-11 |
|
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: 58.41 E-value: 4.91e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567338369 358 AHIGEGSKVPHLTYCGD-ANIGSGVNIGAGTIFANYDGFN-KSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVT 433
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGPNeKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
9-227 |
1.58e-10 |
|
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: 60.99 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKL---LHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILS--KDWP-DVEVALQPER 82
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTpkpMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGdgSKFGvNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 83 NGTGGAVqcgitSL--GDATGEIIVTYGDVpmLDSDTLSDLVDAHRAQHNAVTVLTA--RVPNPtgYGrVVRV-GEEVAK 157
Cdd:cd06426 81 LGTAGAL-----SLlpEKPTDPFLVMNGDI--LTNLNYEHLLDFHKENNADATVCVReyEVQVP--YG-VVETeGGRITS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567338369 158 IVEhKdATEEELkideINSGIYVFDavtlRDGLGSLKadnaQGELY-LTDVIGYARSQGKRVGALVTDDVW 227
Cdd:cd06426 151 IEE-K-PTHSFL----VNAGIYVLE----PEVLDLIP----KNEFFdMPDLIEKLIKEGKKVGVFPIHEYW 207
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
292-437 |
2.77e-10 |
|
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: 60.52 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 292 IESDAVVGPDttlrdVEIGKGSHVirthGELAVIGENCEVGPFSRLRPGTTLGNGGKIGSFV--------------ETK- 356
Cdd:cd03351 8 VDPGAKIGEN-----VEIGPFCVI----GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFAsigeapqdlkykgePTRl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 357 ----NAHIGEGSKV-------PHLTYCGDAN-------IGSGVNIGAGTIFANYdgfnkskTTL------GDEVFIGSNS 412
Cdd:cd03351 79 eigdNNTIREFVTIhrgtaqgGGVTRIGNNNllmayvhVAHDCVIGNNVILANN-------ATLaghveiGDYAIIGGLS 151
|
170 180
....*....|....*....|....*
gi 567338369 413 VLVAPVTVGDGAFVAAGSAVTNDIP 437
Cdd:cd03351 152 AVHQFCRIGRHAMVGGGSGVVQDVP 176
|
|
| PRK05289 |
PRK05289 |
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
289-437 |
3.74e-10 |
|
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 60.50 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 289 ATKIESDAVVGPDTTL-RDVEIGKGSHVirthGELAVIGENCEVGPFSRLRPGTTLGNGGKIGSFvetknAHIGEgskVP 367
Cdd:PRK05289 2 MAKIHPTAIVEPGAKIgENVEIGPFCVI----GPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPF-----ASIGE---DP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 368 -HLTY--------CGDANI-------------GSGV-------------------NIGAGTIFANYdgfnkskTTL---- 402
Cdd:PRK05289 70 qDLKYkgeptrlvIGDNNTirefvtinrgtvqGGGVtrigdnnllmayvhvahdcVVGNHVILANN-------ATLaghv 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 567338369 403 --GDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIP 437
Cdd:PRK05289 143 evGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVP 179
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
8-138 |
4.62e-09 |
|
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: 56.53 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQ--VEEILSKDWPDVEVALQPERNGT 85
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTefFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 86 ggaVQCGITSLGDATgeiIVTYGDV--PMLDSDTLSDLVDAHRAQHNAVTVLTAR 138
Cdd:TIGR00453 81 ---VRNGLKALKDAE---FVLVHDAarPFVPKELLDRLLEALRKAGAAILALPVA 129
|
|
| CysE |
COG1045 |
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
357-440 |
9.54e-09 |
|
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440667 [Multi-domain] Cd Length: 174 Bit Score: 54.70 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 357 NAHIGEGSKVPHltycgdaniGSGVNIGAGTIFANY-----------DGFNKSKT--TLGDEVFIGSNSVLVAPVTVGDG 423
Cdd:COG1045 71 GATIGRGFFIDH---------GTGVVIGETAVIGDNvtiyqgvtlggTGKEKGKRhpTIGDNVVIGAGAKILGPITIGDN 141
|
90
....*....|....*..
