|
Name |
Accession |
Description |
Interval |
E-value |
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-456 |
0e+00 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 728.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 3 KPKITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQQLGT 82
Cdd:PRK14356 3 ASTTGALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVLQEQQLGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 83 GHALQVAWDAVKADGTDYCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTITPRDTAQFGRVVRdENQRISAIVEAKDYC 162
Cdd:PRK14356 83 GHALQCAWPSLTAAGLDRVLVVNGDTPLVTTDTIDDFLKEAAGADLAFMTLTLPDPGAYGRVVR-RNGHVAAIVEAKDYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 163 MAVHGPVTGEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIRAES 242
Cdd:PRK14356 162 EALHGPETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLVGLAVAEGMNVLGVNCGEDPNLLGVNTPAELVRSEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 243 ELRRRIVEAHIDRGVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGCVVREFCHIEG 322
Cdd:PRK14356 242 LLRARIVEKHLESGVLIHAPESVRIGPRATIEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVVSSGATIHSFSHLEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 323 AEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFTTTI 402
Cdd:PRK14356 322 AEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNKHRTVI 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 503281339 403 GPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNIHRRLK 456
Cdd:PRK14356 402 GEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIARGRQKNLPRKKK 455
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
5-457 |
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: 604.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 5 KITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQQLGTGH 84
Cdd:COG1207 2 PLAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVEFVLQEEQLGTGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 85 ALQVAWDAVKADgTDYCLVINGDTPLITAEGLGRL--AGQAGCCDLAFMTITPRDTAQFGRVVRDENQRISAIVEAKDYC 162
Cdd:COG1207 82 AVQQALPALPGD-DGTVLVLYGDVPLIRAETLKALlaAHRAAGAAATVLTAELDDPTGYGRIVRDEDGRVLRIVEEKDAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 163 M---AVHgpvtgEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIR 239
Cdd:COG1207 161 EeqrAIR-----EINTGIYAFDAAALREALPKLSNDNAQGEYYLTDVIAIARADGLKVAAVQPEDPWEVLGVNDRVQLAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 240 AESELRRRIVEAHIDRGVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGCVVReFCH 319
Cdd:COG1207 236 AERILQRRIAERLMRAGVTIIDPATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIK-YSV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 320 IEGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFT 399
Cdd:COG1207 315 IEDAVVGAGATVGPFARLRPGTVLGEGVKIGNFVEVKNSTIGEGSKVNHLSYIGDAEIGEGVNIGAGTITCNYDGVNKHR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503281339 400 TTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI---HRRLKK 457
Cdd:COG1207 395 TVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNIegwVRPKKK 455
|
|
| glmU |
TIGR01173 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ... |
8-451 |
5.70e-171 |
|
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: 487.94 E-value: 5.70e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQQLGTGHALQ 87
Cdd:TIGR01173 3 VVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAARALGPQKIHVVYGHGAEQVRKALANRDVNWVLQAEQLGTGHAVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 88 VAWDAVKADGtdYCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTITPRDTAQFGRVVRDENQRISAIVEAKDyCMAVHG 167
Cdd:TIGR01173 83 QALPFLSDDG--DVLVLYGDVPLISAETLERLLEAHRQNGITLLTAKLDDPTGYGRIIRENDGKVTAIVEDKD-ANAEQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 168 PVTgEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIRAESELRRR 247
Cdd:TIGR01173 160 AIK-EINTGVYVFDGAALKRWLPKLSNNNAQGEYYLTDVIALAVADGETVRAVQVDDSDEVLGVNDRLQLAQLERILQRR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 248 IVEAHIDRGVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGCVVREFCHIEGAEVGP 327
Cdd:TIGR01173 239 IAKKLLLAGVTLRDPARFDIRGTVEIGRDVEIDPNVILEGKVKIGDDVVIGPGCVIKNSVIGSNVVIKAYSVLEGSEIGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 328 QAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFTTTIGPGAF 407
Cdd:TIGR01173 319 GCDVGPFARLRPGSVLGAGVHIGNFVEVKNARIGKGSKAGHLSYLGDAEIGSNVNIGAGTITCNYDGANKHKTIIGDGVF 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 503281339 408 IGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI 451
Cdd:TIGR01173 399 IGSNTQLVAPVKVGDGATIAAGSTVTKDVPEGALAISRARQRNI 442
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-458 |
4.74e-155 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 447.36 E-value: 4.74e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 7 TALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAgQFVLQAQQLGTGHAL 86
Cdd:PRK14354 4 YAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRS-EFALQEEQLGTGHAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 87 QVAWDAVK-ADGTdyCLVINGDTPLITAEGLGRL-----AGQAGCCDLafmTITPRDTAQFGRVVRDENQRISAIVEAKD 160
Cdd:PRK14354 83 MQAEEFLAdKEGT--TLVICGDTPLITAETLKNLidfheEHKAAATIL---TAIAENPTGYGRIIRNENGEVEKIVEQKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 161 ---YCMAVHgpvtgEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPREL 237
Cdd:PRK14354 158 ateEEKQIK-----EINTGTYCFDNKALFEALKKISNDNAQGEYYLTDVIEILKNEGEKVGAYQTEDFEESLGVNDRVAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 238 IRAESELRRRIVEAHIDRGVLIHNPET------VIIGPRVAVEPGAEIFGHCEIyGASSVaagsrLGSYTHITDSTFAPG 311
Cdd:PRK14354 233 AEAEKVMRRRINEKHMVNGVTIIDPEStyidadVEIGSDTVIEPGVVIKGNTVI-GEDCV-----IGPGSRIVDSTIGDG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 312 CVVReFCHIEGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCN 391
Cdd:PRK14354 307 VTIT-NSVIEESKVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIKKSTIGEGTKVSHLTYIGDAEVGENVNIGCGTITVN 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503281339 392 YDGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI-----HRRLKKS 458
Cdd:PRK14354 386 YDGKNKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKegyvkKLPHKKK 457
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-450 |
6.51e-151 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 436.60 E-value: 6.51e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 1 MTKPKITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQF--VLQAQ 78
Cdd:PRK14353 1 MTDRTCLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAeiFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 79 QLGTGHALQVAWDAVkADGTDYCLVINGDTPLITAEGLGRL-AGQAGCCDLAFMTITPRDTAQFGRVVRDeNQRISAIVE 157
Cdd:PRK14353 81 RLGTAHAVLAAREAL-AGGYGDVLVLYGDTPLITAETLARLrERLADGADVVVLGFRAADPTGYGRLIVK-GGRLVAIVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 158 AKD---------YCmavhgpvtgevNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDiSL 228
Cdd:PRK14353 159 EKDasdeeraitLC-----------NSGVMAADGADALALLDRVGNDNAKGEYYLTDIVAIARAEGLRVAVVEAPED-EV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 229 MGINSPRELIRAESELRRRIVEAHIDRGVLIHNPETV------IIGPRVAVEPGAeIFGhceiygassvaagsrlgsyth 302
Cdd:PRK14353 227 RGINSRAELAEAEAVWQARRRRAAMLAGVTLIAPETVffsydtVIGRDVVIEPNV-VFG--------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 303 iTDSTFAPGCVVREFCHIEGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGAN 382
Cdd:PRK14353 285 -PGVTVASGAVIHAFSHLEGAHVGEGAEVGPYARLRPGAELGEGAKVGNFVEVKNAKLGEGAKVNHLTYIGDATIGAGAN 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503281339 383 IGAGTITCNYDGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVN 450
Cdd:PRK14353 364 IGAGTITCNYDGFNKHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQET 431
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
10-451 |
