|
Name |
Accession |
Description |
Interval |
E-value |
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
3-451 |
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: 720.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-DVEYALQEPQLGTGHAV 81
Cdd:COG1207 4 AVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADlDVEFVLQEEQLGTGHAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 82 MQAK-ALAEEDGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSAEE 158
Cdd:COG1207 84 QQALpALPGDDGTVLVLYGDVPLIRAETLkaLLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRIVEEKDATEEQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 159 LAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKH 238
Cdd:COG1207 164 RAIREINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADGLKVAAVQPEDPWEVLGVNDRVQLAEAERILQRR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 239 INHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVESKVGAK 318
Cdd:COG1207 244 IAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSVIEDAVVGAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 319 TTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFI 398
Cdd:COG1207 324 ATVGPFARLRPGTVLGEGVKIGNFVEVKNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDGAFI 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495965695 399 GSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKNK 451
Cdd:COG1207 404 GSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIEGWVRPKKKK 456
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-451 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 680.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 2 KSAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDDVEYALQEPQLGTGHAV 81
Cdd:PRK14354 3 RYAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFALQEEQLGTGHAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 82 MQAKA-LAEEDGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSAEE 158
Cdd:PRK14354 83 MQAEEfLADKEGTTLVICGDTPLITAETLknLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKIVEQKDATEEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 159 LAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKH 238
Cdd:PRK14354 163 KQIKEINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGEKVGAYQTEDFEESLGVNDRVALAEAEKVMRRR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 239 INHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVESKVGAK 318
Cdd:PRK14354 243 INEKHMVNGVTIIDPESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVDSTIGDGVTITNSVIEESKVGDN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 319 TTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFI 398
Cdd:PRK14354 323 VTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVNYDGKNKFKTIIGDNAFI 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495965695 399 GSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKNK 451
Cdd:PRK14354 403 GCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKEGYVKKLPHK 455
|
|
| glmU |
TIGR01173 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
3-450 |
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: 575.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-DVEYALQEPQLGTGHAV 81
Cdd:TIGR01173 2 SVVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALANrDVNWVLQAEQLGTGHAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 82 MQAKALAEEDGDTIIVNGDGPCIQKETILKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSAEELAI 161
Cdd:TIGR01173 82 LQALPFLSDDGDVLVLYGDVPLISAETLERLLEAHRQNGITLLTAKLDDPTGYGRIIRENDGKVTAIVEDKDANAEQKAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 162 KEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKHINH 241
Cdd:TIGR01173 162 KEINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRAVQVDDSDEVLGVNDRLQLAQLERILQRRIAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 242 KHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVE-SKVGAKTT 320
Cdd:TIGR01173 242 KLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKVKIGDDVVIGPGCVIKNSVIGSNVVIKAYSVLEgSEIGEGCD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 321 IGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFIGS 400
Cdd:TIGR01173 322 VGPFARLRPGSVLGAGVHIGNFVEVKNARIGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHKTIIGDGVFIGS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 495965695 401 NCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKN 450
Cdd:TIGR01173 402 NTQLVAPVKVGDGATIAAGSTVTKDVPEGALAISRARQRNIEGWVRPKKK 451
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-451 |
2.06e-172 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 491.57 E-value: 2.06e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD--DVEYALQEPQLGTGHA 80
Cdd:PRK14355 5 AAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGdgDVSFALQEEQLGTGHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 81 VMQA-KALAEEDGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSAE 157
Cdd:PRK14355 85 VACAaPALDGFSGTVLILCGDVPLLRAETLqgMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIVEEKDATPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 158 ELAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKK 237
Cdd:PRK14355 165 ERSIREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAAEGLRCLAFPVADPDEIMGVNDRAQLAEAARVLRR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 238 HINHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVE-SKVG 316
Cdd:PRK14355 245 RINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEdSVVG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 317 AKTTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGA 396
Cdd:PRK14355 325 DDVAIGPMAHLRPGTELSAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHRTVIEDDV 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495965695 397 FIGSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKNK 451
Cdd:PRK14355 405 FVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKEGWKLRKKDK 459
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-447 |
8.77e-167 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 476.73 E-value: 8.77e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKSAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD--DVEYALQEPQLGTG 78
Cdd:PRK14360 1 MLAVAILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHlpGLEFVEQQPQLGTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 79 HAVMQAKA-LAEEDGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCS 155
Cdd:PRK14360 81 HAVQQLLPvLKGFEGDLLVLNGDVPLLRPETLeaLLNTHRSSNADVTLLTARLPNPKGYGRVFCDGNNLVEQIVEDRDCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 156 AEELAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVeifhKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWM 235
Cdd:PRK14360 161 PAQRQNNRINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTV----SLLDPVMAVEVEDYQEINGINDRKQLAQCEEIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 236 KKHINHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVESKV 315
Cdd:PRK14360 237 QNRIKEKWMLAGVTFIDPASCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLIENSQIGENVTVLYSVVSDSQI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 316 GAKTTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDG 395
Cdd:PRK14360 317 GDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDGVKKHRTVIGDR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 495965695 396 AFIGSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSK 447
Cdd:PRK14360 397 SKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKENWKKK 448
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-438 |
3.46e-163 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 469.03 E-value: 3.46e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQ---DDVEYALQEPQLGTGHA 80
Cdd:PRK14352 7 VIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAelaPEVDIAVQDEQPGTGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 81 VMQA-KALAEE-DGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSA 156
Cdd:PRK14352 87 VQCAlEALPADfDGTVVVTAGDVPLLDGETLadLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQDGEVTAIVEQKDATP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 157 EELAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMK 236
Cdd:PRK14352 167 SQRAIREVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAIAREAGHRVGAHHADDSAEVAGVNDRVQLAALGAELN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 237 KHINHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVESKVG 316
Cdd:PRK14352 247 RRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVRTHGSESEIG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 317 AKTTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGA 396
Cdd:PRK14352 327 AGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVNKHRTTIGSHV 406
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 495965695 397 FIGSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQ 438
Cdd:PRK14352 407 RTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSEGPQ 448
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-451 |
1.01e-161 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 463.95 E-value: 1.01e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD---DVEYALQEPQLGTGHA 80
Cdd:PRK14353 8 AIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKiapDAEIFVQKERLGTAHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 81 VMQAK-ALAEEDGDTIIVNGDGPCIQKETILKAFAANQNYACTVltsVL----ADGERYGRIVRnRDGMVEKIVEAKDCS 155
Cdd:PRK14353 88 VLAAReALAGGYGDVLVLYGDTPLITAETLARLRERLADGADVV---VLgfraADPTGYGRLIV-KGGRLVAIVEEKDAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 156 AEELAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEeTMGVNDRVDLAKANSWM 235
Cdd:PRK14353 164 DEERAITLCNSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIARAEGLRVAVVEAPEDE-VRGINSRAELAEAEAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 236 KKHINHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHlqgntkIGSHVTIlpnsflrnaliEDGVTIDS-SKIVESK 314
Cdd:PRK14353 243 QARRRRAAMLAGVTLIAPETVFFSYDTVIGRDVVIEPNVV------FGPGVTV-----------ASGAVIHAfSHLEGAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 315 VGAKTTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKD 394
Cdd:PRK14353 306 VGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGAGANIGAGTITCNYDGFNKHRTEIGA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 495965695 395 GAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKNK 451
Cdd:PRK14353 386 GAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKPGWAKKLRER 442
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-451 |
2.70e-154 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 444.98 E-value: 2.70e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKsAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAeVDRIIVVVGHGANSVKEYLQDDVEYALQEPQLGTGHA 80
Cdd:PRK14357 1 MR-ALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKKV-AQKVGVVLGHEAELVKKLLPEWVKIFLQEEQLGTAHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 81 VMQAKALAEEDGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMveKIVEAKDCSAEE 158
Cdd:PRK14357 79 VMCARDFIEPGDDLLILYGDVPLISENTLkrLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKY--RIVEDKDAPEEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 159 LAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVeifhKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKH 238
