|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
76-517 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 845.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 76 EEIVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAIQRATIEGSGGL 155
Cdd:PLN02338 2 EEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 156 FPASKESTDEIQLFLGNAGTAMRPLTAAVVAAGGNARYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVIG 235
Cdd:PLN02338 82 FPVSGDSKEDVELFLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 236 KGGLPGGTVKLSGSVSSQYLTALLMAAPLALGDVTIEIVDKLISVPYVEMTIKLMERFGVSVEHSDSWDRFLIRGGQKYK 315
Cdd:PLN02338 162 AGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDSWDRFFIKGGQKYK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 316 SPGNAFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPRAPSGRKHLRAI 395
Cdd:PLN02338 242 SPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 396 DVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDD 475
Cdd:PLN02338 322 DVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYDD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1109197953 476 HRMAMAFSLAACAEVPVTIKDPGCTRKTFPDYFEVLQKFSKH 517
Cdd:PLN02338 402 HRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAKH 443
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
78-513 |
5.31e-180 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 511.94 E-value: 5.31e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 78 IVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAiQRATIEGSGGLFP 157
Cdd:COG0128 4 LTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGGGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 158 ASKEStdeiqLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDCfLGTNCPPVRVIGkG 237
Cdd:COG0128 83 EPDAV-----LDCGNSGTTMRLLTGLLALQPG--EVVLTGDESLRKRPMGRLLDPLRQLGARIES-RGGGYLPLTIRG-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 238 GLPGGTVKLSGSVSSQYLTALLMAAPLALGDVTIEIVDKLISVPYVEMTIKLMERFGVSVEHSDsWDRFLIRGGQKYKsP 317
Cdd:COG0128 154 PLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEG-YRRFTVPGGQRYR-P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 318 GNAFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPrapsgrkhLRAIDV 397
Cdd:COG0128 232 GDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSP--------LKGIDI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 398 NMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDDHR 477
Cdd:COG0128 304 DLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHR 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 1109197953 478 MAMAFSLAAC-AEVPVTIKDPGCTRKTFPDYFEVLQK 513
Cdd:COG0128 384 IAMAFAVAGLrAEGPVTIDDAECVAKSFPDFFELLES 420
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
86-514 |
4.11e-168 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 481.29 E-value: 4.11e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 86 ISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSaiQRATIEGSGGLFPaskesTDE 165
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG--GTVEIVGGGGLGL-----PPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 166 IQLFLGNAGTAMRPLTAAVVAAGGNarYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVrvIGKGGLPGGTVK 245
Cdd:cd01556 74 AVLDCGNSGTTMRLLTGLLALQGGD--SVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL--IGGGGLKGGEVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 246 LSGSVSSQYLTALLMAAPLALGDVTIEIVdKLISVPYVEMTIKLMERFGVSVEHSDsWDRFLIRGGQKYKSPgNAFVEGD 325
Cdd:cd01556 150 IPGAVSSQFKSALLLAAPLAEGPTTIIIG-ELESKPYIDHTERMLRAFGAEVEVDG-YRTITVKGGQKYKGP-EYTVEGD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 326 ASSASYFLAGAAVTGGTVTVEGCGTSSlqGDVKFAEVLEKMGAEVSWT-ENSVTVKGPPrapsgrkHLRAIDVNMNKMPD 404
Cdd:cd01556 227 ASSAAFFLAAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGnEDTVVVESGG-------KLKGIDIDGNDIPD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 405 VAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPE-RLNVTEIDTYDDHRMAMAFS 483
Cdd:cd01556 298 EAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVYTYGDHRIAMSFA 377
|
410 420 430
....*....|....*....|....*....|..