2.14e-127 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 376.96 E-value: 2.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 10 VLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAG-QFVLQAQQLGTGHALQV 88
Cdd:PRK14360 6 ILAAGKGTRMKSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPGlEFVEQQPQLGTGHAVQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 89 AWDAVKaDGTDYCLVINGDTPLITAEGLGRLAG--QAGCCDLAFMTITPRDTAQFGRVVRDENQRISAIVEAKDyCmavh 166
Cdd:PRK14360 86 LLPVLK-GFEGDLLVLNGDVPLLRPETLEALLNthRSSNADVTLLTARLPNPKGYGRVFCDGNNLVEQIVEDRD-C---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 167 gpvTGE------VNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLaVASAMAVEsVQCGDDISlmGINSPRELIRA 240
Cdd:PRK14360 160 ---TPAqrqnnrINAGIYCFNWPALAEVLPKLSSNNDQKEYYLTDTVSL-LDPVMAVE-VEDYQEIN--GINDRKQLAQC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 241 ESELRRRIVEAHIDRGVLIHNP------ETVIIGPRVAVEPGAEIFGHCEIygassvAAGSRLGSYTHITDSTFAPGCVV 314
Cdd:PRK14360 233 EEILQNRIKEKWMLAGVTFIDPasctisETVELGPDVIIEPQTHLRGNTVI------GSGCRIGPGSLIENSQIGENVTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 315 ReFCHIEGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDG 394
Cdd:PRK14360 307 L-YSVVSDSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQLGEGSKVNHLSYIGDATLGEQVNIGAGTITANYDG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 503281339 395 KNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI 451
Cdd:PRK14360 386 VKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-457 |
8.43e-127 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 375.52 E-value: 8.43e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 1 MTKPKITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQQL 80
Cdd:PRK09451 1 MLNSAMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEPLNWVLQAEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 81 GTGHALQVAwDAVKADGTDyCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTITPRDTAQFGRVVRdENQRISAIVEAKD 160
Cdd:PRK09451 81 GTGHAMQQA-APFFADDED-ILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDNPTGYGRITR-ENGKVVGIVEQKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 161 ycMAVHGPVTGEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIRA 240
Cdd:PRK09451 158 --ATDEQRQIQEINTGILVANGADLKRWLAKLTNNNAQGEYYITDIIALAHQEGREIVAVHPQRLSEVEGVNNRLQLARL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 241 ESELRRRIVEAHIDRGVLIHNPE------TVIIGPRVAVEPGAEIFGHceiygassVAAGSR--LGSYTHITDSTFAPGC 312
Cdd:PRK09451 236 ERVYQAEQAEKLLLAGVMLRDPArfdlrgTLTHGRDVEIDTNVIIEGN--------VTLGNRvkIGAGCVLKNCVIGDDC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 313 VVREFCHIEGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNY 392
Cdd:PRK09451 308 EISPYSVVEDANLGAACTIGPFARLRPGAELAEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503281339 393 DGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI---HRRLKK 457
Cdd:PRK09451 388 DGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIqgwQRPVKK 455
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-451 |
7.75e-126 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 372.94 E-value: 7.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPlFGQAAITVVGHGSGLVEQAFPEMAgQFVLQAQQLGTGHALQ 87
Cdd:PRK14357 3 ALVLAAGKGTRMKSKIPKVLHKISGKPMINWVIDTAKK-VAQKVGVVLGHEAELVKKLLPEWV-KIFLQEEQLGTAHAVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 88 VAWDAVKADgtDYCLVINGDTPLITAEGLGRLAGQ--AGCCDLAFMTITPRDTAQFGRVVRDENQriSAIVEAKDYCMAV 165
Cdd:PRK14357 81 CARDFIEPG--DDLLILYGDVPLISENTLKRLIEEhnRKGADVTILVADLEDPTGYGRIIRDGGK--YRIVEDKDAPEEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 166 HGPVtgEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAvasaMAVESVQCGDDISLMGINSPRELIRAESELR 245
Cdd:PRK14357 157 KKIK--EINTGIYVFSGDFLLEVLPKIKNENAKGEYYLTDAVNFA----EKVRVVKTEDLLEITGVNTRIQLAWLEKQLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 246 RRIVEAHIDRGVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGC-VVREFChiEGAE 324
Cdd:PRK14357 231 MRILEELMENGVTILDPNTTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVkIIRSEC--EKSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 325 VGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFTTTIGP 404
Cdd:PRK14357 309 IEDDVSVGPFSRLREGTVLKKSVKIGNFVEIKKSTIGENTKAQHLTYLGDATVGKNVNIGAGTITCNYDGKKKNPTFIED 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 503281339 405 GAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI 451
Cdd:PRK14357 389 GAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-450 |
6.41e-122 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 363.29 E-value: 6.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 5 KITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAG-QFVLQAQQLGTG 83
Cdd:PRK14355 3 NLAAIILAAGKGTRMKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDvSFALQEEQLGTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 84 HALQVAWDAVkADGTDYCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTITPRDTAQFG--RVVRDENQRISAIVEAKDY 161
Cdd:PRK14355 83 HAVACAAPAL-DGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAAVTVLTARLENPFGygRIVRDADGRVLRIVEEKDA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 162 CMAVHGpvTGEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIRAE 241
Cdd:PRK14355 162 TPEERS--IREVNSGIYCVEAAFLFDAIGRLGNDNAQGEYYLTDIVAMAAAEGLRCLAFPVADPDEIMGVNDRAQLAEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 242 SELRRRIVEAHIDRGVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGCVVREFCHIE 321
Cdd:PRK14355 240 RVLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 322 GAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFTTT 401
Cdd:PRK14355 320 DSVVGDDVAIGPMAHLRPGTELSAHVKIGNFVETKKIVMGEGSKASHLTYLGDATIGRNVNIGCGTITCNYDGVKKHRTV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 503281339 402 IGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVN 450
Cdd:PRK14355 400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVN 448
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-451 |
7.42e-121 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 361.18 E-value: 7.42e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQF--VLQAQQLGTGHA 85
Cdd:PRK14352 7 VIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEVdiAVQDEQPGTGHA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 86 LQVAWDAVKADGTDYCLVINGDTPLITAEGLGRLAG--QAGCCDLAFMTITPRDTAQFGRVVRDENQRISAIVEAKDYC- 162
Cdd:PRK14352 87 VQCALEALPADFDGTVVVTAGDVPLLDGETLADLVAthTAEGNAVTVLTTTLDDPTGYGRILRDQDGEVTAIVEQKDATp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 163 --MAVHgpvtgEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIRA 240
Cdd:PRK14352 167 sqRAIR-----EVNSGVYAFDAAVLRSALARLSSDNAQGELYLTDVLAIAREAGHRVGAHHADDSAEVAGVNDRVQLAAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 241 ESELRRRIVEAHIDRGVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGCVVREfCHI 320
Cdd:PRK14352 242 GAELNRRIVEAWMRAGVTIVDPATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVR-THG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 321 EGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFTT 400
Cdd:PRK14352 321 SESEIGAGATVGPFTYLRPGTVLGEEGKLGAFVETKNATIGRGTKVPHLTYVGDADIGEHSNIGASSVFVNYDGVNKHRT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI 451
Cdd:PRK14352 401 TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVSEGPQRNI 451
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
6-451 |
6.12e-115 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 346.20 E-value: 6.12e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 6 ITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQQLGTGHA 85
Cdd:PRK14358 8 LDVVILAAGQGTRMKSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAFARQEQQLGTGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 86 LQVAWDAVKADGTDyCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTITPR--DTAQFGRVVRDENQRISAIVEAKDYCM 163