Cdd:PRK14357 157 KKIKEINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAV----NFAEKVRVVKTEDLLEITGVNTRIQLAWLEKQLRMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 239 INHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVESKVGAK 318
Cdd:PRK14357 233 ILEELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKIIRSECEKSVIEDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 319 TTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFI 398
Cdd:PRK14357 313 VSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTFIEDGAFI 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495965695 399 GSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKNK 451
Cdd:PRK14357 393 GSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWVLKKRKE 445
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
5-448 |
6.58e-135 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 397.04 E-value: 6.58e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 5 IVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDD-VEYALQEPQLGTGHAVMQ 83
Cdd:PRK14358 11 VILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSgVAFARQEQQLGTGDAFLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 84 -AKALAEEDGDTIIVNGDGPCIQKETiLKAFAAN---QNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSAEEL 159
Cdd:PRK14358 91 gASALTEGDADILVLYGDTPLLRPDT-LRALVADhraQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQKDATDAEK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 160 AIKEINTGIFCFKtSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKHI 239
Cdd:PRK14358 170 AIGEFNSGVYVFD-ARAPELARRIGNDNKAGEYYLTDLLGLYRAGGAQVRAFKLSDPDEVLGANDRAGLAQLEATLRRRI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 240 NHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVE-SKVGAK 318
Cdd:PRK14358 249 NEAHMKAGVTLQDPGTILIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSVLHEGAVIKPHSVLEgAEVGAG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 319 TTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFI 398
Cdd:PRK14358 329 SDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNKHQSKVGAGVFI 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 495965695 399 GSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKY 448
Cdd:PRK14358 409 GSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNLEGWSRRY 458
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-451 |
2.76e-133 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 391.70 E-value: 2.76e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 2 KSAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDD-VEYALQEPQLGTGHA 80
Cdd:PRK09451 6 MSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEpLNWVLQAEQLGTGHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 81 VMQAKALAEEDGDTIIVNGDGPCIQKETILKAFAANQNYACTVLTSVLADGERYGRIVRnRDGMVEKIVEAKDCSAEELA 160
Cdd:PRK09451 86 MQQAAPFFADDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDNPTGYGRITR-ENGKVVGIVEQKDATDEQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 161 IKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKHIN 240
Cdd:PRK09451 165 IQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGREIVAVHPQRLSEVEGVNNRLQLARLERVYQAEQA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 241 HKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVE-SKVGAKT 319
Cdd:PRK09451 245 EKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEdANLGAAC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 320 TIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFIG 399
Cdd:PRK09451 325 TIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 495965695 400 SNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKYKNK 451
Cdd:PRK09451 405 SDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGWQRPVKKK 456
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-441 |
1.07e-129 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 382.53 E-value: 1.07e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-DVEYALQEPQLGTGHAVM 82
Cdd:PRK14356 8 ALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDeDARFVLQEQQLGTGHALQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 83 QAKALAEEDGDT--IIVNGDGPCIQKETILKAFAANQNYACTVLTSVLADGERYGRIVRnRDGMVEKIVEAKDCSAEEL- 159
Cdd:PRK14356 88 CAWPSLTAAGLDrvLVVNGDTPLVTTDTIDDFLKEAAGADLAFMTLTLPDPGAYGRVVR-RNGHVAAIVEAKDYDEALHg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 160 -AIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDLAKANSWMKKH 238
Cdd:PRK14356 167 pETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAVAEGMNVLGVNCGEDPNLLGVNTPAELVRSEELLRAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 239 INHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDS-SKIVESKVGA 317
Cdd:PRK14356 247 IVEKHLESGVLIHAPESVRIGPRATIEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVVSSGATIHSfSHLEGAEVGD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 318 KTTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAF 397
Cdd:PRK14356 327 GCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNKHRTVIGEGAF 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 495965695 398 IGSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIK 441
Cdd:PRK14356 407 IGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQKNL 450
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-448 |
4.52e-126 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 372.40 E-value: 4.52e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKSAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEvDRIIVVVGHGANSVKEYLQ---DDVEYALQEPQ--L 75
Cdd:PRK14359 2 KLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQKERIKEAVLeyfPGVIFHTQDLEnyP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 76 GTGHAVMQAKALAEEdgdTIIVNGDGPCIQKETiLKAFAANQNyacTVLTSV--LADGERYGRIVrNRDGMVEKIVEAKD 153
Cdd:PRK14359 81 GTGGALMGIEPKHER---VLILNGDMPLVEKDE-LEKLLENDA---DIVMSVfhLADPKGYGRVV-IENGQVKKIVEQKD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 154 CSAEELAIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDaEETMGVNDRVDLAKANS 233
Cdd:PRK14359 153 ANEEELKIKSVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAVFVDE-ENFMGVNSKFELAKAEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 234 WMKKHINHKHMLNGVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIgshvtilpnsflRNALIEDGVTIDSSKIVES 313
Cdd:PRK14359 232 IMQERIKKNAMKQGVIMRLPETIYIESGVEFEGECELEEGVRILGKSKI------------ENSHIKAHSVIEESIIENS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 314 kvgaktTIGPMSHLRNNTEIgENCRIGNFVEFKNSHFgNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIK 393
Cdd:PRK14359 300 ------DVGPLAHIRPKSEI-KNTHIGNFVETKNAKL-NGVKAGHLSYLGDCEIDEGTNIGAGTITCNYDGKKKHKTIIG 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495965695 394 DGAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDGDMGIARSRQSIKKGYGSKY 448
Cdd:PRK14359 372 KNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNIKNFYYKF 426
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-228 |
6.93e-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: 326.01 E-value: 6.93e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-DVEYALQEPQLGTGHAVM 82
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANpNVEFVLQEEQLGTGHAVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 83 QAK-ALAEEDGDTIIVNGDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEAKDCSAEEL 159
Cdd:cd02540 81 QALpALKDFEGDVLVLYGDVPLITPETLqrLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVEEKDATEEEK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495965695 160 AIKEINTGIFCFKTSKLFDGLKEITTNNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDRVDL 228
Cdd:cd02540 161 AIREVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVAAVLADDEEEVLGVNDRVQL 229
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
247-438 |
3.65e-105 |
|
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: 310.12 E-value: 3.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 247 GVTILDPDNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSSKIVE-SKVGAKTTIGPMS 325
Cdd:cd03353 1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEgAVIGNGATVGPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 326 HLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYRTTIKDGAFIGSNCNLI 405
Cdd:cd03353 81 HLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDNVFIGSNSQLV 160
|
170 180 190
....*....|....*....|....*....|...
gi 495965695 406 APVTIGENALLAAGSTITDSVDDGDMGIARSRQ 438
Cdd:cd03353 161 APVTIGDGATIAAGSTITKDVPPGALAIARARQ 193
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-422 |
5.71e-71 |
|
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: 229.40 E-value: 5.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKsAIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD------DVEYALQ 71
Cdd:TIGR03992 1 MK-AVILAAGKGTRMRpltETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDgsrggvPIEYVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 72 EPQLGTGHAVMQAKALaeEDGDTIIVNGDgpCIQKETILKAFAANqnYACTVLTSVLADGERYGrIVRNRDGMVEKIVEA 151
Cdd:TIGR03992 80 EEQLGTADALGSAKEY--VDDEFLVLNGD--VLLDSDLLERLIRA--EAPAIAVVEVDDPSDYG-VVETDGGRVTGIVEK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 152 KDCSAEELaikeINTGIFCFkTSKLFDGLKEITTNnAQNEYYLTDLVEIFHKhNEKVNAMIVDdaEETMGVNDRVDLAKA 231
Cdd:TIGR03992 153 PENPPSNL----INAGIYLF-SPEIFELLEKTKLS-PRGEYELTDALQLLID-EGKVKAVELD--GFWLDVGRPWDLLDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 232 NSWMKKHINHKhmlngvtildpdntyIDADVEigedttiyPNVHLQGNTKIGSHVTILPNSFlrnalIEDGVTIdsskiv 311
Cdd:TIGR03992 224 NEALLDNLEPR---------------IEGTVE--------ENVTIKGPVVIGEGAVIRSGTY-----IEGPVYI------ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 312 eskvGAKTTIGPMSHLRNNTEIGENCRIGNFVEFKNSHFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVN--YDGKN--- 386
Cdd:TIGR03992 270 ----GKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFGAGTKVANlrHDDKPvkv 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 495965695 387 ------------KYRTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTI 422
Cdd:TIGR03992 346 tvkgkrvdtgrrKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
4-215 |
7.29e-40 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 142.33 E-value: 7.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD------DVEYALQEPQ 74
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDgskfgvNIEYVVQEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 75 LGTGHAVMQAKALAeEDGDTIIVNGDGPCIQKETILKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIVEaKDC 154
Cdd:cd04181 81 LGTAGAVRNAEDFL-GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVE-KPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495965695 155 SAEelaIKEINTGIFCFKTSkLFDGLKEITTNnaqNEYYLTDLVEIFHKhNEKVNAMIVDD 215
Cdd:cd04181 159 LPE---SNLANAGIYIFEPE-ILDYIPEILPR---GEDELTDAIPLLIE-EGKVYGYPVDG 211
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
4-237 |
2.34e-35 |
|
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: 131.04 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD------DVEYALQEPQ 74
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDgsrfgvRITYVDEGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 75 LGTGHAVMQAKALAEEDgDTIIVNGDG---PCIQKetILKAFAANQNYACTVLTSVlADGERYGRIVRNRDGMVEKIVEA 151
Cdd:COG1208 82 LGTGGALKRALPLLGDE-PFLVLNGDIltdLDLAA--LLAFHREKGADATLALVPV-PDPSRYGVVELDGDGRVTRFVEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 152 KDCSAEELaikeINTGIFCFKTsKLFDGLKEittnnaqNEYYltDLVEIFHK--HNEKVNAMIVDDAEETMGVNDrvDLA 229
Cdd:COG1208 158 PEEPPSNL----INAGIYVLEP-EIFDYIPE-------GEPF--DLEDLLPRliAEGRVYGYVHDGYWLDIGTPE--DLL 221
|
....*...