gi 1109197953 484 LAAC-AEVPVTIKDPGCTRKTFPDYFEVLQKF 514
Cdd:cd01556 378 IAGLvAEGGVTIEDPECVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
88-517 |
4.50e-167 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 478.69 E-value: 4.50e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 88 GTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAIqrATIEGSGGLFPaskestdEIQ 167
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEV--AVIEGVGGKEP-------QAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 168 LFLGNAGTAMRPLTAAVVAAGGNarYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVigKGGLPGGTVKLS 247
Cdd:TIGR01356 72 LDLGNSGTTARLLTGVLALADGE--VVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTI--SGPLPGGIVYIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 248 GSVSSQYLTALLMAAPLALGdVTIEIVD-KLISVPYVEMTIKLMERFGVSVEHSDSwDRFLIRGGQKYKSPGnAFVEGDA 326
Cdd:TIGR01356 148 GSASSQYKSALLLAAPALQA-VGITIVGePLKSRPYIEITLDLLGSFGVEVERSDG-RKIVVPGGQKYGPQG-YDVPGDY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 327 SSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPRapsgrkhLRAIDVNMNKMPDVA 406
Cdd:TIGR01356 225 SSAAFFLAAAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASG-------LKGIKIDMDDMIDEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 407 MTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDDHRMAMAFSLAA 486
Cdd:TIGR01356 298 PTLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAG 377
|
410 420 430
....*....|....*....|....*....|..
gi 1109197953 487 C-AEVPVTIKDPGCTRKTFPDYFEVLQKFSKH 517
Cdd:TIGR01356 378 LvAEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
81-511 |
1.15e-156 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 452.52 E-value: 1.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 81 QPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRV-EEDSAIQRATIEGSGGLFPAS 159
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIiKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 160 kestDEIQLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVigkGGL 239
Cdd:pfam00275 81 ----EDLVLDMGNSGTALRPLTGRLALQSG--EVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKV---RGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 240 PGGTVKLSGSVSSQYLTALLMAAPLALGDVTIeiVDKLISVPYVEMTIKLMERFGVSVEHSDSWDRFLIRGGQKYKSpGN 319
Cdd:pfam00275 152 RLGGIHIDGDVSSQFVTSLLMLAALLAEGTTT--IENLASEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPG-QE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 320 AFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPrapsgrkHLRAIDVNM 399
Cdd:pfam00275 229 YRVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPP-------GLRGKAVDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 400 NKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPE-RLNVTEIDTYDDHRM 478
Cdd:pfam00275 302 RTAPDPAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYGDHRI 381
|
410 420 430
....*....|....*....|....*....|....
gi 1109197953 479 AMAFSLAAC-AEVPVTIKDPGCTRKTFPDYFEVL 511
Cdd:pfam00275 382 AMALALAGLvAEGETIIDDIECTDRSFPDFEEKL 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
76-517 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 845.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 76 EEIVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAIQRATIEGSGGL 155
Cdd:PLN02338 2 EEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 156 FPASKESTDEIQLFLGNAGTAMRPLTAAVVAAGGNARYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVIG 235
Cdd:PLN02338 82 FPVSGDSKEDVELFLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 236 KGGLPGGTVKLSGSVSSQYLTALLMAAPLALGDVTIEIVDKLISVPYVEMTIKLMERFGVSVEHSDSWDRFLIRGGQKYK 315
Cdd:PLN02338 162 AGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDSWDRFFIKGGQKYK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 316 SPGNAFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPRAPSGRKHLRAI 395
Cdd:PLN02338 242 SPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 396 DVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDD 475
Cdd:PLN02338 322 DVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYDD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1109197953 476 HRMAMAFSLAACAEVPVTIKDPGCTRKTFPDYFEVLQKFSKH 517
Cdd:PLN02338 402 HRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAKH 443
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
80-511 |
0e+00 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 533.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 80 LQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAIQRatIEGSGGLFPAS 159
Cdd:PRK11860 9 LPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGGQFPVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 160 KestdeIQLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVIGKGGL 239
Cdd:PRK11860 87 Q-----ADLFLGNAGTAMRPLTAALALLGG--EYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 240 PGGTVKLSGSVSSQYLTALLMAAPLALG-DVTIEIVDKLISVPYVEMTIKLMERFGVSVEHsDSWDRFLIRGGQKYKSPG 318