Cdd:PRK14358 88 FLSGASALTEGDAD-ILVLYGDTPLLRPDTLRALVADHRAQGSAMTILTGElpDATGYGRIVRGADGAVERIVEQKDATD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 164 AVHGpvTGEVNAGIYLLRVSSVDtLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPRELIRAESE 243
Cdd:PRK14358 167 AEKA--IGEFNSGVYVFDARAPE-LARRIGNDNKAGEYYLTDLLGLYRAGGAQVRAFKLSDPDEVLGANDRAGLAQLEAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 244 LRRRIVEAHIDRGVLIHNPETVII------GPRVAVEPGAEIFGHceiygaSSVAAGSRLGSYTHITDSTFAPGCVVREF 317
Cdd:PRK14358 244 LRRRINEAHMKAGVTLQDPGTILIedtvtlGRDVTIEPGVLLRGQ------TRVADGVTIGAYSVVTDSVLHEGAVIKPH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 318 CHIEGAEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNK 397
Cdd:PRK14358 318 SVLEGAEVGAGSDVGPFARLRPGTVLGEGVHIGNFVETKNARLDAGVKAGHLAYLGDVTIGAETNVGAGTIVANFDGVNK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 503281339 398 FTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI 451
Cdd:PRK14358 398 HQSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVARGKQRNL 451
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-451 |
2.03e-114 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 342.74 E-value: 2.03e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 5 KITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVydaIKPLFgqaAIT-----VVGHGSGLVEQA----FPEMagQFVL 75
Cdd:PRK14359 2 KLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYI---LKEAF---AISddvhvVLHHQKERIKEAvleyFPGV--IFHT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 76 QAQQ--LGTGHAL-QVAwdaVKADGTdycLVINGDTPLITAEGLGRLAGQAGccDLAFMTITPRDTAQFGRVVRdENQRI 152
Cdd:PRK14359 74 QDLEnyPGTGGALmGIE---PKHERV---LILNGDMPLVEKDELEKLLENDA--DIVMSVFHLADPKGYGRVVI-ENGQV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 153 SAIVEAKDycmavhgpVTGE------VNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQcGDDI 226
Cdd:PRK14359 145 KKIVEQKD--------ANEEelkiksVNAGVYLFDRKLLEEYLPLLKNQNAQKEYYLTDIIALAIEKGETIKAVF-VDEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 227 SLMGINSPRELIRAESELRRRIVEAHIDRGVLIHNPETVIIgprvavEPGAEIFGHCEIYgassvaAGSRLGSYTHITDS 306
Cdd:PRK14359 216 NFMGVNSKFELAKAEEIMQERIKKNAMKQGVIMRLPETIYI------ESGVEFEGECELE------EGVRILGKSKIENS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 307 TFAPGCVVrEFCHIEGAEVGPqavvgpYARLRPGTVLhTGARVGNFVEMKKAVLgEGAKASHLSYLGDAEVGAGANIGAG 386
Cdd:PRK14359 284 HIKAHSVI-EESIIENSDVGP------LAHIRPKSEI-KNTHIGNFVETKNAKL-NGVKAGHLSYLGDCEIDEGTNIGAG 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503281339 387 TITCNYDGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEGGAIARGRQVNI 451
Cdd:PRK14359 355 TITCNYDGKKKHKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAISRAPQKNI 419
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
256-448 |
2.01e-99 |
|
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: 295.87 E-value: 2.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 256 GVLIHNPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTFAPGCVVREFCHIEGAEVGPQAVVGPYA 335
Cdd:cd03353 1 GVTLIDPETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 336 RLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCNYDGKNKFTTTIGPGAFIGSNTALV 415
Cdd:cd03353 81 HLRPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCNYDGVNKHRTVIGDNVFIGSNSQLV 160
|
170 180 190
....*....|....*....|....*....|...
gi 503281339 416 APVTVGRDALVGAGSTITKDVPDEGGAIARGRQ 448
Cdd:cd03353 161 APVTIGDGATIAAGSTITKDVPPGALAIARARQ 193
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
8-237 |
3.17e-80 |
|
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: 248.20 E-value: 3.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQQLGTGHALQ 87
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEEQLGTGHAVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 88 VAWDAVKaDGTDYCLVINGDTPLITAEGLGRL--AGQAGCCDLAFMTITPRDTAQFGRVVRDENQRISAIVEAKDYC--- 162
Cdd:cd02540 81 QALPALK-DFEGDVLVLYGDVPLITPETLQRLleAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVEEKDATeee 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503281339 163 MAVHgpvtgEVNAGIYLLRVSSVDTLLGQLRNENKSGEYYVTDLIGLAVASAMAVESVQCGDDISLMGINSPREL 237
Cdd:cd02540 160 KAIR-----EVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVADGLKVAAVLADDEEEVLGVNDRVQL 229
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
8-432 |
9.38e-62 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 205.91 E-value: 9.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMH---SSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAG-----QFVLQAQQ 79
Cdd:TIGR03992 3 AVILAAGKGTRMRpltETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRggvpiEYVVQEEQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 80 LGTGHALQVAWDAVKadgtDYCLVINGDTpLITAEGLGRLAGQAGccdLAFMTITPRDTAQFGrVVRDENQRISAIVEAK 159
Cdd:TIGR03992 83 LGTADALGSAKEYVD----DEFLVLNGDV-LLDSDLLERLIRAEA---PAIAVVEVDDPSDYG-VVETDGGRVTGIVEKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 160 DYcmavhgPVTGEVNAGIYLLRvSSVDTLLGQLRnENKSGEYYVTDLIGLAVASAM--AVESvqcgdDISLMGINSPREL 237
Cdd:TIGR03992 154 EN------PPSNLINAGIYLFS-PEIFELLEKTK-LSPRGEYELTDALQLLIDEGKvkAVEL-----DGFWLDVGRPWDL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 238 IRAESELRRRIveahidrgvlihnpETVIIGPrvaVEPGAEIFGhceiygasSVAAGSrlgsythitdstfapGCVVREF 317
Cdd:TIGR03992 221 LDANEALLDNL--------------EPRIEGT---VEENVTIKG--------PVVIGE---------------GAVIRSG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 318 CHIEG-AEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTITCN--YDG 394
Cdd:TIGR03992 261 TYIEGpVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFGAGTKVANlrHDD 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 503281339 395 KN---------------KFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTI 432
Cdd:TIGR03992 341 KPvkvtvkgkrvdtgrrKLGAIVGDGVKTGINVSINPGVKIGSGARIYPGEVV 393
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
8-213 |
1.53e-26 |
|
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: 106.51 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRM--HS-SRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAG-----QFVLQAQQ 79
Cdd:cd04181 1 AVILAAGKGTRLrpLTdTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKfgvniEYVVQEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 80 LGTGHALQVAWDAVkadGTDYCLVINGDTplITAEGLGRLAGQAGC--CDLAFMTITPRDTAQFGRVVRDENQRISAIVE 157
Cdd:cd04181 81 LGTAGAVRNAEDFL---GDDDFLVVNGDV--LTDLDLSELLRFHREkgADATIAVKEVEDPSRYGVVELDDDGRVTRFVE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503281339 158 aKDYcmavhGPVTGEVNAGIYLLRvssvDTLLGQLRNENKSGEYYVTDLIGLAVAS 213
Cdd:cd04181 156 -KPT-----LPESNLANAGIYIFE----PEILDYIPEILPRGEDELTDAIPLLIEE 201
|
|
| LbH_G1P_TT_C_like |
cd05636 |
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ... |
309-433 |
7.86e-26 |
|
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100060 [Multi-domain] Cd Length: 163 Bit Score: 103.05 E-value: 7.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 309 APGCVVREFCHIEG-AEVGPQAVVGPYARLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGT 387
Cdd:cd05636 21 GEGAIVRSGAYIEGpVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLGAGT 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503281339 388 ITCNY--DGKN---------------KFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTIT 433
Cdd:cd05636 101 ITANLrfDDKPvkvrlkgervdtgrrKLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
7-181 |
1.35e-20 |
|
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: 90.21 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 7 TALVLAAGKGTRMH---SSRPKVLQTLLGEPMLRYVYDAIKplfgQAAIT----VVGHGSGLVEQAFPEMAG-----QFV 74
Cdd:COG1208 1 KAVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLA----AAGITeiviNVGYLAEQIEEYFGDGSRfgvriTYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 75 LQAQQLGTGHALQVAWDAVkadGTDYCLVINGDTplITAEGLGRL--AGQAGCCDLAFMTITPRDTAQFGRVVRDENQRI 152
Cdd:COG1208 77 DEGEPLGTGGALKRALPLL---GDEPFLVLNGDI--LTDLDLAALlaFHREKGADATLALVPVPDPSRYGVVELDGDGRV 151
|
170 180
....*....|....*....|....*....