gi 495965695 230 KANSWMKK 237
Cdd:COG1208 222 EANALLLS 229
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
1-235 |
1.06e-31 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 121.14 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKsAIVLAAGKGTRMKS---SLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDD------VEYALQ 71
Cdd:cd04189 1 MK-GLILAGGKGTRLRPltyTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGsrfgvrITYILQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 72 EPQLGTGHAVMQAKALAEED------GDTIIVNGDGPciqketILKAFAANQNYACTVLTSVlADGERYGRIVRnRDGMV 145
Cdd:cd04189 80 EEPLGLAHAVLAARDFLGDEpfvvylGDNLIQEGISP------LVRDFLEEDADASILLAEV-EDPRRFGVAVV-DDGRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 146 EKIVEAKDCSAEELAIkeinTGIFCFkTSKLFDGLKEITTnNAQNEYYLTDLVEIFHKHNEKVNAMIVDDAEETMGVNDr 225
Cdd:cd04189 152 VRLVEKPKEPPSNLAL----VGVYAF-TPAIFDAISRLKP-SWRGELEITDAIQWLIDRGRRVGYSIVTGWWKDTGTPE- 224
|
250
....*....|
gi 495965695 226 vDLAKANSWM 235
Cdd:cd04189 225 -DLLEANRLL 233
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-214 |
2.01e-31 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 121.74 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKsAIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVG-HGANSVKEYLQD------DVEYAL 70
Cdd:COG1209 1 MK-GIILAGGSGTRLRpltLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDgsqlgiKISYAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 71 QEPQLGTGHAVMQAK-ALAEED-----GDTIIvNGDGpcIQKetILKAFAANQNYACTVLTSVlADGERYGRIVRNRDGM 144
Cdd:COG1209 80 QPEPLGLAHAFIIAEdFIGGDPvalvlGDNIF-YGDG--LSE--LLREAAARESGATIFGYKV-EDPERYGVVEFDEDGR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495965695 145 VEKIVE--AKDCSaeELAIkeinTGIFCFkTSKLFDGLKEItTNNAQNEYYLTDLVEIFHKHNEKVNAMIVD 214
Cdd:COG1209 154 VVSLEEkpKEPKS--NLAV----TGLYFY-DNDVVEIAKNL-KPSARGELEITDANQAYLERGKLVVELLGR 217
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
269-423 |
3.07e-25 |
|
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100060 [Multi-domain] Cd Length: 163 Bit Score: 101.13 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 269 TIYPNVHLQGNTKIGshvtilpnsflRNALIEDGVTIDSSKIVeskvGAKTTIGPMSHLRNNTEIGENCRIGNFVEFKNS 348
Cdd:cd05636 7 TVEEGVTIKGPVWIG-----------EGAIVRSGAYIEGPVII----GKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 349 HFGNGSKCAHLTYVGDSDVGERVNFGCGVVTVNY--DGKN---------------KYRTTIKDGAFIGSNCNLIAPVTIG 411
Cdd:cd05636 72 IIMDGTKVPHLNYVGDSVLGENVNLGAGTITANLrfDDKPvkvrlkgervdtgrrKLGAIIGDGVKTGINVSLNPGVKIG 151
|
170
....*....|..
gi 495965695 412 ENALLAAGSTIT 423
Cdd:cd05636 152 PGSWVYPGCVVR 163
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-176 |
1.32e-23 |
|
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: 98.39 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKS---SLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD------DVEYALQEPQ 74
Cdd:cd06915 1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDgyrggiRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 75 LGTGHAVMQAKALAEEDgDTIIVNGDGPC-IQKETILKAFAANQNYACTVLTSVlADGERYGRIVRNRDGMVEKIVEAKD 153
Cdd:cd06915 81 LGTGGAIKNALPKLPED-QFLVLNGDTYFdVDLLALLAALRASGADATMALRRV-PDASRYGNVTVDGDGRVIAFVEKGP 158
|
170 180
....*....|....*....|...
gi 495965695 154 CSAEELaikeINTGIFCFKTSKL 176
Cdd:cd06915 159 GAAPGL----INGGVYLLRKEIL 177
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
4-234 |
4.74e-21 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 91.46 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD---DVEYALQEP--QL 75
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARpgpDVTFVYNPDydET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 76 GTGHAVMQAKALAeeDGDTIIVNGDgpCIQKETILKAFAANQNYAC----TVLTSVLADGERYgriVRNRDGMVEKI--- 148
Cdd:COG1213 82 NNIYSLWLAREAL--DEDFLLLNGD--VVFDPAILKRLLASDGDIVllvdRKWEKPLDEEVKV---RVDEDGRIVEIgkk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 149 VEAKDCSAEelaikeiNTGIFCFK---TSKLFDGLKEITTNNAQNEYYlTDLVEIFHKHNEKVNAMIVDD---AEetmgV 222
Cdd:COG1213 155 LPPEEADGE-------YIGIFKFSaegAAALREALEALIDEGGPNLYY-EDALQELIDEGGPVKAVDIGGlpwVE----I 222
|
250
....*....|..
gi 495965695 223 NDRVDLAKANSW 234
Cdd:COG1213 223 DTPEDLERAEEL 234
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
4-178 |
4.29e-19 |
|
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: 86.15 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNK-PMIGHIIAALRAAEVDRIIVVVG-HGANSVKEYLQD------DVEYALQE 72
Cdd:pfam00483 2 AIILAGGSGTRLWpltRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGDgskfgvQITYALQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 73 PQLGTGHAVMQAKALAEEDGDTIIVNGDGPCIQ---KETILKAFAANQNYACTVLTSVLADGERYGRIVRNRDGMVEKIV 149
Cdd:pfam00483 82 EGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRmdlEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIRFV 161
|
170 180
....*....|....*....|....*....
gi 495965695 150 EAKDcsaEELAIKEINTGIFCFKtSKLFD 178
Cdd:pfam00483 162 EKPK---LPKASNYASMGIYIFN-SGVLD 186
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-116 |
1.33e-17 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 80.59 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSslCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-DVEYAL-QEPQLGTGHA 80
Cdd:COG2068 5 AAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGlGVRVVVnPDWEEGMSSS 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 495965695 81 VmQA--KALAEEDGDTIIVNGDGPCIQKETI---LKAFAAN 116
Cdd:COG2068 83 L-RAglAALPADADAVLVLLGDQPLVTAETLrrlLAAFRES 122
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-109 |
4.17e-17 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 79.14 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSslCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDDVEYAL--QEPQLGTGHA 80
Cdd:cd04182 2 AAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVinPDWEEGMSSS 79
|
90 100 110
....*....|....*....|....*....|..
gi 495965695 81 VmqAKALAE--EDGD-TIIVNGDGPCIQKETI 109
Cdd:cd04182 80 L--AAGLEAlpADADaVLILLADQPLVTAETL 109
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-182 |
1.20e-15 |
|
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: 75.69 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKS---SLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-----DVEYALQEPQ- 74
Cdd:cd06422 2 AMILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDsrfglRITISDEPDEl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 75 LGTGHAVmqAKALAEEDGDTIIV-NGDGPCI---QKETILKAFAANQNYACTVLTSVLaDGERYGRIVRNRDGMVEKive 150
Cdd:cd06422 82 LETGGGI--KKALPLLGDEPFLVvNGDILWDgdlAPLLLLHAWRMDALLLLLPLVRNP-GHNGVGDFSLDADGRLRR--- 155
|
170 180 190
....*....|....*....|....*....|..
gi 495965695 151 akdcSAEELAIKEINTGIFCFKTsKLFDGLKE 182
Cdd:cd06422 156 ----GGGGAVAPFTFTGIQILSP-ELFAGIPP 182
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
333-429 |
2.72e-15 |
|
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.