gi 567338369 424 AFVAAGSAVTNDIPAGA 440
Cdd:COG1045 142 AKIGANSVVLKDVPPGS 158
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
324-441 |
1.27e-08 |
|
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: 53.95 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 324 VIGENCEVGPFSRLRpgttlGNGGKI--GsfvetKNAHIGEGSkVPHLTYCGDANIGSGVNIGAGTIFANydgfnkskTT 401
Cdd:cd04645 19 TLGEGSSVWFGAVLR-----GDVNPIriG-----ERTNIQDGS-VLHVDPGYPTIIGDNVTVGHGAVLHG--------CT 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 567338369 402 LGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTND--IPAGAL 441
Cdd:cd04645 80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSL 121
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
9-138 |
1.57e-08 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 55.14 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHL--REQVEEILSKDWPDVEVAlqperngTG 86
Cdd:PRK00155 6 AIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPddRPDFAELLLAKDPKVTVV-------AG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 567338369 87 GA-----VQCGITSLGDAtgEIIVTYGDV-PMLDSDTLSDLVDAHRAQHNAVTVLTAR 138
Cdd:PRK00155 79 GAerqdsVLNGLQALPDD--DWVLVHDAArPFLTPDDIDRLIEAAEETGAAILAVPVK 134
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
266-437 |
2.88e-08 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 54.64 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 266 TWIETDVELSEDVTILPNTQLLGATKIESD------AVVGPDTtlRDVEI-GKGSHVIrthgelavIGENCEVGPFSRLR 338
Cdd:PRK12461 24 AVIGANVEIGDGTWIGPHAVILGPTRIGKNnkihqgAVVGDEP--QDFTYkGEESRLE--------IGDRNVIREGVTIH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 339 PGTTLGNGGKIGS---FVEtkNAHIGEgskvphltycgDANIGSGVNIGAGTIFANYdgfnkskTTLGDEVFIGSNSVLV 415
Cdd:PRK12461 94 RGTKGGGVTRIGNdnlLMA--YSHVAH-----------DCQIGNNVILVNGALLAGH-------VTVGDRAIISGNCLVH 153
|
170 180
....*....|....*....|..
gi 567338369 416 APVTVGDGAFVAAGSAVTNDIP 437
Cdd:PRK12461 154 QFCRIGALAMMAGGSRISKDVP 175
|
|
| LbH_THP_succinylT |
cd03350 |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
331-456 |
2.91e-08 |
|
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.
Pssm-ID: 100041 [Multi-domain] Cd Length: 139 Bit Score: 52.38 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 331 VGPFSRLRPGTTLGNGGKI--GSFVETkNAHIGEGSKV-PHLTYCGDANIGSGVNIGAGTIFAN-YDGFNKSKTTLGDEV 406
Cdd:cd03350 4 VPPGAIIRDGAFIGPGAVLmmPSYVNI-GAYVDEGTMVdSWATVGSCAQIGKNVHLSAGAVIGGvLEPLQATPVIIEDDV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 567338369 407 FIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAgalgIARSREHVSEGWVP 456
Cdd:cd03350 83 FIGANCEVVEGVIVGKGAVLAAGVVLTQSTPI----YDRETGEIYYGRVP 128
|
|
| LbH_MAT_GAT |
cd03357 |
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
401-441 |
4.16e-08 |
|
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: 52.81 E-value: 4.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 567338369 401 TLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:cd03357 120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
8-147 |
5.61e-08 |
|
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: 52.73 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMksAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwPDVEVALQPE-RNGTG 86
Cdd:TIGR03310 1 DAIILAAGLSSRM--GQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANH-SNITLVHNPQyAEGQS 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567338369 87 GAVQCGItSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLT--ARVPNPTGYGR 147
Cdd:TIGR03310 78 SSIKLGL-ELPVQSDGYLFLLGDQPFVTPDIIQLLLEAFALKNDEIVVPLykGKRGHPVLFPR 139
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
324-441 |