gi 503281339 153 SAIVEAKDycmavhGPVTGEVNAGIYLLR 181
Cdd:COG1208 152 TRFVEKPE------EPPSNLINAGIYVLE 174
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
327-446 |
1.50e-15 |
|
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: 74.83 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 327 PQAVVGPYARLRPGTVLHTGARVGNFVEmkkavLGEGAKASHLSYLG-DAEVGAGANIGAGTITCNYdgknkftTTIGPG 405
Cdd:cd03360 89 PSAVVSPSAVIGEGCVIMAGAVINPDAR-----IGDNVIINTGAVIGhDCVIGDFVHIAPGVVLSGG-------VTIGEG 156
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 503281339 406 AFIGSNTALVAPVTVGRDALVGAGSTITKDVPDegGAIARG 446
Cdd:cd03360 157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPD--GSVVVG 195
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
8-183 |
1.07e-14 |
|
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: 72.97 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHS---SRPKVLQTLLGEPMLRYVydaIKPLFGQAA---ITVVGHGSGLVEQAF-----PEMAGQFVLQ 76
Cdd:cd06915 1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYL---LEYLARQGIsriVLSVGYLAEQIEEYFgdgyrGGIRIYYVIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 77 AQQLGTGHALQVAWDAVKadgTDYCLVINGDTPL-ITAEGLGRLAGQAGCcdLAFMTITP-RDTAQFGRVVRDENQRISA 154
Cdd:cd06915 78 PEPLGTGGAIKNALPKLP---EDQFLVLNGDTYFdVDLLALLAALRASGA--DATMALRRvPDASRYGNVTVDGDGRVIA 152
|
170 180
....*....|....*....|....*....
gi 503281339 155 IVEaKDYCmavhgPVTGEVNAGIYLLRVS 183
Cdd:cd06915 153 FVE-KGPG-----AAPGLINGGVYLLRKE 175
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-114 |
1.16e-14 |
|
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: 72.21 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 6 ITALVLAAGKGTRMHssRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQAQ-QLGTGH 84
Cdd:cd04182 1 IAAIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDwEEGMSS 78
|
90 100 110
....*....|....*....|....*....|
gi 503281339 85 ALQVAWDAVKADgTDYCLVINGDTPLITAE 114
Cdd:cd04182 79 SLAAGLEALPAD-ADAVLILLADQPLVTAE 107
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
3-120 |
6.72e-14 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 70.19 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 3 KPKITALVLAAGKGTRMhsSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFVL-QAQQLG 81
Cdd:COG2068 1 MSKVAAIILAAGASSRM--GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVnPDWEEG 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 503281339 82 TGHALQVAWDAVKADgTDYCLVINGDTPLITAEGLGRLA 120
Cdd:COG2068 79 MSSSLRAGLAALPAD-ADAVLVLLGDQPLVTAETLRRLL 116
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
320-446 |
8.14e-14 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 68.36 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 320 IEGAEVGPQAVVGPYARLRPGTVlhtgaRVGNFVemkkaVLGEGAkasHLSYLGDAEVGAGANIGAGTITCN----YDGK 395
Cdd:COG0110 6 LFGARIGDGVVIGPGVRIYGGNI-----TIGDNV-----YIGPGV---TIDDPGGITIGDNVLIGPGVTILTgnhpIDDP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503281339 396 NKFT-----TTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDegGAIARG 446
Cdd:COG0110 73 ATFPlrtgpVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPP--YAIVAG 126
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
8-123 |
1.33e-13 |
|
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: 68.38 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHssRPKVLQTLLGEPMLRYVYDAIKPLFGQaaITVVGhGSGLVEQAFPEMAGQFVLQAQ-QLGTGHAL 86
Cdd:pfam12804 1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAGDE--VVVVA-NDEEVLAALAGLGVPVVPDPDpGQGPLAGL 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 503281339 87 QVAwdAVKADGTDYCLVINGDTPLITAEGLGRLAGQA 123
Cdd:pfam12804 76 LAA--LRAAPGADAVLVLACDMPFLTPELLRRLLAAA 110
|
|
| NeuD_NnaD |
TIGR03570 |
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ... |
325-440 |
1.66e-12 |
|
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: 65.98 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 325 VGPQAVVGPYARLRPGTVLHTGA------RVGNFVemkkaVLGEGAKASHlsylgDAEVGAGANIGAGTITCNYdgknkf 398
Cdd:TIGR03570 90 IHPSAIVSPSASIGEGTVIMAGAvinpdvRIGDNV-----IINTGAIVEH-----DCVIGDFVHIAPGVTLSGG------ 153
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 503281339 399 tTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEG 440
Cdd:TIGR03570 154 -VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGG 194
|
|
| LbH_WxcM_N_like |
cd03358 |
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ... |
349-446 |
6.11e-12 |
|
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: 62.52 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 349 VGNFVE-MKKAVLGEGAKASHLSYLGD-AEVGAGANIGAGTITCN--------YDGKNKFTTTIGPGAFIGSNTALVAPV 418
Cdd:cd03358 7 IGTNVFiENDVKIGDNVKIQSNVSIYEgVTIEDDVFIGPNVVFTNdlyprskiYRKWELKGTTVKRGASIGANATILPGV 86
|
90 100
....*....|....*....|....*...
gi 503281339 419 TVGRDALVGAGSTITKDVPDegGAIARG 446
Cdd:cd03358 87 TIGEYALVGAGAVVTKDVPP--YALVVG 112
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-123 |
3.74e-11 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 61.75 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 1 MTkPKITALVLAAGKGTRMHssRPKVLQTLLGEPMLRYVYDAIKPLFGQaaITVVGHGsglvEQAFPemagqfvlqaqQL 80
Cdd:COG0746 1 MT-MPITGVILAGGRSRRMG--QDKALLPLGGRPLLERVLERLRPQVDE--VVIVANR----PERYA-----------AL 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503281339 81 GtghaLQVAWDAVKADG-------------TDYCLVINGDTPLITAEGLGRLAGQA 123
Cdd:COG0746 61 G----VPVVPDDPPGAGplagilaaleaapAEWVLVLACDMPFLPPDLVRRLLEAL 112
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
8-207 |
4.98e-11 |
|
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: 62.59 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHS---SRPKVLQTLLGEPMLRYVYDAIKplfgQAAIT----VVGHGSGLVEQAFPE-----MAGQFVL 75
Cdd:cd04189 3 GLILAGGKGTRLRPltyTRPKQLIPVAGKPIIQYAIEDLR----EAGIEdigiVVGPTGEEIKEALGDgsrfgVRITYIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 76 QAQQLGTGHALQVAWDAVKADgtDYCLVInGDTplITAEGLGRLAGQAGCCDL-AFMTITP-RDTAQFGRVVRDENqRIS 153
Cdd:cd04189 79 QEEPLGLAHAVLAARDFLGDE--PFVVYL-GDN--LIQEGISPLVRDFLEEDAdASILLAEvEDPRRFGVAVVDDG-RIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503281339 154 AIVE-AKDycmavhgPVTGEVNAGIYLLR---VSSVDTLLGQLRnenksGEYYVTDLI 207
Cdd:cd04189 153 RLVEkPKE-------PPSNLALVGVYAFTpaiFDAISRLKPSWR-----GELEITDAI 198
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
6-123 |
1.49e-10 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 59.90 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 6 ITALVLAAGKGTRMhsSRPKVLQTLLGEPMLRYVYDAIKPLFGQaaITVVGHGSGLVEQAFpemaGQFVLQAQQLGTG-- 83
Cdd:cd02503 1 ITGVILAGGKSRRM--GGDKALLELGGKPLLEHVLERLKPLVDE--VVISANRDQERYALL----GVPVIPDEPPGKGpl 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 503281339 84 ---HAlqvawdAVKADGTDYCLVINGDTPLITAEGLGRLAGQA 123
Cdd:cd02503 73 agiLA------ALRAAPADWVLVLACDMPFLPPELLERLLAAA 109
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
8-245 |
1.70e-10 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 61.03 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRM---HSSRPKVLQTLLGEPMLRYVYDAIKplfgQAAIT----VVGHGSGLVEQAFPEMAG--QFVL--Q 76
Cdd:COG1213 2 AVILAAGRGSRLgplTDDIPKCLVEIGGKTLLERQLEALA----AAGIKdivvVTGYKAELIEEALARPGPdvTFVYnpD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 77 AQQLGTGHALQVAWDAVKADgtdyCLVINGDTpLITAEGLGRLAGQAG----CCDLAFMTITPRDTaqfgRVVRDENQRI 152
Cdd:COG1213 78 YDETNNIYSLWLAREALDED----FLLLNGDV-VFDPAILKRLLASDGdivlLVDRKWEKPLDEEV----KVRVDEDGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 153 SAI---VEAKDYCmavhgpvtGEvNAGIYLLRVSSVDTLLGQLRNENKSGEY--YVTDLIGLAVASAMAVESVqcgdDIS 227
Cdd:COG1213 149 VEIgkkLPPEEAD--------GE-YIGIFKFSAEGAAALREALEALIDEGGPnlYYEDALQELIDEGGPVKAV----DIG 215
|
250 260
....*....|....*....|.