Pssm-ID: 100048 [Multi-domain] Cd Length: 119 Bit Score: 71.76 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 333 IGENCRIGNFVEF-KNSHFGNGSKCAHLTYVGD-SDVGERVNFGCGVVTVN--------YDGKNKYRTTIKDGAFIGSNC 402
Cdd:cd03358 1 IGDNCIIGTNVFIeNDVKIGDNVKIQSNVSIYEgVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANA 80
|
90 100
....*....|....*....|....*..
gi 495965695 403 NLIAPVTIGENALLAAGSTITDSVDDG 429
Cdd:cd03358 81 TILPGVTIGEYALVGAGAVVTKDVPPY 107
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-232 |
3.46e-15 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 74.58 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKS---SLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDDVE--------YALqe 72
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNikfvynpdYAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 73 pqlgTGHAVMQAKALAEEDGDTIIVNGDgpCIQKETILKAFAANQNYACTVLTSVL-ADGERYGRIVRNRDGMVEKIVEA 151
Cdd:cd02523 79 ----TNNIYSLYLARDFLDEDFLLLEGD--VVFDPSILERLLSSPADNAILVDKKTkEWEDEYVKDLDDAGVLLGIISKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 152 KDcsaeelaIKEIN---TGIFCFKTS---KLFDGLKEITTNNAQNEYYlTDLVEIFhKHNEKVNAMIVDD---AEetmgV 222
Cdd:cd02523 153 KN-------LEEIQgeyVGISKFSPEdadRLAEALEELIEAGRVNLYY-EDALQRL-ISEEGVKVKDISDgfwYE----I 219
|
250
....*....|
gi 495965695 223 NDRVDLAKAN 232
Cdd:cd02523 220 DDLEDLERAE 229
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
4-135 |
5.06e-15 |
|
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: 72.23 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSslCKVMHPVLNKPMIGHIIAALRAAeVDRIIVVVGHgaNSVKEYLQD-DVEYALQE-PQLGTGHAV 81
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRPA-GDEVVVVAND--EEVLAALAGlGVPVVPDPdPGQGPLAGL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 495965695 82 MQAKALAEEDGDTIIVNGDGPCIQKETILKAFAANQNYACTVLtsVLADGERYG 135
Cdd:pfam12804 76 LAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV--VPVYDGGRG 127
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
2-196 |
3.03e-14 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 72.57 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 2 KSAIVLAAGKGTRM---KSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLqdDVEYAL-------- 70
Cdd:cd02541 1 RKAVIPAAGLGTRFlpaTKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHF--DRSYELeetlekkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 71 ---------------------QEPQLGTGHAVMQAKALAEED------GDTIIVNgDGPCIQKetILKAFAAnqnYACTV 123
Cdd:cd02541 79 ktdlleevriisdlanihyvrQKEPLGLGHAVLCAKPFIGDEpfavllGDDLIDS-KEPCLKQ--LIEAYEK---TGASV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 124 LTSVLADGE---RYGRIVRNRD--------GMVEK--IVEAKdcsaEELAIkeinTGIFCFkTSKLFDGLKEITTnNAQN 190
Cdd:cd02541 153 IAVEEVPPEdvsKYGIVKGEKIdgdvfkvkGLVEKpkPEEAP----SNLAI----VGRYVL-TPDIFDILENTKP-GKGG 222
|
....*.
gi 495965695 191 EYYLTD 196
Cdd:cd02541 223 EIQLTD 228
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
327-429 |
1.59e-13 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 67.59 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 327 LRNNTEIGENCRIGNFVEF--KNSHFGNGSKCAHLTYVGDSD---VGERVNFGCGVV--TVNYDGKNKYR-------TTI 392
Cdd:COG0110 5 LLFGARIGDGVVIGPGVRIygGNITIGDNVYIGPGVTIDDPGgitIGDNVLIGPGVTilTGNHPIDDPATfplrtgpVTI 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 495965695 393 KDGAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDG 429
Cdd:COG0110 85 GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPY 121
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
3-143 |
1.60e-13 |
|
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: 69.47 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAA-EVDRIIVVVGHgansvkeylqDDVEYALQEPQLGTG--- 78
Cdd:cd02516 2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHpAIDEIVVVVPP----------DDIDLAKELAKYGLSkvv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 79 ----------HAVMQA-KALAEEDGDTIIVNgDG--PCIQKETILKAFAANQNYACTVLTSVLAD----GERYGRIVR-- 139
Cdd:cd02516 72 kiveggatrqDSVLNGlKALPDADPDIVLIH-DAarPFVSPELIDRLIDALKEYGAAIPAVPVTDtikrVDDDGVVVEtl 150
|
....
gi 495965695 140 NRDG 143
Cdd:cd02516 151 DREK 154
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
257-421 |
2.29e-13 |
|
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: 70.82 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 257 YIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFlrnalIEDGVTIdsskiveskvGAKTTIGPMSHLRNNTEIGEN 336
Cdd:COG1044 104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVV-----IGDGVVI----------GDDCVLHPNVTIYERCVIGDR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 337 CRI-----------GNFVEFKNSHFgngsKCAHLTYVgdsDVGERVNFGCGvvtvnydgknkyrTTIKDGAF----IGSN 401
Cdd:COG1044 169 VIIhsgavigadgfGFAPDEDGGWV----KIPQLGRV---VIGDDVEIGAN-------------TTIDRGALgdtvIGDG 228
|
170 180 190
....*....|....*....|....*....|.
gi 495965695 402 C---NL--IA-PVTIGENALLA-----AGST 421
Cdd:COG1044 229 TkidNLvqIAhNVRIGEHTAIAaqvgiAGST 259
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
5-144 |
3.38e-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: 68.62 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 5 IVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAA-EVDRIIVVVGHGAnsvKEYLQDDVE-YALQEP-QLGTG--- 78
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHpRIDEIVVVVPPDD---IEYFEELLAkYGIDKPvRVVAGgat 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495965695 79 --HAVMQA-KALAEEDgDTIIVNgDG--PCIQKETILKAFAANQNYACTVL------TSVLADGEryGRIVR--NRDGM 144
Cdd:COG1211 78 rqDSVRNGlEALPDDD-DWVLVH-DAarPLVSPELIDRVIEAAREYGAAIPalpvtdTIKRVDDD--GRVTEtvDRSGL 152
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-210 |
3.96e-13 |
|
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: 68.31 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD------DVEYaLQEPQ 74
Cdd:cd06426 1 VVIMAGGKGTRLRpltENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDgskfgvNISY-VREDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 75 -LGTGHAVmqaKALAEEDGDTIIV-NGD---GpcIQKETILKAFAANQNYA--CTVLTSVLADgerYGrIVRNRDGMVEK 147
Cdd:cd06426 80 pLGTAGAL---SLLPEKPTDPFLVmNGDiltN--LNYEHLLDFHKENNADAtvCVREYEVQVP---YG-VVETEGGRITS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495965695 148 IVEAKDCSaeelaiKEINTGIFCFKtSKLFDGLKEittnnaqNEYY-LTDLVEIFHKHNEKVNA 210
Cdd:cd06426 151 IEEKPTHS------FLVNAGIYVLE-PEVLDLIPK-------NEFFdMPDLIEKLIKEGKKVGV 200
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
249-429 |
7.90e-13 |
|
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: 67.05 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 249 TILDPdNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNS------F--------------LRNALIEDGVTIdss 308
Cdd:cd03352 26 VVIGP-GVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAvigsdgFgfapdgggwvkipqLGGVIIGDDVEI--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 309 kiveskvGAKTTI--GPMShlrnNTEIGENCRIGNFVEFknshfgngskcAHltyvgDSDVGERVNFgCGVVTVNydGkn 386
Cdd:cd03352 102 -------GANTTIdrGALG----DTVIGDGTKIDNLVQI-----------AH-----NVRIGENCLI-AAQVGIA--G-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495965695 387 kyRTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDG 429
Cdd:cd03352 150 --STTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPG 190
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-176 |
1.44e-12 |
|
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: 66.85 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKsAIVLAAGKGTRMKS---SLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-------DVEYAL 70
Cdd:cd06425 1 MK-ALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyekklgiKITFSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 71 QEPQLGTGHAVMQAKALAEEDGDTIIV-NGDGPCIQKETILKAFAANQNYACTVLTSVLADGERYGRIVRNRD-GMVEKI 148
Cdd:cd06425 80 ETEPLGTAGPLALARDLLGDDDEPFFVlNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERF 159
|
170 180
....*....|....*....|....*...
gi 495965695 149 VEakdcSAEELAIKEINTGIFCFKTSKL 176
Cdd:cd06425 160 VE----KPKVFVGNKINAGIYILNPSVL 183
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-196 |
1.92e-12 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 67.36 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 2 KSAIVLAAGKGTRM----KSSlCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSV------------------- 58
Cdd:COG1210 4 RKAVIPVAGLGTRFlpatKAI-PKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIedhfdrsyeleatleakgk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 59 KEYLQD--------DVEYALQEPQLGTGHAVMQAKALAEED------GDTIIVnGDGPCIQKetILKAFaanQNYACTVL 124
Cdd:COG1210 83 EELLEEvrsisplaNIHYVRQKEPLGLGHAVLCARPFVGDEpfavllGDDLID-SEKPCLKQ--MIEVY---EETGGSVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 125 ---------TS---VLADGERYGRIVRnRDGMVEKIveakdcSAEE----LAIkeinTG--IFcfkTSKLFDGLKEITTn 186
Cdd:COG1210 157 avqevppeeVSkygIVDGEEIEGGVYR-VTGLVEKP------APEEapsnLAI----VGryIL---TPEIFDILEKTKP- 221
|
250
....*....|
gi 495965695 187 NAQNEYYLTD 196
Cdd:COG1210 222 GAGGEIQLTD 231
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-144 |
4.90e-12 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 65.15 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKSAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAA-EVDRIIVVVGhgansvkeylQDDVEYALQEP------ 73
Cdd:PRK00155 3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHpRIDEIIVVVP----------PDDRPDFAELLlakdpk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 74 -QLGTG-----HAVMQA-KALAEEDgdtIIVNGDG--PCIQKETILKAFAANQNYACTVLTSVLAD----GERYGRIVR- 139
Cdd:PRK00155 73 vTVVAGgaerqDSVLNGlQALPDDD---WVLVHDAarPFLTPDDIDRLIEAAEETGAAILAVPVKDtikrSDDGGGIVDt 149
|
....*.