8.68e-08 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 51.95 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 324 VIGENCEVGPFSRLRpgttlGNGGKIgsfvetknaHIGEGSKVP-----HLTYCGDANIGSGVNIGAGTIF--Anydgfn 396
Cdd:COG0663 30 TIGEDVSVWPGAVLR-----GDVGPI---------RIGEGSNIQdgvvlHVDPGYPLTIGDDVTIGHGAILhgC------ 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 567338369 397 ksktTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTND--IPAGAL 441
Cdd:COG0663 90 ----TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSL 132
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
14-140 |
1.29e-07 |
|
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: 51.81 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 14 AGG-GTRMKSAKsKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQVEEILSKDwpDVEVAlqpERNGTgGAVQCG 92
Cdd:COG2266 2 AGGkGTRLGGGE-KPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKER--GVEVI---ETPGE-GYVEDL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 567338369 93 ITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRAqhNAVTVLTARVP 140
Cdd:COG2266 75 NEALESISGPVLVVPADLPLLTPEIIDDIIDAYLE--SGKPSLTVVVP 120
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
8-143 |
8.07e-07 |
|
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: 49.42 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSklLHEVAGRPMLSYAVSAAKALSPQhlVVVVGHLREQVEEIlskdwpDVEVaLQPERNGTG- 86
Cdd:COG0746 6 TGVILAGGRSRRMGQDKA--LLPLGGRPLLERVLERLRPQVDE--VVIVANRPERYAAL------GVPV-VPDDPPGAGp 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 567338369 87 -GAVQCGITSLgdATGEIIVTYGDVPMLDSDTLSDLVDAHRAQHNAVTVLTARVPNPT 143
Cdd:COG0746 75 lAGILAALEAA--PAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRSGGRLEPL 130
|
|
| LbH_Dynactin_5 |
cd03359 |
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ... |
267-420 |
5.77e-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: 46.44 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 267 WIETDV--ELSEDVTIL--PNTQLLGATKIESDAVVGPDttLRDVEIGKgshvirthgeLAVIGENCEVGPFSRLRPGTT 342
Cdd:cd03359 1 YIETASgnKVSRKSVICgsQNIVLNGKTIIQSDVIIRGD--LATVSIGR----------YCILSEGCVIRPPFKKFSKGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 343 LGNGGKIGSFVetknaHIGEGSKVphltYCgdANIGSGVNIGAGTIFANYdgfnkskTTLGDEVFIGSNSVL-----VAP 417
Cdd:cd03359 69 AFFPLHIGDYV-----FIGENCVV----NA--AQIGSYVHIGKNCVIGRR-------CIIKDCVKILDGTVVppdtvIPP 130
|
...
gi 567338369 418 VTV 420
Cdd:cd03359 131 YSV 133
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
9-220 |
8.32e-06 |
|
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: 46.86 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSA---KSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVV--GHLREQVEEILSKDW-PDVEVALQPer 82
Cdd:cd04183 1 IIIPMAGLGSRFKKAgytYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICrdEHNTKFHLDESLKLLaPNATVVELD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 83 NGTGGAVqCgiTSLGdATGEIIvtyGDVPML--DSDT-----LSDLVDAHRAQHNAVTVLTARVPNP------TGY-GRV 148
Cdd:cd04183 79 GETLGAA-C--TVLL-AADLID---NDDPLLifNCDQivesdLLAFLAAFRERDLDGGVLTFFSSHPrwsyvkLDEnGRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567338369 149 VRVGEEVaKIVEHkdATeeelkideinSGIYVF----DAVTLRDGLgSLKADNAQGELYLTDVIGYARSQGKRVGA 220
Cdd:cd04183 152 IETAEKE-PISDL--AT----------AGLYYFksgsLFVEAAKKM-IRKDDSVNGEFYISPLYNELILDGKKVGI 213
|
|
| LbH_unknown |
cd05635 |
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
288-387 |
9.59e-06 |
|
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100059 [Multi-domain] Cd Length: 101 Bit Score: 44.19 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 288 GATKIESDAVVGPDTTLR-DVEIGKGSHVIrthgelavigencevgPFSRLRPGTTLGNGGKIGSFVEtkNAHIGEGSKV 366
Cdd:cd05635 10 GPIYIGKDAVIEPFAVIEgPVYIGPGSRVK----------------MGARIYGNTTIGPTCKIGGEVE--DSIIEGYSNK 71
|
90 100
....*....|....*....|.