gi 503281339 228 LMG---INSPRELIRAESELR 245
Cdd:COG1213 216 GLPwveIDTPEDLERAEELFA 236
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
4-120 |
2.74e-10 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 59.43 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 4 PKITALVLAAGKGTRMhSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGH-------GSGLVEQAFPEMAGqfvlq 76
Cdd:PRK00317 2 PPITGVILAGGRSRRM-GGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNlaryaafGLPVIPDSLADFPG----- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503281339 77 aqQLGTGHAlqvawdAVKADGTDYCLVINGDTPLITAEGLGRLA 120
Cdd:PRK00317 76 --PLAGILA------GLKQARTEWVLVVPCDTPFIPPDLVARLA 111
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
262-438 |
9.34e-10 |
|
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: 58.19 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 262 PETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHItdstfAPGCVVREFCHI-EGAEVGPQAVVGP----YAR 336
Cdd:cd03352 5 GENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI-----HPNVTIYEGCIIgDRVIIHSGAVIGSdgfgFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 337 LRPG--TVLHTGA-RVGNFVE-----------MKKAVLGEGAKASHLSYlgdaeVGAGANIGAGTITCNYDGknkF--TT 400
Cdd:cd03352 80 DGGGwvKIPQLGGvIIGDDVEiganttidrgaLGDTVIGDGTKIDNLVQ-----IAHNVRIGENCLIAAQVG---IagST 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPD 438
Cdd:cd03352 152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPP 189
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
251-440 |
1.61e-09 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 59.26 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 251 AHIDRGVLIHnpETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHItdstfAPGCVVREFCHIeGAEV--GPQ 328
Cdd:COG1044 103 AVIDPSAKIG--EGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVL-----HPNVTIYERCVI-GDRViiHSG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 329 AVVGP----YARLRPGT---VLHTGA-RVGNFVE-----------MKKAVLGEGAKASHLSYLG-DAEVGAG----ANIG 384
Cdd:COG1044 175 AVIGAdgfgFAPDEDGGwvkIPQLGRvVIGDDVEiganttidrgaLGDTVIGDGTKIDNLVQIAhNVRIGEHtaiaAQVG 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503281339 385 -AGtitcnydgknkfTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEG 440
Cdd:COG1044 255 iAG------------STKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGG 299
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
358-433 |
1.74e-09 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 54.18 E-value: 1.74e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503281339 358 AVLGEGAKASHLSYLGD-AEVGAGANIGAGTITCNYDGKN-KFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTIT 433
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGPNeKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-157 |
3.27e-09 |
|
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: 56.76 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 6 ITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGS--GLVEQAFPEMAGQFVLQAQ----- 78
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDdiDLAKELAKYGLSKVVKIVEggatr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 79 QLGTGHALQvawdAVKADGTDYCLVINGDTPLITAEGLGRL---AGQAGCCDLAfmtITPRDTAqfgrVVRDENQRISAI 155
Cdd:cd02516 81 QDSVLNGLK----ALPDADPDIVLIHDAARPFVSPELIDRLidaLKEYGAAIPA---VPVTDTI----KRVDDDGVVVET 149
|
..
gi 503281339 156 VE 157
Cdd:cd02516 150 LD 151
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
3-157 |
1.95e-08 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 54.75 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 3 KPKITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYvydAIKPLFGQAAIT---VVGHgsglvEQAFPEMAGQFVLQAQ- 78
Cdd:PRK00155 1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEH---TLEAFLAHPRIDeiiVVVP-----PDDRPDFAELLLAKDPk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 79 -QLGTG---------HALQVAWDAvkadgtDYCLVINGDTPLITAEGLGRLAGQA---GCCDLAfmtITPRDTaqfgrVV 145
Cdd:PRK00155 73 vTVVAGgaerqdsvlNGLQALPDD------DWVLVHDAARPFLTPDDIDRLIEAAeetGAAILA---VPVKDT-----IK 138
|
170
....*....|...
gi 503281339 146 R-DENQRISAIVE 157
Cdd:PRK00155 139 RsDDGGGIVDTPD 151
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
7-244 |
2.39e-08 |
|
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: 54.22 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 7 TALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVG--HGSGLVEQAFPEMAG-QFVL--QAQQLG 81
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVspDDTEFFQKYLVARAVpKIVAggDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 82 TGHALQVawdavkADGTDYCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTITPRDTAqfgrVVRDENQRISAIVEaKDY 161
Cdd:TIGR00453 81 VRNGLKA------LKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTL----KRVEADGFVVETVD-REG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 162 CMAVHGPvtgevnagiyllRVSSVDTLLGQLRNENKSGeYYVTDliglavaSAMAVEsvQCGDDISL-------MGINSP 234
Cdd:TIGR00453 150 LWAAQTP------------QAFRTELLKKALARAKLEG-FEITD-------DASAVE--KLGGKVQLvegdalnFKITTP 207
|
250
....*....|
gi 503281339 235 RELIRAESEL 244
Cdd:TIGR00453 208 EDLALAEALL 217
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
8-207 |
2.42e-08 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 55.10 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMH---SSRPKVLQTLLGEPMLRYVYDAIK------------PLFGQAAITVVGHGSGLveqafpEMAGQ 72
Cdd:COG1209 3 GIILAGGSGTRLRpltLTVSKQLLPVYDKPMIYYPLSTLMlagireiliistPEDGPQFERLLGDGSQL------GIKIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 73 FVLQAQQLGTGHALQVAWDAVkadGTDYCLVINGDTpLITAEGLGRL-----AGQAGCcdlafmTI------TPRdtaQF 141
Cdd:COG1209 77 YAVQPEPLGLAHAFIIAEDFI---GGDPVALVLGDN-IFYGDGLSELlreaaARESGA------TIfgykveDPE---RY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503281339 142 GRVVRDENQRISAIVEaK------DYcmAVhgpvtgevnAGIYLLrVSSVDTLLGQLRNeNKSGEYYVTDLI 207
Cdd:COG1209 144 GVVEFDEDGRVVSLEE-KpkepksNL--AV---------TGLYFY-DNDVVEIAKNLKP-SARGELEITDAN 201
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
251-440 |
2.86e-08 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 55.15 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 251 AHIDRGVLIhnPETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHItdstfAPGCVVREFCHI-EGAEVGPQA 329
Cdd:PRK00892 107 AVIDPSAKI--GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRL-----HANVTIYHAVRIgNRVIIHSGA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 330 VVGP----YARLRPG--TVLHTGA-RVGNFVE-----------MKKAVLGEGAKASHLsylgdAEVGAGANIGAGTI--- 388
Cdd:PRK00892 180 VIGSdgfgFANDRGGwvKIPQLGRvIIGDDVEiganttidrgaLDDTVIGEGVKIDNL-----VQIAHNVVIGRHTAiaa 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503281339 389 TCNYDGknkfTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEG 440
Cdd:PRK00892 255 QVGIAG----STKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPG 302
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
8-119 |
4.19e-08 |
|
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.
