|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-432 |
6.66e-160 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 458.07 E-value: 6.66e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKygRDLIVYGSGLDA 80
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIED--DEVVVEGVGGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFD 160
Cdd:PRK02427 80 LKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPIASAQVKSALIFSALQADEPSIIF--EKEATRNHLEI---MLNDFGADIK----TNGLCITVMPRPKLSGRTISIP 231
Cdd:PRK02427 160 YDGPVSSQFVKSLLLLAPLFAEGDTETTviEPLPSRPHTEItlrMLRAFGVEVEnvegWGYRRIVIKGGQRLRGQDITVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 232 GDISSAAFFMVAASLLPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEItakEI 309
Cdd:PRK02427 240 GDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVRSSELKGIDI---DI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 310 PNVIDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPklqiPENNLATHGDHR 389
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP----LAGVVDSYGDHR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488911987 390 IGMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:PRK02427 393 IAMAFAIAGLAAE--GPVTIDDPECVAKSFPDFFEDLASLGAN 433
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-429 |
1.38e-156 |
|
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: 449.15 E-value: 1.38e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKY-GRDLIVYGSGlD 79
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVG-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 80 AFKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAF 159
Cdd:COG0128 80 GLKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGP-LKGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 160 DYHLP-IASAQVKSALIFSALQADEPSIIF-----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPG 232
Cdd:COG0128 159 EYEIPgSASSQFKSALLLAGPLAEGGLEITvtgelESKPYRDHTERMLRAFGVEVEVEGYrRFTVPGGQRYRPGDYTVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 233 DISSAAFFMVAASLLpNSCICLKKVGLNPT--RIGIISVLKRMNANIEVKKTSneaeaygdIIVRSSNLHAVEITAKEIP 310
Cdd:COG0128 239 DISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG--------ITVRGSPLKGIDIDLSDIP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 311 nviDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQipENNLATHGDHRI 390
Cdd:COG0128 310 ---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLK--GAEVDSYGDHRI 384
|
410 420 430
....*....|....*....|....*....|....*....
gi 488911987 391 GMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYL 429
Cdd:COG0128 385 AMAFAVAGLRAE--GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-429 |
1.61e-145 |
|
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: 420.81 E-value: 1.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGlDAFKDPKKPLNMG 91
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 92 NSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAFDYHLPIA-SAQV 170
Cdd:cd01556 80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGG-LKGGEVEIPGAvSSQF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 171 KSALIFSALQADEPSIIF----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAAS 245
Cdd:cd01556 159 KSALLLAAPLAEGPTTIIigelESKPYIDHTERMLRAFGAEVEVDGYrTITVKGGQKYKGPEYTVEGDASSAAFFLAAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 246 LLPnSCICLKKVGLNPTRIGIISVLKRMNANIEVKKTsneaeayGDIIVRSSN-LHAVEITAKEIPnviDELPILTLAAS 324
Cdd:cd01556 239 ITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNE-------DTVVVESGGkLKGIDIDGNDIP---DEAPTLAVLAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 325 LAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCP-KLQIPENNlaTHGDHRIGMMLAVAALLVDT 403
Cdd:cd01556 308 FAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVY--TYGDHRIAMSFAIAGLVAEG 385
|
410 420
....*....|....*....|....*.
gi 488911987 404 SktITLNNPEAIKISYPNFFRDLDYL 429
Cdd:cd01556 386 G--VTIEDPECVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-432 |
6.36e-116 |
|
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: 345.41 E-value: 6.36e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 14 GSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGldaFKDPKKPLNMGNS 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVG---GKEPQAELDLGNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 94 GTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEF-SLTGNGTLPITVIGHPSLkAFDYHLPIASAQVKS 172
Cdd:TIGR01356 78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIsSLEGGGSLPLTISGPLPG-GIVYISGSASSQYKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 173 ALIFSA--LQADEPSIIFEKEATRNHLEIMLNDFGADI----KTNGLCITVMPRPKLSGRTISIPGDISSAAFFMVAAsL 246
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFGveveRSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA-A 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 247 LPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKtsneaeayGDIIVR-SSNLHAVEItakEIPNVIDELPILTLAA 323
Cdd:TIGR01356 236 ITGGRVTLENLGINPTQGDkaIIIVLEEMGADIEVEE--------DDLIVEgASGLKGIKI---DMDDMIDELPTLAVLA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 324 SLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATHGDHRIGMMLAVAALLVDt 403
Cdd:TIGR01356 305 AFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAV--VDTFGDHRIAMAFAVAGLVAE- 381
|
410 420
....*....|....*....|....*....