Cdd:PRK11860 160 LDAPIRVRGDVSSQFLTALLMALPLVARrDITIEVVGELISKPYIEITLNLLARFGIAVQR-EGWQRFTIPAGSRYRSPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 319 NAFVEGDASSASYFLAGAAVTGGT-VTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVkgppRAPSGRkhLRAIDV 397
Cdd:PRK11860 239 EIHVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEV----RRGAWP--LKAIDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 398 NMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPER---LNVTEIDTYD 474
Cdd:PRK11860 313 DCNHIPDAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYD 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1109197953 475 DHRMAMAFSLAA--CAEVPVTIKDPGCTRKTFPDYFEVL 511
Cdd:PRK11860 393 DHRMAMCFSLAAfnPAGLPVRINDPKCVAKTFPDYFEAL 431
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
78-513 |
5.31e-180 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 511.94 E-value: 5.31e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 78 IVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAiQRATIEGSGGLFP 157
Cdd:COG0128 4 LTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGGGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 158 ASKEStdeiqLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDCfLGTNCPPVRVIGkG 237
Cdd:COG0128 83 EPDAV-----LDCGNSGTTMRLLTGLLALQPG--EVVLTGDESLRKRPMGRLLDPLRQLGARIES-RGGGYLPLTIRG-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 238 GLPGGTVKLSGSVSSQYLTALLMAAPLALGDVTIEIVDKLISVPYVEMTIKLMERFGVSVEHSDsWDRFLIRGGQKYKsP 317
Cdd:COG0128 154 PLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEG-YRRFTVPGGQRYR-P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 318 GNAFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPrapsgrkhLRAIDV 397
Cdd:COG0128 232 GDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSP--------LKGIDI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 398 NMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDDHR 477
Cdd:COG0128 304 DLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHR 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 1109197953 478 MAMAFSLAAC-AEVPVTIKDPGCTRKTFPDYFEVLQK 513
Cdd:COG0128 384 IAMAFAVAGLrAEGPVTIDDAECVAKSFPDFFELLES 420
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
77-516 |
3.03e-168 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 482.72 E-value: 3.03e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 77 EIVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDsaiqRATIEGSGGLF 156
Cdd:PRK02427 4 MLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIEDD----EVVVEGVGGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 157 PASKESTdeiqLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDcFLGTNCPPVRVigK 236
Cdd:PRK02427 80 LKEPEDV----LDCGNSGTTMRLLTGLLALQPG--EVVLTGDESLRKRPMGRLLDPLRQMGAKIE-GRDEGYLPLTI--R 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 237 GGLPGGTVKLSGSVSSQY----------LTAllmaaplalGDVTIEIVDKLISVPYVEMTIKLMERFGVSVEHSDSWD-- 304
Cdd:PRK02427 151 GGKKGGPIEYDGPVSSQFvksllllaplFAE---------GDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGyr 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 305 RFLIRGGQKYKsPGNAFVEGDASSASYFLAGAAVTGG-TVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPP 383
Cdd:PRK02427 222 RIVIKGGQRLR-GQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEREGGEPVG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 384 RAPSGRKHLRAIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPE 463
Cdd:PRK02427 301 DIRVRSSELKGIDIDIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1109197953 464 RLnvTEIDTYDDHRMAMAFSLAAC-AEVPVTIKDPGCTRKTFPDYFEVLQKFSK 516
Cdd:PRK02427 381 LA--GVVDSYGDHRIAMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLGA 432
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
86-514 |
4.11e-168 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 481.29 E-value: 4.11e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 86 ISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSaiQRATIEGSGGLFPaskesTDE 165
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG--GTVEIVGGGGLGL-----PPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 166 IQLFLGNAGTAMRPLTAAVVAAGGNarYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVrvIGKGGLPGGTVK 245
Cdd:cd01556 74 AVLDCGNSGTTMRLLTGLLALQGGD--SVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL--IGGGGLKGGEVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 246 LSGSVSSQYLTALLMAAPLALGDVTIEIVdKLISVPYVEMTIKLMERFGVSVEHSDsWDRFLIRGGQKYKSPgNAFVEGD 325
Cdd:cd01556 150 IPGAVSSQFKSALLLAAPLAEGPTTIIIG-ELESKPYIDHTERMLRAFGAEVEVDG-YRTITVKGGQKYKGP-EYTVEGD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 326 ASSASYFLAGAAVTGGTVTVEGCGTSSlqGDVKFAEVLEKMGAEVSWT-ENSVTVKGPPrapsgrkHLRAIDVNMNKMPD 404
Cdd:cd01556 227 ASSAAFFLAAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGnEDTVVVESGG-------KLKGIDIDGNDIPD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 405 VAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPE-RLNVTEIDTYDDHRMAMAFS 483
Cdd:cd01556 298 EAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVYTYGDHRIAMSFA 377
|
410 420 430
....*....|....*....|....*....|..