Pssm-ID: 274516 Cd Length: 188 Bit Score: 53.11 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMhsSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSglvEQAFPEMAGQFVLQ-----AQQLGT 82
Cdd:TIGR03310 2 AIILAAGLSSRM--GQNKLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEA---DELVALLANHSNITlvhnpQYAEGQ 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 503281339 83 GHALQVAwdAVKADGTDYCLVINGDTPLITAEGLGRL 119
Cdd:TIGR03310 77 SSSIKLG--LELPVQSDGYLFLLGDQPFVTPDIIQLL 111
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
9-157 |
1.37e-07 |
|
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: 52.05 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 9 LVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHgsglveqafPEMAGQFVLQAQQLGTGHALQV 88
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVP---------PDDIEYFEELLAKYGIDKPVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 89 A------WDAVKA------DGTDYCLVINGDTPLITAEGLGRL---AGQAGCCDLAfmtITPRDTaqfgrVVR-DENQRI 152
Cdd:COG1211 72 VaggatrQDSVRNglealpDDDDWVLVHDAARPLVSPELIDRVieaAREYGAAIPA---LPVTDT-----IKRvDDDGRV 143
|
....*
gi 503281339 153 SAIVE 157
Cdd:COG1211 144 TETVD 148
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
400-446 |
1.56e-07 |
|
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 49.38 E-value: 1.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503281339 400 TTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDegGAIARG 446
Cdd:cd04647 59 IVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPP--NSIVAG 103
|
|
| LbH_unknown |
cd05635 |
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ... |
310-396 |
1.75e-07 |
|
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100059 [Multi-domain] Cd Length: 101 Bit Score: 49.20 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 310 PGCVVREFCHIEG-AEVGPQAVVGPYARLRPGTVLHTGARVGNFVEmkKAVLGEGAKASHLSYLGDAEVGAGANIGAGti 388
Cdd:cd05635 16 KDAVIEPFAVIEGpVYIGPGSRVKMGARIYGNTTIGPTCKIGGEVE--DSIIEGYSNKQHDGFLGHSYLGSWCNLGAG-- 91
|
....*...
gi 503281339 389 TCNYDGKN 396
Cdd:cd05635 92 TNNSDLKN 99
|
|
| LbH_SAT |
cd03354 |
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ... |
373-438 |
4.55e-07 |
|
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.
Pssm-ID: 100045 [Multi-domain] Cd Length: 101 Bit Score: 47.82 E-value: 4.55e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503281339 373 GDAEVGAGANIGAG-TITCNYDGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPD 438
Cdd:cd03354 27 ETAVIGDNCTIYQGvTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPA 93
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
8-220 |
2.96e-06 |
|
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: 48.40 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMH---SSRPKVLQTLLG-EPMLRYVYDAIKPLfGQAAITVVghgsgLVEQAFPEMAGQF---------V 74
Cdd:pfam00483 2 AIILAGGSGTRLWpltRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVI-----LTQEHRFMLNELLgdgskfgvqI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 75 LQAQQ---LGTGHALQVAWDAVKADGTDyCLVINGDtpLITAEGLGRLAGQA----GCCDLAFMtITPRDTA-QFGRVVR 146
Cdd:pfam00483 76 TYALQpegKGTAPAVALAADFLGDEKSD-VLVLGGD--HIYRMDLEQAVKFHiekaADATVTFG-IVPVEPPtGYGVVEF 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503281339 147 DENQRISAIVEAKDycmavHGPVTGEVNAGIYLLRVSSVDTLLGQLrNENKSGEYYVTDLIGLAVASAMAVESV 220
Cdd:pfam00483 152 DDNGRVIRFVEKPK-----LPKASNYASMGIYIFNSGVLDFLAKYL-EELKRGEDEITDILPKALEDGKLAYAF 219
|
|
| LbH_XAT |
cd03349 |
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ... |
400-438 |
3.02e-06 |
|
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: 46.77 E-value: 3.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503281339 400 TTIGPGAFIGSNtALVAP-VTVGRDALVGAGSTITKDVPD 438
Cdd:cd03349 74 VIIGNDVWIGHG-ATILPgVTIGDGAVIAAGAVVTKDVPP 112
|
|
| LbH_wcaF_like |
cd05825 |
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
401-446 |
8.36e-06 |
|
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: 44.52 E-value: 8.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503281339 401 TIGPGAFIGSNtALVAP-VTVGRDALVGAGSTITKDVPDegGAIARG 446
Cdd:cd05825 58 VIGDGAWVAAE-AFVGPgVTIGEGAVVGARSVVVRDLPA--WTVYAG 101
|
|
| LbH_MAT_GAT |
cd03357 |
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ... |
401-438 |
1.08e-05 |
|
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: 45.49 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|....*...
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPD 438
Cdd:cd03357 120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPA 157
|
|
| lacA |
PRK09527 |
galactoside O-acetyltransferase; Reviewed |
398-437 |
1.52e-05 |
|
galactoside O-acetyltransferase; Reviewed
Pssm-ID: 181930 [Multi-domain] Cd Length: 203 Bit Score: 45.76 E-value: 1.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503281339 398 FTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVP 437
Cdd:PRK09527 130 FPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIP 169
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-119 |
1.66e-05 |
|
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: 46.02 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 7 TALVLAAGKGTRMHS---SRPKVLQTLLGEPMLRYVYDAIKplfgQAAIT--VV--GHGSGLVEQAFPEMAGQFVLQ--- 76
Cdd:cd06422 1 KAMILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDRLA----AAGIRriVVntHHLADQIEAHLGDSRFGLRITisd 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 503281339 77 --AQQLGTGHALqvaWDAVKADGTDYCLVINGDTplITAEGLGRL 119
Cdd:cd06422 77 epDELLETGGGI---KKALPLLGDEPFLVVNGDI--LWDGDLAPL 116
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
6-60 |
1.72e-05 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 46.67 E-value: 1.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 503281339 6 ITALVLAAGKGTRMhSSRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSG 60
Cdd:PRK14489 6 IAGVILAGGLSRRM-NGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPAR 59
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
1-125 |
1.74e-05 |
|
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional
Pssm-ID: 236492 [Multi-domain] Cd Length: 378 Bit Score: 46.76 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 1 MTKPKITALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDAIK--PLFGQAAITVVGHGSGLVEQAFPEMAGQFVLQA- 77
Cdd:PRK09382 1 TLMSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSsaPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503281339 78 ---QQlgtghALQVAWDAVKadgTDYCLVINGDTPLITAEGLGRLA---GQAGC 125
Cdd:PRK09382 81 atrQE-----SVRNALEALD---SEYVLIHDAARPFVPKELIDRLIealDKADC 126
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
258-452 |
2.30e-05 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 45.78 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 258 LIHnpETVIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHItdstfAPGCVVREFCHI-EGAEVG--PQ------ 328
Cdd:PRK12461 1 MIH--PTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVI-----LGPTRIGKNNKIhQGAVVGdePQdftykg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 329 ----AVVGPYARLRPGTVLHTGARVGNfvemkKAVLGEG----AKaSHLSYlgDAEVGAGANIGAGTITCNYdgknkftT 400
Cdd:PRK12461 74 eesrLEIGDRNVIREGVTIHRGTKGGG-----VTRIGNDnllmAY-SHVAH--DCQIGNNVILVNGALLAGH-------V 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDEggAIARGRQVNIH 452
Cdd:PRK12461 139 TVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPY--CMMAGHPTNVH 188
|
|
| PRK10502 |
PRK10502 |
putative acyl transferase; Provisional |
401-446 |
3.29e-05 |
|
putative acyl transferase; Provisional
Pssm-ID: 236703 [Multi-domain] Cd Length: 182 Bit Score: 44.56 E-value: 3.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503281339 401 TIGPGAFIGSNtALVAP-VTVGRDALVGAGSTITKDVPdeGGAIARG 446
Cdd:PRK10502 126 VIGEGCWLAAD-VFVAPgVTIGSGAVVGARSSVFKSLP--ANTICRG 169
|
|
| CysE |
COG1045 |
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ... |
401-438 |
3.73e-05 |
|
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440667 [Multi-domain] Cd Length: 174 Bit Score: 43.92 E-value: 3.73e-05
10 20 30
....*....|....*....|....*....|....*...