gi 567338369 367 PHLTYCGDANIGSGVNIGAGT 387
Cdd:cd05635 72 QHDGFLGHSYLGSWCNLGAGT 92
|
|
| DapD |
COG2171 |
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ... |
331-474 |
9.73e-06 |
|
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441774 [Multi-domain] Cd Length: 268 Bit Score: 47.03 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 331 VGPFSRLR------PGTTLgnggkIGSFVETkNAHIGEGSKVphltycgD--------ANIGSGVNIGAGT-IFANYDGF 395
Cdd:COG2171 100 IVPGARVRlgaylaPGVVL-----MPSFVNI-GAYVDEGTMV-------DtwatvgscAQIGKNVHLSGGAgIGGVLEPL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 396 NKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAgalgIARSREHVSEGWVPRTR---PGSKAAKAAEKST 472
Cdd:COG2171 167 QAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKI----YDRVTGEVYYGRVPAGSvvvPGSLPGKDGDYGL 242
|
..
gi 567338369 473 KT 474
Cdd:COG2171 243 YC 244
|
|
| lacA |
PRK09527 |
galactoside O-acetyltransferase; Reviewed |
401-437 |
1.32e-05 |
|
galactoside O-acetyltransferase; Reviewed
Pssm-ID: 181930 [Multi-domain] Cd Length: 203 Bit Score: 46.15 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|....*..
gi 567338369 401 TLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIP 437
Cdd:PRK09527 133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIP 169
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
9-188 |
1.87e-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: 46.42 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRM----KSAKSKLLHEVAG-RPMLSYAVSAAKALSPQ-HLVVVVG-----HLREQVEEILskdwPDVEVA 77
Cdd:cd02509 3 PVILAGGSGTRLwplsRESYPKQFLKLFGdKSLLQQTLDRLKGLVPPdRILVVTNeeyrfLVREQLPEGL----PEENII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 78 LQPERNGTGGAVqcgitslGDATGEIIVTYGDVPM--LDSDTLSDLVDA-HRAQHNAVTVLTAR-------VPN-P-TGY 145
Cdd:cd02509 79 LEPEGRNTAPAI-------ALAALYLAKRDPDAVLlvLPSDHLIEDVEAfLKAVKKAVEAAEEGylvtfgiKPTrPeTGY 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 567338369 146 GRVVRVGE------EVAKIVEHKDATEEELKIDE----INSGIYVFDAVTLRD 188
Cdd:cd02509 152 GYIEAGEKlgggvyRVKRFVEKPDLETAKEYLESgnylWNSGIFLFRAKTFLE 204
|
|
| NRPS_term_dom |
TIGR02353 |
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
346-439 |
1.89e-05 |
|
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.
Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 47.05 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 346 GGKIGsfvetKNAHIGegSKVPHLTycGDANIGSGVNIGAGTIFANY----DGFNKSKTTLGDEVFIGSNSVLVAPVTVG 421
Cdd:TIGR02353 112 GAKIG-----KGVDIG--SLPPVCT--DLLTIGAGTIVRKEVMLLGYraerGRLHTGPVTLGRDAFIGTRSTLDIDTSIG 182
|
90 100
....*....|....*....|
gi 567338369 422 DGAFVAAGSAVTND--IPAG 439
Cdd:TIGR02353 183 DGAQLGHGSALQGGqsIPDG 202
|
|
| PRK10092 |
PRK10092 |
maltose O-acetyltransferase; Provisional |
401-438 |
2.52e-05 |
|
maltose O-acetyltransferase; Provisional
Pssm-ID: 182235 [Multi-domain] Cd Length: 183 Bit Score: 44.80 E-value: 2.52e-05
10 20 30
....*....|....*....|....*....|....*...