gi 1109197953 484 LAAC-AEVPVTIKDPGCTRKTFPDYFEVLQKF 514
Cdd:cd01556 378 IAGLvAEGGVTIEDPECVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
88-517 |
4.50e-167 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 478.69 E-value: 4.50e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 88 GTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAIqrATIEGSGGLFPaskestdEIQ 167
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEV--AVIEGVGGKEP-------QAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 168 LFLGNAGTAMRPLTAAVVAAGGNarYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVigKGGLPGGTVKLS 247
Cdd:TIGR01356 72 LDLGNSGTTARLLTGVLALADGE--VVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTI--SGPLPGGIVYIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 248 GSVSSQYLTALLMAAPLALGdVTIEIVD-KLISVPYVEMTIKLMERFGVSVEHSDSwDRFLIRGGQKYKSPGnAFVEGDA 326
Cdd:TIGR01356 148 GSASSQYKSALLLAAPALQA-VGITIVGePLKSRPYIEITLDLLGSFGVEVERSDG-RKIVVPGGQKYGPQG-YDVPGDY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 327 SSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPRapsgrkhLRAIDVNMNKMPDVA 406
Cdd:TIGR01356 225 SSAAFFLAAAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASG-------LKGIKIDMDDMIDEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 407 MTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDDHRMAMAFSLAA 486
Cdd:TIGR01356 298 PTLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAG 377
|
410 420 430
....*....|....*....|....*....|..
gi 1109197953 487 C-AEVPVTIKDPGCTRKTFPDYFEVLQKFSKH 517
Cdd:TIGR01356 378 LvAEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
81-511 |
1.15e-156 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 452.52 E-value: 1.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 81 QPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRV-EEDSAIQRATIEGSGGLFPAS 159
Cdd:pfam00275 1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIiKLDDEKSVVIVEGLGGSFEAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 160 kestDEIQLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVigkGGL 239
Cdd:pfam00275 81 ----EDLVLDMGNSGTALRPLTGRLALQSG--EVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKV---RGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 240 PGGTVKLSGSVSSQYLTALLMAAPLALGDVTIeiVDKLISVPYVEMTIKLMERFGVSVEHSDSWDRFLIRGGQKYKSpGN 319
Cdd:pfam00275 152 RLGGIHIDGDVSSQFVTSLLMLAALLAEGTTT--IENLASEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPG-QE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 320 AFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGPPrapsgrkHLRAIDVNM 399
Cdd:pfam00275 229 YRVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPP-------GLRGKAVDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 400 NKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPE-RLNVTEIDTYDDHRM 478
Cdd:pfam00275 302 RTAPDPAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYGDHRI 381
|
410 420 430
....*....|....*....|....*....|....