gi 488911987 404 sKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:TIGR01356 382 -GEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
12-426 |
5.17e-98 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 299.60 E-value: 5.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRD---LIVYGSGLDAFKDPKKPL 88
Cdd:pfam00275 6 LSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEksvVIVEGLGGSFEAPEDLVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 89 NMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGE-FSLTGNGTLPITVIGHPsLKAFDYHLPIAS 167
Cdd:pfam00275 86 DMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEiEGREGYNYAPLKVRGLR-LGGIHIDGDVSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 168 AQVKSALIFSALQADEPSII--FEKEATRNHLEIMLNDFGADIKTNG--LCITVMPRPKLSGRTISIPGDISSAAFFMVA 243
Cdd:pfam00275 165 QFVTSLLMLAALLAEGTTTIenLASEPYIDDTENMLKKFGAKIEGSGteLSITVKGGEKLPGQEYRVEGDRSSAAYFLVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 244 ASLLPnSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSneaeaygDIIVRSSNLHAVEItakEIPNVIDELPILTL 321
Cdd:pfam00275 245 AAITG-GTVTVENVGINSLQGDeaLLEILEKMGAEITQEEDA-------DIVVGPPGLRGKAV---DIRTAPDPAPTTAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 322 AASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGM-VIDGCPKLQIPEnnLATHGDHRIGMMLAVAALL 400
Cdd:pfam00275 314 LAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAE--VDSYGDHRIAMALALAGLV 391
|
410 420
....*....|....*....|....*.
gi 488911987 401 VDTSKTItlNNPEAIKISYPNFFRDL 426
Cdd:pfam00275 392 AEGETII--DDIECTDRSFPDFEEKL 415
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-432 |
6.66e-160 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 458.07 E-value: 6.66e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKygRDLIVYGSGLDA 80
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIED--DEVVVEGVGGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFD 160
Cdd:PRK02427 80 LKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPIASAQVKSALIFSALQADEPSIIF--EKEATRNHLEI---MLNDFGADIK----TNGLCITVMPRPKLSGRTISIP 231
Cdd:PRK02427 160 YDGPVSSQFVKSLLLLAPLFAEGDTETTviEPLPSRPHTEItlrMLRAFGVEVEnvegWGYRRIVIKGGQRLRGQDITVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 232 GDISSAAFFMVAASLLPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEItakEI 309
Cdd:PRK02427 240 GDPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVRSSELKGIDI---DI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 310 PNVIDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPklqiPENNLATHGDHR 389
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP----LAGVVDSYGDHR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488911987 390 IGMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:PRK02427 393 IAMAFAIAGLAAE--GPVTIDDPECVAKSFPDFFEDLASLGAN 433
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-429 |
1.38e-156 |
|
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: 449.15 E-value: 1.38e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKY-GRDLIVYGSGlD 79
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGVG-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 80 AFKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAF 159
Cdd:COG0128 80 GLKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGP-LKGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 160 DYHLP-IASAQVKSALIFSALQADEPSIIF-----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPG 232
Cdd:COG0128 159 EYEIPgSASSQFKSALLLAGPLAEGGLEITvtgelESKPYRDHTERMLRAFGVEVEVEGYrRFTVPGGQRYRPGDYTVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 233 DISSAAFFMVAASLLpNSCICLKKVGLNPT--RIGIISVLKRMNANIEVKKTSneaeaygdIIVRSSNLHAVEITAKEIP 310
Cdd:COG0128 239 DISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG--------ITVRGSPLKGIDIDLSDIP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 311 nviDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQipENNLATHGDHRI 390
Cdd:COG0128 310 ---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLK--GAEVDSYGDHRI 384
|
410 420 430
....*....|....*....|....*....|....*....