gi 567338369 401 TLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPA 438
Cdd:PRK10092 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPD 168
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
9-140 |
2.55e-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: 45.34 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRM---KSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVghlREQVEEILSKDW----------PDVE 75
Cdd:cd04198 3 AVILAGGGGSRLyplTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV---PEEEQAEISTYLrsfplnlkqkLDEV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567338369 76 VALQPERNGTGGAVQcGITSLgdATGEIIVTYGDVpMLDSDtLSDLVDAHRAQHNAVTVLTARVP 140
Cdd:cd04198 80 TIVLDEDMGTADSLR-HIRKK--IKKDFLVLSCDL-ITDLP-LIELVDLHRSHDASLTVLLYPPP 139
|
|
| PRK10502 |
PRK10502 |
putative acyl transferase; Provisional |
401-439 |
4.69e-05 |
|
putative acyl transferase; Provisional
Pssm-ID: 236703 [Multi-domain] Cd Length: 182 Bit Score: 44.17 E-value: 4.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 567338369 401 TLGDEVFIGSNSVlVAP-VTVGDGAFVAAGSAVTNDIPAG 439
Cdd:PRK10502 126 VIGEGCWLAADVF-VAPgVTIGSGAVVGARSSVFKSLPAN 164
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
8-132 |
6.24e-05 |
|
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: 43.72 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLAAGGGTRMKSAKSKLlhEVAGRPMLSYAVsaaKALSPQ--HLVVVVGHlreqveEILSKDWPDVEVAlqPERNGT 85
Cdd:cd02503 2 TGVILAGGKSRRMGGDKALL--ELGGKPLLEHVL---ERLKPLvdEVVISANR------DQERYALLGVPVI--PDEPPG 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 567338369 86 GGAVQcGI-TSLGDATGE-IIVTYGDVPMLDSDTLSDLVDAHRAQHNAV 132
Cdd:cd02503 69 KGPLA-GIlAALRAAPADwVLVLACDMPFLPPELLERLLAAAEEGADAV 116
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
10-207 |
7.94e-05 |
|
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: 44.10 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 10 IVLAAGGGTRM---KSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVG--HLrEQVEEILS--KDWP-DVEVALQPE 81
Cdd:cd02538 4 IILAGGSGTRLyplTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpeDL-PLFKELLGdgSDLGiRITYAVQPK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 82 RNGTGGAVQCGITSLGDatGEIIVTYGDVPMLDSDtLSDLVDAHRAQHNAVTVLTARVPNPTGYGrVVRVGEE--VAKIV 159
Cdd:cd02538 83 PGGLAQAFIIGEEFIGD--DPVCLILGDNIFYGQG-LSPILQRAAAQKEGATVFGYEVNDPERYG-VVEFDENgrVLSIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 567338369 160 EHKdateEELKIDEINSGIYVFDAvTLRDGLGSLKAdNAQGELYLTDV 207
Cdd:cd02538 159 EKP----KKPKSNYAVTGLYFYDN-DVFEIAKQLKP-SARGELEITDV 200
|
|
| PLN02739 |
PLN02739 |
serine acetyltransferase |
309-441 |
7.99e-05 |
|
serine acetyltransferase
Pssm-ID: 215394 [Multi-domain] Cd Length: 355 Bit Score: 44.64 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 309 IGKGshVIRTHGELAVIGENCEVGPFSRLRPGTTLGNGGKigsfvETKNAHigegskvphltycgdANIGSGVNIGAGTi 388
Cdd:PLN02739 214 IGKG--ILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGK-----ETGDRH---------------PKIGDGALLGACV- 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 567338369 389 fanydgfnkskTTLGDevfigsnsvlvapVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:PLN02739 271 -----------TILGN-------------ISIGAGAMVAAGSLVLKDVPSHSM 299
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
9-238 |
1.01e-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: 43.59 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 9 VIVLAAGGGTRMKSAKSKLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHL--REQVEEILSkDWPDVEVALQPERNGTg 86