gi 495965695 140 -NRDGM 144
Cdd:PRK00155 150 pDRSGL 155
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
3-130 |
6.93e-12 |
|
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: 64.62 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAAE-VDRIIVVVghgANSVKEYLQDDVEyALQEPQLGTG--- 78
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPaIDEVVVVV---SPDDTEFFQKYLV-ARAVPKIVAGgdt 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 495965695 79 --HAVMQA-KALaeEDGDTIIVNgDG--PCIQKETILKAFAANQNYACTVLTSVLAD 130
Cdd:TIGR00453 77 rqDSVRNGlKAL--KDAEFVLVH-DAarPFVPKELLDRLLEALRKAGAAILALPVAD 130
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
247-426 |
1.03e-11 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 65.04 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 247 GVTILDpdNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFL-------------------RNALIEDGVTIDS 307
Cdd:PRK12461 17 GVEIGP--FAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftykgeesrleigDRNVIREGVTIHR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 308 SkiveSKVGAKTTIGPMSHLRNNTEIGENCRIGNfvefkNSHFGNGSKCAhltyvgdsdvgervnfgcGVVTVNydgknk 387
Cdd:PRK12461 95 G----TKGGGVTRIGNDNLLMAYSHVAHDCQIGN-----NVILVNGALLA------------------GHVTVG------ 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 495965695 388 yrttikDGAFIGSNCNLIAPVTIGENALLAAGSTITDSV 426
Cdd:PRK12461 142 ------DRAIISGNCLVHQFCRIGALAMMAGGSRISKDV 174
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
249-409 |
2.53e-11 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 64.78 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 249 TILDPdNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNS------F--------------LRNALIEDGVTIdss 308
Cdd:PRK00892 137 VVIGA-GAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAvigsdgFgfandrggwvkipqLGRVIIGDDVEI--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 309 kiveskvGAKTTI--GPMShlrnNTEIGENCRIGNFVEF-KNSHFGNGSKCAHLTYV-GDSDVGERVNFGCGVVTVNydg 384
Cdd:PRK00892 213 -------GANTTIdrGALD----DTVIGEGVKIDNLVQIaHNVVIGRHTAIAAQVGIaGSTKIGRYCMIGGQVGIAG--- 278
|
170 180
....*....|....*....|....*
gi 495965695 385 knkyRTTIKDGAFIGSNCNLIAPVT 409
Cdd:PRK00892 279 ----HLEIGDGVTITAMSGVTKSIP 299
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
257-430 |
2.98e-11 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 64.39 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 257 YIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFlrnalIEDGVTIdsskiveskvGAKTTIGPMSHLRNNTEIGEN 336
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAV-----IGDGVKI----------GADCRLHANVTIYHAVRIGNR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 337 C------RIGN----FVEFKNSHFgngsKCAHLTYVgdsDVGERVNFGCGvvtvnydgknkyrTTIKDGAF----IGSNC 402
Cdd:PRK00892 173 ViihsgaVIGSdgfgFANDRGGWV----KIPQLGRV---IIGDDVEIGAN-------------TTIDRGALddtvIGEGV 232
|
170 180 190
....*....|....*....|....*....|....
gi 495965695 403 ---NL--IA-PVTIGENALLAAGSTITDSVDDGD 430
Cdd:PRK00892 233 kidNLvqIAhNVVIGRHTAIAAQVGIAGSTKIGR 266
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
5-194 |
3.29e-11 |
|
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: 63.04 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 5 IVLAAGKGTRMKS---SLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVG-------HGANSVKEYLQDDVEYALQEPQ 74
Cdd:cd04183 2 IIPMAGLGSRFKKagyTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRdehntkfHLDESLKLLAPNATVVELDGET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 75 LGTGHAVMQAKALAEEDGDTIIVNGDGpcIQKETI---LKAFAANQNYACTVltSVLADGERYGRIVRNRDGMVEKIVEA 151
Cdd:cd04183 82 LGAACTVLLAADLIDNDDPLLIFNCDQ--IVESDLlafLAAFRERDLDGGVL--TFFSSHPRWSYVKLDENGRVIETAEK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495965695 152 KDCSaeELAIkeinTGIFCFKTSKLF-DGLKEITTNNAQ--NEYYL 194
Cdd:cd04183 158 EPIS--DLAT----AGLYYFKSGSLFvEAAKKMIRKDDSvnGEFYI 197
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
7-127 |
3.82e-11 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 61.83 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 7 LAAGKGTRMKSSLcKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQD-DVEYaLQEPqlGTGHAV-MQA 84
Cdd:COG2266 1 MAGGKGTRLGGGE-KPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKErGVEV-IETP--GEGYVEdLNE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 495965695 85 kALAEEDGDTIIVNGDGPCIQKETILKAFAANQNY---ACTVLTSV 127
Cdd:COG2266 77 -ALESISGPVLVVPADLPLLTPEIIDDIIDAYLESgkpSLTVVVPA 121
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
249-429 |
7.43e-11 |
|
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: 63.11 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 249 TILDPdNTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNS------F---------------LRNALIEDGVTIds 307
Cdd:COG1044 133 VVIGP-GVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAvigadgFgfapdedggwvkipqLGRVVIGDDVEI-- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 308 skiveskvGAKTTI--GPMShlrnNTEIGENCRIGNFVEFknshfgngskcAHLTYVGD------------Sdvgervnf 373
Cdd:COG1044 210 --------GANTTIdrGALG----DTVIGDGTKIDNLVQI-----------AHNVRIGEhtaiaaqvgiagS-------- 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495965695 374 gcgvvtvnydgknkyrTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDG 429
Cdd:COG1044 259 ----------------TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEG 298
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
3-120 |
2.93e-10 |
|
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: 59.28 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSlcKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYL--QDDVEYALQ-EPQLGTGH 79
Cdd:TIGR03310 1 DAIILAAGLSSRMGQN--KLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLanHSNITLVHNpQYAEGQSS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495965695 80 AVMQAKALAEEDGDTIIVNGDGPCIQKETI---LKAFAANQNYA 120
Cdd:TIGR03310 79 SIKLGLELPVQSDGYLFLLGDQPFVTPDIIqllLEAFALKNDEI 122
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-118 |
4.88e-10 |
|
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.
Pssm-ID: 396773 Cd Length: 217 Bit Score: 59.27 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSslcKVMHPVLNKPMIGHII-AALRAAEVDRIIVvvghgANSVKEYLQDDVEYALQ----EPQLGTG 78
Cdd:pfam02348 2 AIIPARLGSKRLPG---KNLLDLGGKPLIHHVLeAALKSGAFEKVIV-----ATDSEEIADVAKEFGAGvvmtSGSLSSG 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495965695 79 -HAVMQAKALAEEDGDTIIVN--GDGPCIQKETILKAFAANQN 118
Cdd:pfam02348 74 tDRFYEVVKAFLNDHDDIIVNiqGDNPLLQPEVILKAIETLLN 116
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
248-429 |
9.52e-10 |
|
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.
Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 57.88 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 248 VTILDPDnTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTIlpNSflrNALIEdgvtidsskiveskvgakttigpmsHl 327
Cdd:cd03360 84 ATLIHPS-AVVSPSAVIGEGCVIMAGAVINPDARIGDNVII--NT---GAVIG-------------------------H- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 328 rnnteigeNCRIGNFVefknsHFGNGSKCahltyvgdsdvgervnfgCGVVTvnydgknkyrttIKDGAFIGSNCNLIAP 407
Cdd:cd03360 132 --------DCVIGDFV-----HIAPGVVL------------------SGGVT------------IGEGAFIGAGATIIQG 168
|
170 180
....*....|....*....|..
gi 495965695 408 VTIGENALLAAGSTITDSVDDG 429
Cdd:cd03360 169 VTIGAGAIIGAGAVVTKDVPDG 190
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
1-150 |
1.72e-09 |
|
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: 57.97 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKsAIVLAAGKGTRMkSSLCKVMH----PVLNKPMIGHIIAALRAAEVDRIIVVVGHGANS-VKEYLQD------DVEYA 69
Cdd:cd02538 1 MK-GIILAGGSGTRL-YPLTKVVSkqllPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPlFKELLGDgsdlgiRITYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 70 LQEPQLGtghaVMQAKALAEE---DGDTIIVNGD----GPCIQKetILKAFAANQNYAcTVLTSVLADGERYGRIVRNRD 142
Cdd:cd02538 79 VQPKPGG----LAQAFIIGEEfigDDPVCLILGDnifyGQGLSP--ILQRAAAQKEGA-TVFGYEVNDPERYGVVEFDEN 151
|
....*...