gi 488911987 391 GMMLAVAALLVDtsKTITLNNPEAIKISYPNFFRDLDYL 429
Cdd:COG0128 385 AMAFAVAGLRAE--GPVTIDDAECVAKSFPDFFELLESL 421
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-429 |
1.61e-145 |
|
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: 420.81 E-value: 1.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGlDAFKDPKKPLNMG 91
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 92 NSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPsLKAFDYHLPIA-SAQV 170
Cdd:cd01556 80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGG-LKGGEVEIPGAvSSQF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 171 KSALIFSALQADEPSIIF----EKEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAAS 245
Cdd:cd01556 159 KSALLLAAPLAEGPTTIIigelESKPYIDHTERMLRAFGAEVEVDGYrTITVKGGQKYKGPEYTVEGDASSAAFFLAAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 246 LLPnSCICLKKVGLNPTRIGIISVLKRMNANIEVKKTsneaeayGDIIVRSSN-LHAVEITAKEIPnviDELPILTLAAS 324
Cdd:cd01556 239 ITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNE-------DTVVVESGGkLKGIDIDGNDIP---DEAPTLAVLAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 325 LAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCP-KLQIPENNlaTHGDHRIGMMLAVAALLVDT 403
Cdd:cd01556 308 FAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPlKGAGVEVY--TYGDHRIAMSFAIAGLVAEG 385
|
410 420
....*....|....*....|....*.
gi 488911987 404 SktITLNNPEAIKISYPNFFRDLDYL 429
Cdd:cd01556 386 G--VTIEDPECVAKSFPNFFEDLESL 409
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
12-422 |
6.11e-134 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 402.07 E-value: 6.11e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIK--KYGRdLIVYGSGLDAFKDPKKPLN 89
Cdd:PRK14806 312 VKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEgpHNGR-VTIHGVGLHGLKAPPGPLY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 90 MGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFDYHLPIASAQ 169
Cdd:PRK14806 391 MGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEGRPPLSIRGGQRLKGIHYDLPMASAQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 170 VKSALIFSALQADEPSIIFEKEATRNHLEIMLNDFGADIKTNGLCITVMPRPKLSGRTISIPGDISSAAFFMVAASLLPN 249
Cdd:PRK14806 471 VKSCLLLAGLYAEGETSVTEPAPTRDHTERMLRGFGYPVKVEGNTISVEGGGKLTATDIEVPADISSAAFFLVAASIAEG 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 250 SCICLKKVGLNPTRIGIISVLKRMNANIEVkktSNEAEAYG----DIIVRSSNLHAVEITAKEIPNVIDELPILTLAASL 325
Cdd:PRK14806 551 SELTLEHVGINPTRTGVIDILKLMGADITL---ENEREVGGepvaDIRVRGARLKGIDIPEDQVPLAIDEFPVLFVAAAC 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 326 AKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCpklQIPENNLATHGDHRIGMMLAVAALlvDTSK 405
Cdd:PRK14806 628 AEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGG---IFGGGEVESHGDHRIAMSFSVASL--RASG 702
|
410
....*....|....*..
gi 488911987 406 TITLNNPEAIKISYPNF 422
Cdd:PRK14806 703 PITIHDCANVATSFPNF 719
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-432 |
6.36e-116 |
|
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: 345.41 E-value: 6.36e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 14 GSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGldaFKDPKKPLNMGNS 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVG---GKEPQAELDLGNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 94 GTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEF-SLTGNGTLPITVIGHPSLkAFDYHLPIASAQVKS 172
Cdd:TIGR01356 78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIsSLEGGGSLPLTISGPLPG-GIVYISGSASSQYKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 173 ALIFSA--LQADEPSIIFEKEATRNHLEIMLNDFGADI----KTNGLCITVMPRPKLSGRTISIPGDISSAAFFMVAAsL 246
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFGveveRSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA-A 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 247 LPNSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKtsneaeayGDIIVR-SSNLHAVEItakEIPNVIDELPILTLAA 323
Cdd:TIGR01356 236 ITGGRVTLENLGINPTQGDkaIIIVLEEMGADIEVEE--------DDLIVEgASGLKGIKI---DMDDMIDELPTLAVLA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 324 SLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATHGDHRIGMMLAVAALLVDt 403
Cdd:TIGR01356 305 AFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAV--VDTFGDHRIAMAFAVAGLVAE- 381
|
410 420
....*....|....*....|....*....