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPD 438
Cdd:COG1045 119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPP 156
|
|
| DapD |
COG2171 |
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ... |
309-447 |
3.96e-05 |
|
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: 45.11 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 309 APGCVVREfchieGAEVGPQAVVGP-Y----ARLRPGTVLHTGARVGNfvemkKAVLGEGakaSHLSylgdaevgAGANI 383
Cdd:COG2171 101 VPGARVRL-----GAYLAPGVVLMPsFvnigAYVDEGTMVDTWATVGS-----CAQIGKN---VHLS--------GGAGI 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503281339 384 GaGTItcnyDGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITK-----DVpdEGGAIARGR 447
Cdd:COG2171 160 G-GVL----EPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiyDR--VTGEVYYGR 221
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
8-107 |
4.44e-05 |
|
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: 44.53 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRM---HSSRPKVLQTLLGEPMLRYVYDAIKplfgQAAIT----VVGHGSGLVEQAFPEMAG-QFVL--QA 77
Cdd:cd02523 1 AIILAAGRGSRLrplTEDRPKCLLEINGKPLLERQIETLK----EAGIDdiviVTGYKKEQIEELLKKYPNiKFVYnpDY 76
|
90 100 110
....*....|....*....|....*....|
gi 503281339 78 QQLGTGHALQVAWDAVKADgtdyCLVINGD 107
Cdd:cd02523 77 AETNNIYSLYLARDFLDED----FLLLEGD 102
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
8-186 |
8.12e-05 |
|
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: 43.74 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMHS---SRPKVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQ------FVLQAQ 78
Cdd:cd06425 3 ALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKlgikitFSIETE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 79 QLGTGHALQVAWDAVKADGTDYcLVINGDtpLITAEGLGRLAG--QAGCCDLAFMTITPRDTAQFGRVVRDENQ-RISAI 155
Cdd:cd06425 83 PLGTAGPLALARDLLGDDDEPF-FVLNSD--VICDFPLAELLDfhKKHGAEGTILVTKVEDPSKYGVVVHDENTgRIERF 159
|
170 180 190
....*....|....*....|....*....|..
gi 503281339 156 VEA-KDYcmavhgpVTGEVNAGIYLLRVSSVD 186
Cdd:cd06425 160 VEKpKVF-------VGNKINAGIYILNPSVLD 184
|
|
| PLN02739 |
PLN02739 |
serine acetyltransferase |
331-437 |
1.10e-04 |
|
serine acetyltransferase
Pssm-ID: 215394 [Multi-domain] Cd Length: 355 Bit Score: 44.26 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 331 VGPYARLRPGTVLHTGARVgnfVEMKKAVLGEGAKASHLSYLGdaevGAGANIGagtitcnyDGKNKftttIGPGAFIGS 410
Cdd:PLN02739 208 IHPAARIGKGILLDHGTGV---VIGETAVIGDRVSILHGVTLG----GTGKETG--------DRHPK----IGDGALLGA 268
|
90 100
....*....|....*....|....*..
gi 503281339 411 NTALVAPVTVGRDALVGAGSTITKDVP 437
Cdd:PLN02739 269 CVTILGNISIGAGAMVAAGSLVLKDVP 295
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
11-133 |
2.44e-04 |
|
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: 41.80 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 11 LAAGKGTRMhSSRPKVLQTLLGEPMLRYVYDAIKPL-FGQAAITVVGHGSGLveQAFPEMAGQFVLQAQQLGTGHALQVA 89
Cdd:COG2266 1 MAGGKGTRL-GGGEKPLLEICGKPMIDRVIDALEEScIDKIYVAVSPNTPKT--REYLKERGVEVIETPGEGYVEDLNEA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503281339 90 WDAVKadgtDYCLVINGDTPLITAEGLGRLAGQAGCCDLAFMTI 133
Cdd:COG2266 78 LESIS----GPVLVVPADLPLLTPEIIDDIIDAYLESGKPSLTV 117
|
|
| LbH_UDP-GlcNAc_AT |
cd03351 |
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ... |
251-437 |
3.88e-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: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 251 AHIDRGVLIHnpETVIIGPRVAVEPGAEIfghceiygassvAAGSRLGSYTHITDSTF-APGCVVREFCHIeGAEvgPQ- 328
Cdd:cd03351 6 AIVDPGAKIG--ENVEIGPFCVIGPNVEI------------GDGTVIGSHVVIDGPTTiGKNNRIFPFASI-GEA--PQd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 329 ---------AVVGPYARLRPGTVLHTGA-------RVGNfvemkKAVLGEGAKASHLSYLGDAEVGA-GANIgAGTITcn 391
Cdd:cd03351 69 lkykgeptrLEIGDNNTIREFVTIHRGTaqgggvtRIGN-----NNLLMAYVHVAHDCVIGNNVILAnNATL-AGHVE-- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503281339 392 ydgknkftttIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVP 437
Cdd:cd03351 141 ----------IGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVP 176
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
8-207 |
6.58e-04 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 40.96 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAGKGTRMH---SSRPKVLQTLLGEPMLRYVYDAIKpLFGQAAITV-VGHGSGLVEQAFPEMAG-----QFVLQAQ 78
Cdd:cd06426 1 VVIMAGGKGTRLRpltENTPKPMLKVGGKPILETIIDRFI-AQGFRNFYIsVNYLAEMIEDYFGDGSKfgvniSYVREDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 79 QLGTGHALQVawdaVKADGTDYCLVINGDtpLITAEGLGRLagqagccdLAF-------MTITPRD---TAQFGrVVRDE 148
Cdd:cd06426 80 PLGTAGALSL----LPEKPTDPFLVMNGD--ILTNLNYEHL--------LDFhkennadATVCVREyevQVPYG-VVETE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 149 NQRISAIVEAKDYcmavhgpvTGEVNAGIYLLRVSSVDTLlgqlrnenKSGEYY-VTDLI 207
Cdd:cd06426 145 GGRITSIEEKPTH--------SFLVNAGIYVLEPEVLDLI--------PKNEFFdMPDLI 188
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
265-343 |
7.19e-04 |
|
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: 38.38 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 265 VIIGPRVAVEPGAEIFGHCEIYGASSVAAGSRLGSYTHITDSTfapGCVVREFCHIEG-AEVGPQAVVGPYARLRPGTVL 343
Cdd:cd00208 1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKN---PTIIGDNVEIGAnAVIHGGVKIGDNAVIGAGAVV 77
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
8-188 |
7.68e-04 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 41.09 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 8 ALVLAAG--KGTRMhssRP------KVLQTLLGEPMLRYVYDAIKPLFGQAAITVVGHGSGLVEQAFPEMAGQFV----- 74
Cdd:cd06428 1 AVILVGGpqKGTRF---RPlsldvpKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFnvpir 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 75 -LQA-QQLGTGHALQVAWDAVKADGTDYCLVINGDTplitaeglgrlagqagCCDLAF----------------MTITP- 135
Cdd:cd06428 78 yLQEyKPLGTAGGLYHFRDQILAGNPSAFFVLNADV----------------CCDFPLqellefhkkhgasgtiLGTEAs 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503281339 136 RDTA-QFGRVVRDEN-QRISAIVEAkdycmavhgP---VTGEVNAGIYLLRVSSVDTL 188
Cdd:cd06428 142 REQAsNYGCIVEDPStGEVLHYVEK---------PetfVSDLINCGVYLFSPEIFDTI 190
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
267-389 |
8.18e-04 |
|
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: 39.70 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 267 IGPRVAVEPGAEIFGHCEIYGASSVAAGS---------RLGSYTHITDstfapGCVVREFcHIEGAEVGPQAVVGPYArl 337
Cdd:cd04645 2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAvlrgdvnpiRIGERTNIQD-----GSVLHVD-PGYPTIIGDNVTVGHGA-- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503281339 338 rpgtVLHtGARVGN--FVEMkKAVLGEGAKashlsylgdaeVGAGANIGAGTIT 389
Cdd:cd04645 74 ----VLH-GCTIGDncLIGM-GAIILDGAV-----------IGKGSIVAAGSLV 110
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
401-455 |
9.92e-04 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 40.01 E-value: 9.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTIT--KDVPDegGAIARGRQVNIHRRL 455