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPddTPEFRQLLG-DPSIQLVAGGDTRQDS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 87 gaVQCGITSLGDATGEIIVTYGDVPMLDSDTLSDLVDAHRaQHNAVTVLTARVPNptgygrVVRVGEEVAKIVEHKDate 166
Cdd:pfam01128 79 --VLNGLKALAGTAKFVLVHDGARPCLPHADLARLLAALE-TGTQGAILALPVTD------TIKRVEADGVVAGTPD--- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567338369 167 eelkideinsgiyvfdavtlRDGLgsLKADNAQGelYLTDVIGYARSQGKRVGALVTDDVWQTEGVNDRVQL 238
Cdd:pfam01128 147 --------------------RSGL--WAAQTPQG--FRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQV 194
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
8-183 |
2.23e-04 |
|
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: 43.01 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 8 AVIVLaaGG---GTRMK--SAKS-KLLHEVAGRPMLSYAVSAAKALSPQHLVVVVGHLREQV--EEILS-KDWPDVEVAL 78
Cdd:cd06428 1 AVILV--GGpqkGTRFRplSLDVpKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVfsDFISDaQQEFNVPIRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 79 QPERN--GTGGavqcGITS-----LGDATGEIIVTYGDV----PmldsdtLSDLVDAHRAQHNAVTVLTARVPNPTG--Y 145
Cdd:cd06428 79 LQEYKplGTAG----GLYHfrdqiLAGNPSAFFVLNADVccdfP------LQELLEFHKKHGASGTILGTEASREQAsnY 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 567338369 146 GRVVRvGEEVAKIVEHKDATEEELKiDEINSGIYVFDA 183
Cdd:cd06428 149 GCIVE-DPSTGEVLHYVEKPETFVS-DLINCGVYLFSP 184
|
|
| LbH_wcaF_like |
cd05825 |
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
328-441 |
2.41e-04 |
|
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.
Pssm-ID: 100063 [Multi-domain] Cd Length: 107 Bit Score: 40.28 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 328 NCEVGPFSRLRPGTTLGNGGKIgsfvetknaHIGEgskvphltycgDANIGSGVNIGAGTifANYD----GFNKSKTTLG 403
Cdd:cd05825 3 NLTIGDNSWIGEGVWIYNLAPV---------TIGS-----------DACISQGAYLCTGS--HDYRspafPLITAPIVIG 60
|
90 100 110
....*....|....*....|....*....|....*....
gi 567338369 404 DEVFIGSNSVlVAP-VTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:cd05825 61 DGAWVAAEAF-VGPgVTIGEGAVVGARSVVVRDLPAWTV 98
|
|
| LbH_gamma_CA |
cd00710 |
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
324-441 |
3.95e-04 |
|
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: 41.07 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 324 VIGENCEVGPFSRLR----PGTTLGNGGKIGSFV-----ETKNAHIGEGSKVPHLTYC-GDANIGSGVNIGAGTIFanyd 393
Cdd:cd00710 22 IIGDNVFVGPGASIRadegTPIIIGANVNIQDGVvihalEGYSVWIGKNVSIAHGAIVhGPAYIGDNCFIGFRSVV---- 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 567338369 394 gFNkskTTLGDEVFIGSNSVlVAPVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:cd00710 98 -FN---AKVGDNCVIGHNAV-VDGVEIPPGRYVPAGAVITSQTQADAL 140
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
118-346 |
3.99e-04 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 42.75 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 118 LSDLVDAHRAQHNAVTVLTARVPNP--TGYGrVVRVGEE--VAKIVEHKDATEEELkideINSGIYVFDAVTLRDglgSL 193
Cdd:COG0448 131 YRQMLDFHIESGADITVACIEVPREeaSRFG-VMEVDEDgrITEFEEKPKDPKSAL----ASMGIYVFNKDVLIE---LL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 194 KADNAQGEL-YLTDVI---------------GYARsqgkRVGALvtDDVWQT--EGVNDRVQLAAMNAevNRRICER--- 252
Cdd:COG0448 203 EEDAPNSSHdFGKDIIprlldrgkvyayefdGYWR----DVGTI--DSYYEAnmDLLDPEPEFNLYDP--EWPIYTKqkd 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 253 ----WMREGVTIVDPLT---TWIETDVE---LSEDVTILPNTQLlgatkieSDAVVGPdttlrDVEIGKGSHVIRthgel 322
Cdd:COG0448 275 lppaKFVRGGKVKNSLVsngCIISGTVEnsvLFRGVRVESGAVV-------ENSVIMP-----GVVIGEGAVIEN----- 337
|
250 260
....*....|....*....|....