gi 495965695 143 GMVEKIVE 150
Cdd:cd02538 152 GRVLSIEE 159
|
|
| PRK05289 |
PRK05289 |
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase; |
256-348 |
8.24e-09 |
|
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
Pssm-ID: 235390 [Multi-domain] Cd Length: 262 Bit Score: 56.26 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 256 TYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFL-------------------RNALIEDGVTIDSSKIVEskvG 316
Cdd:PRK05289 27 CVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkykgeptrlvigDNNTIREFVTINRGTVQG---G 103
|
90 100 110
....*....|....*....|....*....|....
gi 495965695 317 AKTTIGpmSH--LRNNTEIGENCRIGNFVEFKNS 348
Cdd:PRK05289 104 GVTRIG--DNnlLMAYVHVAHDCVVGNHVILANN 135
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
256-423 |
8.37e-09 |
|
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: 56.29 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 256 TYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFL-------------------RNALIEDGVTIDSSKiveSKVG 316
Cdd:cd03351 24 CVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkykgeptrleigDNNTIREFVTIHRGT---AQGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 317 AKTTIGpmSH--LRNNTEIGENCRIGNfvefkNSHFGNGSKCAhltyvgdsdvgervnfgcGVVTVNydgknkyrttikD 394
Cdd:cd03351 101 GVTRIG--NNnlLMAYVHVAHDCVIGN-----NVILANNATLA------------------GHVEIG------------D 143
|
170 180
....*....|....*....|....*....
gi 495965695 395 GAFIGSNCNLIAPVTIGENALLAAGSTIT 423
Cdd:cd03351 144 YAIIGGLSAVHQFCRIGRHAMVGGGSGVV 172
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
248-429 |
1.26e-08 |
|
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.
Pssm-ID: 274656 [Multi-domain] Cd Length: 201 Bit Score: 54.81 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 248 VTILDPDnTYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSflrnaliedgvtidsskIVEskvgakttigpmsHl 327
Cdd:TIGR03570 87 ATLIHPS-AIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGA-----------------IVE-------------H- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 328 rnnteigeNCRIGNFVefknsHFGNGSKCahltyvgdsdvgervnfgCGVVTVNydgknkyrttikDGAFIGSNCNLIAP 407
Cdd:TIGR03570 135 --------DCVIGDFV-----HIAPGVTL------------------SGGVVIG------------EGVFIGAGATIIQG 171
|
170 180
....*....|....*....|..
gi 495965695 408 VTIGENALLAAGSTITDSVDDG 429
Cdd:TIGR03570 172 VTIGAGAIVGAGAVVTKDIPDG 193
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
4-132 |
1.70e-08 |
|
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.
Pssm-ID: 133011 Cd Length: 233 Bit Score: 54.89 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAagkgtRMKSS-LC-KVMHPVLNKPMIGHIIAALRAA-EVDRIIVvvghgANSVKEylQDD--VEYALQE---PQL 75
Cdd:cd02518 2 AIIQA-----RMGSTrLPgKVLKPLGGKPLLEHLLDRLKRSkLIDEIVI-----ATSTNE--EDDplEALAKKLgvkVFR 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495965695 76 GTGHAVMQ--AKALAEEDGDTII-VNGDGPCIQ----KETILKAFAANQNYACTVLTSVLADGE 132
Cdd:cd02518 70 GSEEDVLGryYQAAEEYNADVVVrITGDCPLIDpeiiDAVIRLFLKSGADYTSNTLPRTYPDGL 133
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
261-430 |
1.78e-08 |
|
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: 54.34 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 261 DVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFlrnalIEDGVTIdsskiveskvGAKTTIGPMSHLRNNTEIGENCRIG 340
Cdd:cd03352 1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVV-----IGDGVVI----------GDDCVIHPNVTIYEGCIIGDRVIIH 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 341 N----------FVEFKNSHFgngsKCAHLTYVgdsDVGERVNFGCGVvTVNydgknkyR-----TTIKDGA--------- 396
Cdd:cd03352 66 SgavigsdgfgFAPDGGGWV----KIPQLGGV---IIGDDVEIGANT-TID-------RgalgdTVIGDGTkidnlvqia 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495965695 397 ---FIGSNCnLIA-------PVTIGENALLAAGSTITDSVDDGD 430
Cdd:cd03352 131 hnvRIGENC-LIAaqvgiagSTTIGDNVIIGGQVGIAGHLTIGD 173
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
330-429 |
2.71e-08 |
|
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: 51.69 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 330 NTEIGENCRIGNfvefkNSHFGNGSKCahltyvgdsDVGERVNFG--CGVVTVNYDGKNKYR----------TTIKDGAF 397
Cdd:cd04647 1 NISIGDNVYIGP-----GCVISAGGGI---------TIGDNVLIGpnVTIYDHNHDIDDPERpieqgvtsapIVIGDDVW 66
|
90 100 110
....*....|....*....|....*....|..
gi 495965695 398 IGSNCNLIAPVTIGENALLAAGSTITDSVDDG 429
Cdd:cd04647 67 IGANVVILPGVTIGDGAVVGAGSVVTKDVPPN 98
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
1-131 |
3.45e-08 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 54.05 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKSAIVLAAgkgtRMKSS-L-CKVMHPVLNKPMIGHIIAALRAAE-VDRIIVvvghgANSVKEylQDD--VEYAlqePQL 75
Cdd:COG1861 2 MKIVAIIQA----RMGSTrLpGKVLKPLGGKPVLEHVIERLKRSKlIDEVVV-----ATTTDP--ADDplVDLA---KEL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495965695 76 G----TGHA--VMQ--AKALAEEDGDTII-VNGDGPCIQKETI---LKAFAANQN-YACTVLTSVLADG 131
Cdd:COG1861 68 GvpvfRGSEddVLSryYQAAEAYGADVVVrITGDCPLIDPALIdelIAAFLESGAdYVSNSLPRTYPRG 136
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
258-431 |
4.18e-08 |
|
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: 53.18 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 258 IDADVEIGEDTTIYPNVHLQGNTKIGSHVTilpnsflrnalIEDGVTIdsskiveskvGAKTTIGPMSHLRNNTEIGENC 337
Cdd:cd03352 4 IGENVSIGPNAVIGEGVVIGDGVVIGPGVV-----------IGDGVVI----------GDDCVIHPNVTIYEGCIIGDRV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 338 RIGN----------FVEFKNSHFgngsKCAHLTYVgdsDVGERVNFGCGvvtvnydgknkyrTTIKDGAF----IGSNC- 402
Cdd:cd03352 63 IIHSgavigsdgfgFAPDGGGWV----KIPQLGGV---IIGDDVEIGAN-------------TTIDRGALgdtvIGDGTk 122
|
170 180 190
....*....|....*....|....*....|....
gi 495965695 403 --NL--IAP-VTIGENALLAAGSTITDSVDDGDM 431
Cdd:cd03352 123 idNLvqIAHnVRIGENCLIAAQVGIAGSTTIGDN 156
|
|
| LpxA |
COG1043 |
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
256-423 |
4.73e-08 |
|
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: 53.87 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 256 TYIDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPN----------------SFLR---NALIEDGVTIDSSKIVEskvG 316
Cdd:COG1043 26 CVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFasigeepqdlkykgepTRLEigdNNTIREFVTIHRGTVQG---G 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 317 AKTTIGpmSH--LRNNTEIGENCRIGNFVefknsHFGNGSKCAhltyvgdsdvgervnfgcGVVTVNydgknkyrttikD 394
Cdd:COG1043 103 GVTRIG--DDnlLMAYVHVAHDCVVGNNV-----ILANNATLA------------------GHVEVG------------D 145
|
170 180
....*....|....*....|....*....
gi 495965695 395 GAFIGSNCNLIAPVTIGENALLAAGSTIT 423
Cdd:COG1043 146 HAIIGGLSAVHQFVRIGAHAMVGGGSGVV 174
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
270-433 |
1.01e-07 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 52.72 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 270 IYPNVHLQGNTKIGSHVTILPNSFlrnalIEDGVTIdsskiveskvGAKTTIGPMSHLRNNTEIGENCRIgnfvefknsH 349
Cdd:PRK12461 2 IHPTAVIDPSAKLGSGVEIGPFAV-----IGANVEI----------GDGTWIGPHAVILGPTRIGKNNKI---------H 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 350 FGN--GSKCAHLTYVGDS---DVGERVNFGCGVvTVNYDGKNKYRTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTITD 424
Cdd:PRK12461 58 QGAvvGDEPQDFTYKGEEsrlEIGDRNVIREGV-TIHRGTKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAG 136
|
....*....