gi 1109197953 479 AMAFSLAAC-AEVPVTIKDPGCTRKTFPDYFEVL 511
Cdd:pfam00275 382 AMALALAGLvAEGETIIDDIECTDRSFPDFEEKL 415
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
76-509 |
1.24e-129 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 392.53 E-value: 1.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 76 EEIVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSaiQRATIEGSGGL 155
Cdd:PRK11861 241 EHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDG--GTCVVGGTRGA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 156 FPASKEStdeiqLFLGNAGTAMRPLTAAVVAAGGNarYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVIG 235
Cdd:PRK11861 319 FTAKTAD-----LFLGNAGTAVRPLTAALAVNGGE--YRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 236 KGGLPGGTVKLSGSVSSQYLTALLMA---APLALGDVTIEIVDKLISVPYVEMTIKLMERFGVSVEHsDSWDRFLIRGGQ 312
Cdd:PRK11861 392 ATISVDAPIRVRGDVSSQFLTALLMTlplVKAKDGASVVEIDGELISKPYIEITIKLMARFGVTVER-DGWQRFTVPAGV 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 313 KYKSPGNAFVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAEVSWTENSVTVKGpprapSGRKH- 391
Cdd:PRK11861 471 RYRSPGTIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVRG-----IGHDHg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 392 -LRAIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNV-TE 469
Cdd:PRK11861 546 rLAPIDMDFNLIPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTPnAS 625
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1109197953 470 IDTYDDHRMAMAFSLAACAEVPVTIKDPGCTRKTFPDYFE 509
Cdd:PRK11861 626 IDTYDDHRMAMCFSLVSLGGVPVRINDPKCVGKTFPDYFD 665
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
86-513 |
2.78e-104 |
|
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine enolpyruvyl transferase. Both enzymes catalyze the reaction of enolpyruvyl transfer.
Pssm-ID: 238795 Cd Length: 408 Bit Score: 318.39 E-value: 2.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 86 ISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAiqRATIEGSGGlfPASKESTDE 165
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDG--VITIQGVGM--AGLKAPQNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 166 iqLFLGNAGTAMRPLTAAVVAAGGnaRYVLDGVPRMRERPIGDLVEGLKQLGADVDCFLGTNCPPVRVigKGGLPGGTVK 245
Cdd:cd01554 77 --LNLGNSGTAIRLISGVLAGADF--EVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLK--GGKNLGPIHY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 246 LSGSVSSQYLTALLMAAPLALGDVTIEIVdklISVPYVEMTIKLMERFGVSVEhSDSWDRFLIRGGQKYKSPgNAFVEGD 325
Cdd:cd01554 151 EDPIASAQVKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHIS-VQGTKKIVVQGPQKLTGQ-KYVVPGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 326 ASSASYFLAGAAVTGGTVTVEGCGTSSlqGDVKFAEVLEKMGAEVSWTENSVTVKgpprapsgRKHLRAIDVNMN---KM 402
Cdd:cd01554 226 ISSAAFFLVAAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVE--------SSDLKATEICGAlipRL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 403 PDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDTYDDHRMAMAF 482
Cdd:cd01554 296 IDELPIIALLALQAQGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMT 375
|
410 420 430
....*....|....*....|....*....|..
gi 1109197953 483 SLAAC-AEVPVTIKDPGCTRKTFPDYFEVLQK 513
Cdd:cd01554 376 ALAALvADGEVELDRAEAINTSYPSFFDDLES 407
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
63-510 |
1.05e-32 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 132.43 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 63 ASVATTKKPSKAPEEIVLQPIKEISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDS 142
Cdd:PRK14806 289 ARRAYVEAMNANDVSYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGPH 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 143 AiQRATIEGSG--GLFPASKEstdeiqLFLGNAGTAMRPLTAAVVAAGGNAryVLDGVPRMRERPIGDLVEGLKQLGADV 220
Cdd:PRK14806 369 N-GRVTIHGVGlhGLKAPPGP------LYMGNSGTSMRLLSGLLAAQSFDS--VLTGDASLSKRPMERVAKPLREMGAVI 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 221 DCflGTNC-PPVRVIGKGGLPGGTVKLSGSvSSQYLTALLMAAPLALGDVTIeivdkLISVPYVEMTIKLMERFGVSVEH 299
Cdd:PRK14806 440 ET--GEEGrPPLSIRGGQRLKGIHYDLPMA-SAQVKSCLLLAGLYAEGETSV-----TEPAPTRDHTERMLRGFGYPVKV 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 300 SDswDRFLIRGGQKYKSpGNAFVEGDASSASYFLAGAAVTGGT-VTVEGCGTSSLQgdVKFAEVLEKMGAEVSwTENSVT 378
Cdd:PRK14806 512 EG--NTISVEGGGKLTA-TDIEVPADISSAAFFLVAASIAEGSeLTLEHVGINPTR--TGVIDILKLMGADIT-LENERE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 379 VKGPP----RAPSGRkhLRAIDVNMNKMP---DVAMTLAVVALFADGPTAIRDVASWRVKETERMIAVCTELRKLGATVE 451
Cdd:PRK14806 586 VGGEPvadiRVRGAR--LKGIDIPEDQVPlaiDEFPVLFVAAACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCE 663
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 452 EGPDYCIITPPErLNVTEIDTYDDHRMAMAFSLAAC-AEVPVTIKDPGCTRKTFPDYFEV 510
Cdd:PRK14806 664 PTPDGIIIEGGI-FGGGEVESHGDHRIAMSFSVASLrASGPITIHDCANVATSFPNFLEL 722
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
323-514 |
1.38e-29 |
|
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.