gi 567338369 323 AVIGENCEVGpfsrlrPGTTLGNG 346
Cdd:COG0448 338 AIIDKNVVIP------PGVVIGED 355
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
283-424 |
4.98e-04 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 42.31 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 283 NTQLLGATKIESDAVVGPDttlrdveigkgshvirthgelAVIGENCEVGPFsrlrpgttlgnggkigsfvetknAHIGE 362
Cdd:COG1044 90 YPPPAPAPGIHPSAVIDPS---------------------AKIGEGVSIGPF-----------------------AVIGA 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567338369 363 GSKvphltycgdanIGSGVNIGAGTIfanydgfnkskttLGDEVFIGSNSVLVAPVTVGDGA 424
Cdd:COG1044 126 GVV-----------IGDGVVIGPGVV-------------IGDGVVIGDDCVLHPNVTIYERC 163
|
|
| PLN02296 |
PLN02296 |
carbonate dehydratase |
359-439 |
5.51e-04 |
|
carbonate dehydratase
Pssm-ID: 215167 [Multi-domain] Cd Length: 269 Bit Score: 41.65 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 359 HIGEGSKVphlTY-C---GDAN---IGSGVNIGAGTIF----ANYDGfNKSKTTLGDEVFIGSNSVLVA----------- 416
Cdd:PLN02296 72 QVGRGSSI---WYgCvlrGDVNsisVGSGTNIQDNSLVhvakTNLSG-KVLPTIIGDNVTIGHSAVLHGctvedeafvgm 147
|
90 100 110
....*....|....*....|....*....|.
gi 567338369 417 ------PVTVGDGAFVAAGSAVTND--IPAG 439
Cdd:PLN02296 148 gatlldGVVVEKHAMVAAGALVRQNtrIPSG 178
|
|
| PLN02357 |
PLN02357 |
serine acetyltransferase |
308-438 |
8.10e-04 |
|
serine acetyltransferase
Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 41.41 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 308 EIGKGshVIRTHGELAVIGENCEVGPFSRLRPGTTLGNGGKIgsfvetknahigegskvphltyCGDAN--IGSGVNIGA 385
Cdd:PLN02357 234 KIGQG--ILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQ----------------------SGDRHpkIGDGVLIGA 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 567338369 386 GT-IFANydgfnkskttlgdevfigsnsvlvapVTVGDGAFVAAGSAVTNDIPA 438
Cdd:PLN02357 290 GTcILGN--------------------------ITIGEGAKIGAGSVVLKDVPP 317
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
297-388 |
8.34e-04 |
|
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: 37.94 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 297 VVGPDTtlrdvEIGKGSHVIRThgelaVIGENCEVGPFSRLRpgttlgnggkiGSFVeTKNAHIGEGSKVPHLTYCGDAN 376
Cdd:cd05787 1 VIGRGT-----SIGEGTTIKNS-----VIGRNCKIGKNVVID-----------NSYI-WDDVTIEDGCTIHHSIVADGAV 58
|
90
....*....|..