Cdd:COG0663 90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPP--GSLVVGSPAKVVREL 144
|
|
| PLN02357 |
PLN02357 |
serine acetyltransferase |
343-443 |
1.00e-03 |
|
serine acetyltransferase
Pssm-ID: 215205 [Multi-domain] Cd Length: 360 Bit Score: 41.02 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 343 LHTGARVGNFVEMKKA---VLGEGAK-ASHLSYLGDAEVGaganiGAGTITCNYDGKnkftttIGPGAFIGSNTALVAPV 418
Cdd:PLN02357 229 IHPGAKIGQGILLDHAtgvVIGETAVvGNNVSILHNVTLG-----GTGKQSGDRHPK------IGDGVLIGAGTCILGNI 297
|
90 100
....*....|....*....|....*
gi 503281339 419 TVGRDALVGAGSTITKDVPDEGGAI 443
Cdd:PLN02357 298 TIGEGAKIGAGSVVLKDVPPRTTAV 322
|
|
| PRK02726 |
PRK02726 |
molybdenum cofactor guanylyltransferase; |
2-44 |
1.05e-03 |
|
molybdenum cofactor guanylyltransferase;
Pssm-ID: 235063 Cd Length: 200 Bit Score: 40.02 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 503281339 2 TKPKITALVLAAGKGTRMhsSRPKVLQTLLGEPMLRYVYDAIK 44
Cdd:PRK02726 4 VKNNLVALILAGGKSSRM--GQDKALLPWQGVPLLQRVARIAA 44
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
323-452 |
1.09e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 40.89 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 323 AEVGPQAVVGPyarlrpgtvlhtgarvgnfvemkKAVLGEGAKASHLSYlgdaeVGAGANIGAGTItcnydgknkftttI 402
Cdd:PRK00892 101 AGIHPSAVIDP-----------------------SAKIGEGVSIGPNAV-----IGAGVVIGDGVV-------------I 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 503281339 403 GPGAFIGSNtalvapVTVGRDALVGAGSTITKDVpdeggAIarGRQVNIH 452
Cdd:PRK00892 140 GAGAVIGDG------VKIGADCRLHANVTIYHAV-----RI--GNRVIIH 176
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
273-351 |
1.14e-03 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 37.61 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503281339 273 VEPGAEIFGHCEIyGASSVAAGSRLGSYTHITDSTFAPGCVVREFCHIEGAEVGPQAVVGPYARLRPGTVLHTGARVGN 351
Cdd:cd03356 2 IGESTVIGENAII-KNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
6-68 |
1.37e-03 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 40.25 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 6 ITALVLAAGKGTRM----HSSRPKVLQTLLG-EPMLRYVYDAIKPLFGQAAITVVGHGS--GLVEQAFPE 68
Cdd:cd02509 1 IYPVILAGGSGTRLwplsRESYPKQFLKLFGdKSLLQQTLDRLKGLVPPDRILVVTNEEyrFLVREQLPE 70
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
291-384 |
1.40e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 40.97 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 291 VAAGSRLGsytHITDSTFAPGCVVRefchieGAEVGpQAVvgpyarLRPGTVLHTGARVGNFVEMKKAVLGEGAKASHLS 370
Cdd:PRK00844 304 VDGGGRVG---SAQDSLVSAGSIIS------GATVR-NSV------LSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAI 367
|
90
....*....|....
gi 503281339 371 YLGDAEVGAGANIG 384
Cdd:PRK00844 368 LDKNVVVPPGATIG 381
|
|
| LbH_THP_succinylT |
cd03350 |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ... |
309-447 |
3.05e-03 |
|
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: 37.75 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 309 APGCVVREfchieGAEVGPQAVvgpyarLRPGTVLHTGARV--GNFVEMKkAVLGegakashlsylGDAEVGAGANIGAG 386
Cdd:cd03350 5 PPGAIIRD-----GAFIGPGAV------LMMPSYVNIGAYVdeGTMVDSW-ATVG-----------SCAQIGKNVHLSAG 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503281339 387 T-ITCNYDGKNKFTTTIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVP---DEGGAIARGR 447
Cdd:cd03350 62 AvIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPiydRETGEIYYGR 126
|
|
| LpxA |
COG1043 |
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ... |
251-437 |
3.06e-03 |
|
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: 39.23 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 251 AHIDRGVLIHnpETVIIGPRVAVEPGAEIfghceiygassvAAGSRLGSYTHITD-STFAPGCVVREFCHIeGAEvgPQ- 328
Cdd:COG1043 8 AIVDPGAKLG--ENVEIGPFCVIGPDVEI------------GDGTVIGSHVVIEGpTTIGKNNRIFPFASI-GEE--PQd 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 329 ---------AVVGPYARLRPGTVLHTGA-------RVGN---FveMKkavlgegakASHlsylgdaeVGAGANIGAGTIT 389
Cdd:COG1043 71 lkykgeptrLEIGDNNTIREFVTIHRGTvqgggvtRIGDdnlL--MA---------YVH--------VAHDCVVGNNVIL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503281339 390 CNYdgknkfTT-----TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVP 437
Cdd:COG1043 132 ANN------ATlaghvEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVP 178
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
309-388 |
4.51e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.02 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 309 APGCVVREFCHIEGAEVGPQAVVGPYARLRpGTVLHTGARVGNFVEMKKAVLGEGAKASHLSYLGDAEVGAGANIGAGTI 388
Cdd:cd04652 3 GENTQVGEKTSIKRSVIGANCKIGKRVKIT-NCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGTE 81
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
283-340 |
5.69e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 38.70 E-value: 5.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503281339 283 CEIYGA---SSVAAGSRLGSYTHITDSTFAPGCVVREFCHIEGAEVGPQAVVGPYARLRPG 340
Cdd:PRK05293 300 CVVYGTvehSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGG 360
|
|
| PRK10092 |
PRK10092 |
maltose O-acetyltransferase; Provisional |
401-445 |
6.63e-03 |
|
maltose O-acetyltransferase; Provisional
Pssm-ID: 182235 [Multi-domain] Cd Length: 183 Bit Score: 37.49 E-value: 6.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 503281339 401 TIGPGAFIGSNTALVAPVTVGRDALVGAGSTITKDVPDE---GGAIAR 445
Cdd:PRK10092 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNvvvGGNPAR 178
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
303-438 |
6.95e-03 |
|
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: 37.01 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 303 ITDSTF-APGCVVrefchIEGAEVGPQAVVGPYARLRpgtvlhtgARVGNFVEMKKAVLGEGAkASHLSYLGDAEVGAGA 381
Cdd:cd04645 2 IDPSAFiAPNATV-----IGDVTLGEGSSVWFGAVLR--------GDVNPIRIGERTNIQDGS-VLHVDPGYPTIIGDNV 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503281339 382 NIGAGTI--TCnydgknkfttTIGPGAFIGSNTALVAPVTVGRDALVGAGSTIT--KDVPD 438
Cdd:cd04645 68 TVGHGAVlhGC----------TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPP 118
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
309-410 |
7.67e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 38.20 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503281339 309 APGCVVREFCHI-EGAEVGPQAVVGPYARLRPGTVLHTGarvgnfvemkkAVLGEGAKashlsylgdaeVGAGANIGAG- 386
Cdd:PRK00892 104 HPSAVIDPSAKIgEGVSIGPNAVIGAGVVIGDGVVIGAG-----------AVIGDGVK-----------IGADCRLHANv 161
|
90 100
....*....|....*....|....*
gi 503281339 387 TITCNYD-GKNkftTTIGPGAFIGS 410
Cdd:PRK00892 162 TIYHAVRiGNR---VIIHSGAVIGS 183
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
8-42 |
8.51e-03 |
|
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: 37.81 E-value: 8.51e-03
10 20 30
....*....|....*....|....*....|....*
gi 503281339 8 ALVLAAGKGTRMHSSRPKVLQTLLGEPMLRYVYDA 42
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDA 35
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|
| |