Pssm-ID: 238794 Cd Length: 211 Bit Score: 115.45 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 323 EGDASSASYFLAGAAVTGGTVTVEGCGTSS-----LQGDVKFAEVLEKM-GAEVSWTENSVTvkgppRAPSGRKHLRAID 396
Cdd:cd01553 7 KGGGQILRSFLVLAAISGGPITVTGIRPDRakpglLRQHLTFLKALEKIcGATVEGGELGSD-----RISFRPGTVRGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 397 VNMN-----KMPDVAMTLAVVALFADGPTAIRDVASWRV----KETERMIAVCTELRKLGATVEEGPD------------ 455
Cdd:cd01553 82 VRFAigsagSCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvv 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1109197953 456 YCIITPPERLNVTEIdtyddhRMAMAFSLAAcaeVPVTIKDPGCTRKTFPDYFEVLQKF 514
Cdd:cd01553 162 ATEVSPVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
86-488 |
1.21e-11 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.
Pssm-ID: 238796 Cd Length: 400 Bit Score: 66.34 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 86 ISGTVKLPGSKSLSNRILLLAALSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSA----IQRATIEgsggLFPASKE 161
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEntlvIDASNIN----STEAPYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 162 STDEIQ---LFLG----NAGTAMRPLtaavvaaggnaryvldgvP---RMRERPIgDL-VEGLKQLGADVDCFLGTncpp 230
Cdd:cd01555 77 LVRKMRasiLVLGpllaRFGEARVSL------------------PggcAIGARPV-DLhLKGLEALGAKIEIEDGY---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 231 VRVIGKGGLPGGTVKL------------SGSVSSQyltallmaaplalGDVTI-------EIVDkLIsvpyvEMTIKLme 291
Cdd:cd01555 134 VEAKAAGRLKGARIYLdfpsvgatenimMAAVLAE-------------GTTVIenaarepEIVD-LA-----NFLNKM-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 292 rfGVSVEHSDSwDRFLIRG-----GQKYKspgnafVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGdvkFAEVLEKM 366
Cdd:cd01555 193 --GAKIEGAGT-DTIRIEGverlhGAEHT------VIPDRIEAGTFLVAAAITGGDITVENVIPEHLEA---VLAKLREM 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 367 GAEVSWTENSVTVKGPPrapsgrKHLRAIDVNMNKMP----DVAMTLAVVALFADGPTAIRDvaswRVKEtERMIAVcTE 442
Cdd:cd01555 261 GAKIEIGEDGIRVDGDG------GRLKAVDIETAPYPgfptDLQAQFMALLTQAEGTSVITE----TIFE-NRFMHV-DE 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1109197953 443 LRKLGATVE-EGPDyCIITPPERLNVTEIDTyDDHRMAMAFSLAACA 488
Cdd:cd01555 329 LNRMGADIKvEGNT-AIIRGVTKLSGAPVMA-TDLRAGAALVLAGLA 373
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
87-465 |
1.01e-10 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 63.47 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 87 SGTVKLPGSKslsNRIL-LLAA--LSQGTTVIDNLLSSDDIHYMLGALRTLGLRVEEDSAiqrATIEgsgglFPASKEST 163
Cdd:COG0766 13 SGEVRISGAK---NAALpILAAalLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDG---GTLT-----IDASNINS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 164 DEIQ-----------LFLGnagtamrPLtaavvaaggnaryvldgVPRMRE-------------RPIgDL-VEGLKQLGA 218