gi 567338369 377 IGSGVNIGAGTI 388
Cdd:cd05787 59 IGKGCTIPPGSL 70
|
|
| PRK09677 |
PRK09677 |
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional |
394-454 |
1.27e-03 |
|
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
Pssm-ID: 137467 [Multi-domain] Cd Length: 192 Bit Score: 39.86 E-value: 1.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567338369 394 GFNKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGAL------GIARSREHVSEGW 454
Cdd:PRK09677 125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTViagnpaKIIKKYNHETKLW 191
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
278-351 |
1.63e-03 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 37.23 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567338369 278 VTILPNTQLLGATKIESDAVVGPDttlrdVEIGKGSHVIRTHGEL----AVIGENCEVGPFSRLRPGTTLGNGGKIGS 351
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGPVVIGDN-----VNIGPGAVIGAATGPNeknpTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73
|
|
| PRK10191 |
PRK10191 |
putative acyl transferase; Provisional |
374-441 |
3.89e-03 |
|
putative acyl transferase; Provisional
Pssm-ID: 182295 [Multi-domain] Cd Length: 146 Bit Score: 37.95 E-value: 3.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567338369 374 DANIGSGVNIGagtifaNYDGFNKSKTTLGDEVFIGSNSVLVAPVTVGDGAFVAAGSAVTNDIPAGAL 441
Cdd:PRK10191 73 DFTIRHGVTIG------NRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNAL 134
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
324-388 |
4.32e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.02 E-value: 4.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 324 VIGENCEVGPFSRLR-----PGTTLGNGGKIGSFVETKNAHIGEGSKvphLTYCgdaNIGSGVNIGAGTI 388
Cdd:cd04652 18 VIGANCKIGKRVKITncvimDNVTIEDGCTLENCIIGNGAVIGEKCK---LKDC---LVGSGYRVEAGTE 81
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
399-428 |
4.95e-03 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 34.62 E-value: 4.95e-03
10 20 30
....*....|....*....|....*....|
gi 567338369 399 KTTLGDEVFIGSNSVLVAPVTVGDGAFVAA 428
Cdd:pfam00132 1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
320-388 |
5.15e-03 |
|
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: 36.07 E-value: 5.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567338369 320 GELAVIGENCEVGPfSRLRPGTTLGNGGKIGSFVETKNAHIGEGSKVPHLTYCGDANIGSGVNIGAGTI 388
Cdd:cd03356 3 GESTVIGENAIIKN-SVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCI 70
|
|
| PLN02694 |
PLN02694 |
serine O-acetyltransferase |
308-438 |
5.53e-03 |
|
serine O-acetyltransferase
Pssm-ID: 178297 [Multi-domain] Cd Length: 294 Bit Score: 38.86 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567338369 308 EIGKGshVIRTHGELAVIGENCEVGPFSRLRPGTTLGNGGKIgsfvetknahigegskvphltyCGDAN--IGSGVNIGA 385
Cdd:PLN02694 168 KIGKG--ILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKA----------------------CGDRHpkIGDGVLIGA 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 567338369 386 GTifanydgfnkskTTLGDevfigsnsvlvapVTVGDGAFVAAGSAVTNDIPA 438
Cdd:PLN02694 224 GA------------TILGN-------------VKIGEGAKIGAGSVVLIDVPP 251
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
323-351 |
5.74e-03 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 34.23 E-value: 5.74e-03
10 20
....*....|....*....|....*....
gi 567338369 323 AVIGENCEVGPFSRLRPGTTLGNGGKIGS 351
Cdd:pfam00132 2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
|
|
| Hexapep_2 |
pfam14602 |
Hexapeptide repeat of succinyl-transferase; |
400-433 |
6.35e-03 |
|
Hexapeptide repeat of succinyl-transferase;
Pssm-ID: 434064 [Multi-domain] Cd Length: 33 Bit Score: 34.34 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|....
gi 567338369 400 TTLGDEVFIGSNSVLvaPVTVGDGAFVAAGSAVT 433
Cdd:pfam14602 1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVIT 32
|
|
| |