gi 495965695 425 SVDDGDMGI 433
Cdd:PRK12461 137 HVTVGDRAI 145
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
4-100 |
1.07e-07 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 52.26 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDDVEYALQEPQ------ 74
Cdd:cd02507 3 AVVLADGFGSRFLpltSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMivdvit 82
|
90 100 110
....*....|....*....|....*....|..
gi 495965695 75 ------LGTGHAVMQAKALaeEDGDTIIVNGD 100
Cdd:cd02507 83 sdlcesAGDALRLRDIRGL--IRSDFLLLSCD 112
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
4-115 |
3.55e-07 |
|
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: 50.91 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRMKSSLCKVMHPVLNKPMIGHIIAALRAA-EVDRIIVVVGhgansvkeylQDDVEYALQEP-----QLGT 77
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASpVVDRIVVAVS----------PDDTPEFRQLLgdpsiQLVA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495965695 78 G-----HAVMQA-KALAEEDGDTIIVNGDGPCIQKETILKAFAA 115
Cdd:pfam01128 71 GgdtrqDSVLNGlKALAGTAKFVLVHDGARPCLPHADLARLLAA 114
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
3-123 |
9.46e-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: 49.04 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 3 SAIVLAAGKGTRMKSSlcKVMHPVLNKPMIGHIIAALRAAeVDRIIVVvghgANSVKEYLQDDVEYaLQEPQLGTG---- 78
Cdd:COG0746 6 TGVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLRPQ-VDEVVIV----ANRPERYAALGVPV-VPDDPPGAGplag 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 495965695 79 -HAVMQAkalAEEDgDTIIVNGDGPCIQKETI--LKAfAANQNYACTV 123
Cdd:COG0746 78 iLAALEA---APAE-WVLVLACDMPFLPPDLVrrLLE-ALEEGADAVV 120
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
4-189 |
1.43e-06 |
|
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: 49.56 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAG--KGTRMKS---SLCKVMHPVLNKPMIGHIIAALraAEVDRI--IVVVGHGANSV--------KEYLQDDVEY 68
Cdd:cd06428 1 AVILVGGpqKGTRFRPlslDVPKPLFPVAGKPMIHHHIEAC--AKVPDLkeVLLIGFYPESVfsdfisdaQQEFNVPIRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 69 aLQEPQ-LGTGHAVMQAKALAEEDG--DTIIVNGDGPCIQKETILKAFAANQNYACTVL-TSVLAD-GERYGRIVRNRD- 142
Cdd:cd06428 79 -LQEYKpLGTAGGLYHFRDQILAGNpsAFFVLNADVCCDFPLQELLEFHKKHGASGTILgTEASREqASNYGCIVEDPSt 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495965695 143 GMVEKIVEAKDCSAEELaikeINTGIFCFKTSkLFDGLKEITTNNAQ 189
Cdd:cd06428 158 GEVLHYVEKPETFVSDL----INCGVYLFSPE-IFDTIKKAFQSRQQ 199
|
|
| LbH_SAT |
cd03354 |
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
350-429 |
1.87e-06 |
|
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.
Pssm-ID: 100045 [Multi-domain] Cd Length: 101 Bit Score: 46.28 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 350 FGNGSKCAHLTYV---GDSDVGERVNFGCGVVT-VNYDGKNKYRTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTITDS 425
Cdd:cd03354 11 IGPGLFIDHGTGIvigETAVIGDNCTIYQGVTLgGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD 90
|
....
gi 495965695 426 VDDG 429
Cdd:cd03354 91 VPAN 94
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
257-341 |
3.53e-06 |
|
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: 44.93 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 257 YIDADVEIGEDTTIYPNVhlqgntkIGSHVTILPNSFLRNALIEDGVTIDS-SKIVESKVGAKTTIGPMSHLRNNTEIGE 335
Cdd:cd03356 1 LIGESTVIGENAIIKNSV-------IGDNVRIGDGVTITNSILMDNVTIGAnSVIVDSIIGDNAVIGENVRVVNLCIIGD 73
|
....*.
gi 495965695 336 NCRIGN 341
Cdd:cd03356 74 DVVVED 79
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
351-423 |
5.81e-06 |
|
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: 44.16 E-value: 5.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495965695 351 GNGSKCAHLTYVGD-SDVGERVNFGCGVVTVNYDGKNKYR-TTIKDGAFIGSNCNLIAPVTIGENALLAAGSTIT 423
Cdd:cd00208 4 GEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGPNEKNpTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
3-53 |
6.18e-06 |
|
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: 46.41 E-value: 6.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 495965695 3 SAIVLAAGKGTRMKSSlcKVMHPVLNKPMIGHIIAALRAAeVDRIIVVVGH 53
Cdd:cd02503 2 TGVILAGGKSRRMGGD--KALLELGGKPLLEHVLERLKPL-VDEVVISANR 49
|
|
| LbH_XAT |
cd03349 |
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
312-426 |
1.63e-05 |
|
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: 44.46 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 312 ESKVGAKTTIGPM--SHLRNNTEIGENCRIGNFVefknsHFGNGSKcaHLTYVGDSDVGERVNFGCGVVTVNYDGKNKYR 389
Cdd:cd03349 1 NISVGDYSYGSGPdcDVGGDKLSIGKFCSIAPGV-----KIGLGGN--HPTDWVSTYPFYIFGGEWEDDAKFDDWPSKGD 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 495965695 390 TTIKDGAFIGSNCnLIAP-VTIGENALLAAGSTITDSV 426
Cdd:cd03349 74 VIIGNDVWIGHGA-TILPgVTIGDGAVIAAGAVVTKDV 110
|
|
| LbH_unknown |
cd05635 |
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
299-388 |
2.29e-05 |
|
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: 43.03 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 299 IEDGVTIDSSKIVESKV--GAKTTIGPMSHLRNNTEIGENCRIGNFVEfkNSHFGNGSKCAHLTYVGDSDVGERVNFGCG 376
Cdd:cd05635 14 IGKDAVIEPFAVIEGPVyiGPGSRVKMGARIYGNTTIGPTCKIGGEVE--DSIIEGYSNKQHDGFLGHSYLGSWCNLGAG 91
|
90
....*....|..
gi 495965695 377 vvTVNYDGKNKY 388
Cdd:cd05635 92 --TNNSDLKNNY 101
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
263-423 |
2.38e-05 |
|
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.
Pssm-ID: 100051 [Multi-domain] Cd Length: 153 Bit Score: 44.32 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 263 EIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNaliedgvtiDSSKIveskvgaktTIGpmshlrNNTEIGENCRIgnf 342
Cdd:cd04645 1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRG---------DVNPI---------RIG------ERTNIQDGSVL--- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 343 vefknshfgngskcaHLTYVGDSDVGERVNFGCGVVTvnydgknkYRTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTI 422
Cdd:cd04645 54 ---------------HVDPGYPTIIGDNVTVGHGAVL--------HGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLV 110
|
.
gi 495965695 423 T 423
Cdd:cd04645 111 P 111
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-143 |
3.27e-05 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 45.11 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKSAIVLAAgkgtRMKSS-L-CKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHgansvkeylqDDVEYALQEpqLGtG 78
Cdd:PRK05450 1 MKFLIIIPA----RYASTrLpGKPLADIGGKPMIVRVYERASKAGADRVVVATDD----------ERIADAVEA--FG-G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 79 HAVMQAKA-------LAE------EDGDTIIVN--GDGPCIQKETI--LKAFAANQNYACTVLTSVLADGERYGR----- 136
Cdd:PRK05450 64 EVVMTSPDhpsgtdrIAEaaaklgLADDDIVVNvqGDEPLIPPEIIdqVAEPLANPEADMATLAVPIHDAEEAFNpnvvk 143
|
....*..
gi 495965695 137 IVRNRDG 143
Cdd:PRK05450 144 VVLDADG 150
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-100 |
6.82e-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: 43.80 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 4 AIVLAAGKGTRM---KSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVV---------GHGANSVKEYLQDDVEY--A 69
Cdd:cd04198 3 AVILAGGGGSRLyplTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqaeisTYLRSFPLNLKQKLDEVtiV 82
|
90 100 110
....*....|....*....|....*....|.