Cdd:COG0766 82 TEAPyelvrkmrasiLVLG-------PL-----------------LARFGEarvslpggcaigaRPI-DLhLKGLEALGA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 219 DVDcflgtncppvrvIGKG-------GLPGGTVKLSG-SVssqyltallmaaplalG-------------DVTI------ 271
Cdd:COG0766 137 EIE------------IEHGyiearagRLKGARIYLDFpSV----------------GatenimmaavlaeGTTVienaar 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 272 --EIVDklisvpyvemTIKLMERFGVSVEHSDSwDRFLIRGGQKYKsPGNAFVEGD---ASSasyFLAGAAVTGGTVTVE 346
Cdd:COG0766 189 epEIVD----------LANFLNAMGAKIEGAGT-DTITIEGVEKLH-GAEHTVIPDrieAGT---FLVAAAITGGDVTVK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 347 GCGTSSLQGdvkFAEVLEKMGAEVSWTENSVTVKGPPRapsgrkhLRAIDVnmnK-------MPDVAMTLAVVALFADGp 419
Cdd:COG0766 254 NVIPEHLEA---VLAKLREAGVEIEEGDDGIRVRGPGR-------LKAVDI---KtapypgfPTDLQAQFMALLTQAEG- 319
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1109197953 420 TAIrdvaswrVKET---ERMIAVcTELRKLGATVEEGPDYCIITPPERL 465
Cdd:COG0766 320 TSV-------ITETvfeNRFMHV-DELNRMGADIKLDGHTAIVRGVTKL 360
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
332-488 |
2.33e-06 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 50.03 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 332 FLAGAAVTGGTVTVEGCGTSSLQGdvkFAEVLEKMGAEVSWTENSVTVKGPPRapsgrkhLRAIDVnmnK-------MPD 404
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEA---VLAKLREAGAEIEEGEDGIRVDMPGR-------LKAVDI---KtapypgfPTD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 405 ---VAMTLAVValfADGpTAIrdvaswrVKET---ERMIAVcTELRKLGATVEEGPDYCIITPPERLNVTEID-TydDHR 477
Cdd:PRK09369 307 mqaQFMALLTQ---AEG-TSV-------ITETifeNRFMHV-PELIRMGADIEVDGHTAVVRGVEKLSGAPVMaT--DLR 372
|
170
....*....|.
gi 1109197953 478 MAMAFSLAACA 488
Cdd:PRK09369 373 ASASLVLAGLV 383
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
360-472 |
2.24e-05 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 46.90 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 360 AEVLEKMGAEVSWTENSV-TVKGPPRapsgrkhLRAIDVNMnkMPD--VAMTLAVVALFADGPTAIRDVaswrvkETERM 436
Cdd:COG0766 196 ANFLNAMGAKIEGAGTDTiTIEGVEK-------LHGAEHTV--IPDriEAGTFLVAAAITGGDVTVKNV------IPEHL 260
|
90 100 110
....*....|....*....|....*....|....*.
gi 1109197953 437 IAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDT 472
Cdd:COG0766 261 EAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKT 296
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
360-472 |
2.13e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 43.87 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109197953 360 AEVLEKMGAEVS-WTENSVTVKGPPRapsgrkhLRAIDVNMnkMPD--VAMTLAVVALFADGPTAIRDVaswrvkETERM 436
Cdd:PRK09369 197 ANFLNKMGAKISgAGTDTITIEGVER-------LHGAEHTV--IPDriEAGTFLVAAAITGGDVTIRGA------RPEHL 261
|
90 100 110
....*....|....*....|....*....|....*.
gi 1109197953 437 IAVCTELRKLGATVEEGPDYCIITPPERLNVTEIDT 472
Cdd:PRK09369 262 EAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKT 297
|
|
| |