gi 495965695 70 LQEPqLGTGHAVMqaKALAEEDGDTIIVNGD 100
Cdd:cd04198 83 LDED-MGTADSLR--HIRKKIKKDFLVLSCD 110
|
|
| LbH_THP_succinylT |
cd03350 |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
318-444 |
8.55e-05 |
|
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: 42.37 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 318 KTTIGPMSHLRNNTEIGENCRI--GNFVEFkNSHFGNGSKCAHLTYVGD-SDVGERVNFGCGVV---TVNYDGKNKyrTT 391
Cdd:cd03350 1 GRRVPPGAIIRDGAFIGPGAVLmmPSYVNI-GAYVDEGTMVDSWATVGScAQIGKNVHLSAGAViggVLEPLQATP--VI 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 495965695 392 IKDGAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDGDmgiaRSRQSIKKGY 444
Cdd:cd03350 78 IEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYD----RETGEIYYGR 126
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
258-335 |
1.04e-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: 40.64 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 258 IDADVEIGEDTTIYPNVhLQGNTKIGSHVTIlPNSFL-RNALIEDGVTIDSSKIVES-KVGAKTTIGPMSHLRNNTEIGE 335
Cdd:cd05787 2 IGRGTSIGEGTTIKNSV-IGRNCKIGKNVVI-DNSYIwDDVTIEDGCTIHHSIVADGaVIGKGCTIPPGSLISFGVVIGD 79
|
|
| LbH_gamma_CA |
cd00710 |
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
264-354 |
2.52e-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: 41.46 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 264 IGEDTTIYPNVHLQGNTKIGSHVTILPNSFLR-----------NALIEDGVTIDSSKIVESKVGAKTTIGPMSHLRNNTE 332
Cdd:cd00710 5 IDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRadegtpiiigaNVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVHGPAY 84
|
90 100
....*....|....*....|...
gi 495965695 333 IGENCRIG-NFVEFkNSHFGNGS 354
Cdd:cd00710 85 IGDNCFIGfRSVVF-NAKVGDNC 106
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
305-422 |
4.16e-04 |
|
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: 42.03 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 305 IDSSKIVES--KVGAKTTIGPMSHLRNNTEIGENCRIGNFVEF-------KNSHFGN----GSKCAHLTYVGDS---DVG 368
Cdd:cd03351 2 IHPTAIVDPgaKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIdgpttigKNNRIFPfasiGEAPQDLKYKGEPtrlEIG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495965695 369 ERVNFGCGvVTVNydgknkyRTTIKDGAF--IGSNCNLIAPV------TIGENALLAAGSTI 422
Cdd:cd03351 82 DNNTIREF-VTIH-------RGTAQGGGVtrIGNNNLLMAYVhvahdcVIGNNVILANNATL 135
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-63 |
5.09e-04 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon 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 epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 41.44 E-value: 5.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495965695 4 AIVLAAGKGTRMK---SSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQ 63
Cdd:cd04197 3 AVVLADSFNRRFRpltKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIE 65
|
|
| PRK10502 |
PRK10502 |
putative acyl transferase; Provisional |
391-427 |
6.56e-04 |
|
putative acyl transferase; Provisional
Pssm-ID: 236703 [Multi-domain] Cd Length: 182 Bit Score: 40.70 E-value: 6.56e-04
10 20 30
....*....|....*....|....*....|....*...
gi 495965695 391 TIKDGAFIGSNCnLIAP-VTIGENALLAAGSTITDSVD 427
Cdd:PRK10502 126 VIGEGCWLAADV-FVAPgVTIGSGAVVGARSSVFKSLP 162
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
261-288 |
1.09e-03 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 36.16 E-value: 1.09e-03
10 20
....*....|....*....|....*...
gi 495965695 261 DVEIGEDTTIYPNVHLQGNTKIGSHVTI 288
Cdd:pfam00132 1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
3-50 |
1.24e-03 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 39.78 E-value: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 495965695 3 SAIVLAAGKGTRMKSSlCKVMHPVLNKPMIGHIIAALRaAEVDRIIVV 50
Cdd:PRK00317 5 TGVILAGGRSRRMGGV-DKGLQELNGKPLIQHVIERLA-PQVDEIVIN 50
|
|
| LbH_wcaF_like |
cd05825 |
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
391-429 |
1.30e-03 |
|
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.
Pssm-ID: 100063 [Multi-domain] Cd Length: 107 Bit Score: 38.36 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 495965695 391 TIKDGAFIGSNCnLIAP-VTIGENALLAAGSTITDSVDDG 429
Cdd:cd05825 58 VIGDGAWVAAEA-FVGPgVTIGEGAVVGARSVVVRDLPAW 96
|
|
| LbH_FBP |
cd04650 |
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ... |
251-340 |
1.36e-03 |
|
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.
Pssm-ID: 100055 [Multi-domain] Cd Length: 154 Bit Score: 39.09 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 251 LDPdNTYIDADVEIGEDTTIYPNVHLQGNT---KIGSHVTILPNSFLRNAL-----IEDGVTIDSSKIVE-SKVGAKTTI 321
Cdd:cd04650 9 VHP-TSYVIGDVVIGELTSVWHYAVIRGDNdsiYIGKYSNVQENVSIHTDHgypteIGDYVTIGHNAVVHgAKVGNYVIV 87
|
90
....*....|....*....
gi 495965695 322 GPMSHLRNNTEIGENCRIG 340
Cdd:cd04650 88 GMGAILLNGAKIGDHVIIG 106
|
|
| LbH_M1P_guanylylT_C |
cd05824 |
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
258-341 |
1.50e-03 |
|
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 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: 100062 [Multi-domain] Cd Length: 80 Bit Score: 37.52 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 258 IDADVEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEDGVTIDSskiveSKVGAKTTIGPMSHLRNNTEIGENC 337
Cdd:cd05824 2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKS-----SIVGWNSTVGRWTRLENVTVLGDDV 76
|
....
gi 495965695 338 RIGN 341
Cdd:cd05824 77 TIKD 80
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
1-67 |
1.52e-03 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 40.27 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 1 MKSAIVLAAGKGTRM---KSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLQDDVE 67
Cdd:PRK13389 8 VKKAVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFE 77
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
4-71 |
1.67e-03 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 40.26 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495965695 4 AIVLAAGKGTRM---KSSLCKVMHPVLNKPMIGHIIAALRAAEVDRIIVVVGHGANSVKEYLqdDVEYALQ 71
Cdd:PRK10122 6 AVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHF--DTSYELE 74
|
|
| dapD |
PRK11830 |
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional |
390-425 |
3.74e-03 |
|
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
Pssm-ID: 236996 [Multi-domain] Cd Length: 272 Bit Score: 39.02 E-value: 3.74e-03
10 20 30
....*....|....*....|....*....|....*.
gi 495965695 390 TTIKDGAFIGSNCNLIAPVTIGENALLAAGSTITDS 425
Cdd:PRK11830 177 VIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQS 212
|
|
| LbH_paaY_like |
cd04745 |
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
263-340 |
3.75e-03 |
|
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.
Pssm-ID: 100058 [Multi-domain] Cd Length: 155 Bit Score: 37.73 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 263 EIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRN----ALIEDGVTIDSSKIVESKVGAKTTIGPMSHLRNNT-----EI 333
Cdd:cd04745 2 VVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGdfgrIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAilhgcTI 81
|
....*..
gi 495965695 334 GENCRIG 340
Cdd:cd04745 82 GRNALVG 88
|
|
| LbH_MAT_GAT |
cd03357 |
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
391-429 |
3.84e-03 |
|
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100047 [Multi-domain] Cd Length: 169 Bit Score: 38.17 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|....*....
gi 495965695 391 TIKDGAFIGSNCNLIAPVTIGENALLAAGSTITDSVDDG 429
Cdd:cd03357 120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPAN 158
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
262-341 |
4.57e-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: 36.07 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965695 262 VEIGEDTTIYPNVHLQGNTKIGSHVTILPNSFLRNALIEdgvTIDSSKIVE--SKVGAKTTIGPmshlrnNTEIGENCRI 339
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGP---NEKNPTIIGdnVEIGANAVIHG------GVKIGDNAVI 71
|
..
gi 495965695 340 GN 341
Cdd:cd00208 72 GA 73
|
|
| DapD |
COG2171 |
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ... |
389-425 |
5.03e-03 |
|
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: 38.56 E-value: 5.03e-03
10 20 30
....*....|....*....|....*....|....*..
gi 495965695 389 RTTIKDGAFIGSNCNLIAPVTIGENALLAAGSTITDS 425
Cdd:COG2171 170 PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAS 206
|
|
| Hexapep |
pfam00132 |
Bacterial transferase hexapeptide (six repeats); |
313-341 |
5.53e-03 |
|
Bacterial transferase hexapeptide (six repeats);
Pssm-ID: 459684 [Multi-domain] Cd Length: 30 Bit Score: 34.23 E-value: 5.53e-03
10 20
....*....|....*....|....*....
gi 495965695 313 SKVGAKTTIGPMSHLRNNTEIGENCRIGN 341
Cdd:pfam00132 2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
|
|
| Hexapep_2 |
pfam14602 |
Hexapeptide repeat of succinyl-transferase; |
390-423 |
7.30e-03 |
|
Hexapeptide repeat of succinyl-transferase;
Pssm-ID: 434064 [Multi-domain] Cd Length: 33 Bit Score: 33.95 E-value: 7.30e-03
10 20 30
....*....|....*....|....*....|....
gi 495965695 390 TTIKDGAFIGSNCnlIAPVTIGENALLAAGSTIT 423
Cdd:pfam14602 1 VIIGDNCLIGANS--GIGVSLGDNCVVGAGVVIT 32
|
|
| |