gi 488911987 404 sKTITLNNPEAIKISYPNFFRDLDYLLNN 432
Cdd:TIGR01356 382 -GEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
12-426 |
5.17e-98 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 299.60 E-value: 5.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRD---LIVYGSGLDAFKDPKKPL 88
Cdd:pfam00275 6 LSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEksvVIVEGLGGSFEAPEDLVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 89 NMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGE-FSLTGNGTLPITVIGHPsLKAFDYHLPIAS 167
Cdd:pfam00275 86 DMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEiEGREGYNYAPLKVRGLR-LGGIHIDGDVSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 168 AQVKSALIFSALQADEPSII--FEKEATRNHLEIMLNDFGADIKTNG--LCITVMPRPKLSGRTISIPGDISSAAFFMVA 243
Cdd:pfam00275 165 QFVTSLLMLAALLAEGTTTIenLASEPYIDDTENMLKKFGAKIEGSGteLSITVKGGEKLPGQEYRVEGDRSSAAYFLVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 244 ASLLPnSCICLKKVGLNPTRIG--IISVLKRMNANIEVKKTSneaeaygDIIVRSSNLHAVEItakEIPNVIDELPILTL 321
Cdd:pfam00275 245 AAITG-GTVTVENVGINSLQGDeaLLEILEKMGAEITQEEDA-------DIVVGPPGLRGKAV---DIRTAPDPAPTTAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 322 AASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGM-VIDGCPKLQIPEnnLATHGDHRIGMMLAVAALL 400
Cdd:pfam00275 314 LAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAE--VDSYGDHRIAMALALAGLV 391
|
410 420
....*....|....*....|....*.
gi 488911987 401 VDTSKTItlNNPEAIKISYPNFFRDL 426
Cdd:pfam00275 392 AEGETII--DDIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-429 |
1.88e-94 |
|
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: 290.27 E-value: 1.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGLDAFKDPKKPLNMG 91
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 92 NSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAFDYHLPIASAQVK 171
Cdd:cd01554 81 NSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 172 SALIFSALQADEPSIIFE--KEATRNHLEIMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAASLLP 248
Cdd:cd01554 161 SALMFAALLAKGETVIIEaaKEPTINHTENMLQTFGGHISVQGTkKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAIAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 249 NSCIClKKVGLNPTRIGIISVLKRMNANIEVkktsneAEAYgdIIVRSSNLHAVEITAKEIPNVIDELPILTLAASLAKG 328
Cdd:cd01554 241 GRLVL-QNVGINETRTGIIDVLRAMGAKIEI------GEDT--ISVESSDLKATEICGALIPRLIDELPIIALLALQAQG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 329 RTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATHGDHRIGMMLAVAALLVDTskTIT 408
Cdd:cd01554 312 TTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGAR--VNTFGDHRIGMMTALAALVADG--EVE 387
|
410 420
....*....|....*....|.
gi 488911987 409 LNNPEAIKISYPNFFRDLDYL 429
Cdd:cd01554 388 LDRAEAINTSYPSFFDDLESL 408
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-423 |
9.20e-33 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 130.98 E-value: 9.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 1 MKNLKTKQFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGrDLIVYGSGLDA 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDG-GTCVVGGTRGA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 81 FKDPKKPLNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIgHPSLKAFD 160
Cdd:PRK11861 319 FTAKTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRI-RPATISVD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 161 YHLPI---ASAQVKSALIFSA--LQADEPSIIFEKEA---TRNHLEI---MLNDFGADIKTNGLCITVMP---RPKLSGr 226
Cdd:PRK11861 398 APIRVrgdVSSQFLTALLMTLplVKAKDGASVVEIDGeliSKPYIEItikLMARFGVTVERDGWQRFTVPagvRYRSPG- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 227 TISIPGDISSAAFFMvAASLLPNSCICLKKVGLNPTR--IGIISVLKRMNANIEVKKTSNEAEAYGDiivRSSNLHAVEI 304
Cdd:PRK11861 477 TIMVEGDASSASYFL-AAGALGGGPLRVEGVGRASIQgdVGFANALMQMGANVTMGDDWIEVRGIGH---DHGRLAPIDM 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 305 TAKEIPnviDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQiPENNLAT 384
Cdd:PRK11861 553 DFNLIP---DAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLT-PNASIDT 628
|
410 420 430
....*....|....*....|....*....|....*....
gi 488911987 385 HGDHRIGMMLAVAALlvdTSKTITLNNPEAIKISYPNFF 423
Cdd:PRK11861 629 YDDHRMAMCFSLVSL---GGVPVRINDPKCVGKTFPDYF 664
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
8-426 |
4.79e-28 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 117.07 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 8 QFQGLNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRDLIVYGSGlDAFKDPKKP 87
Cdd:PRK11860 11 PLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYRITGLG-GQFPVKQAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 88 LNMGNSGTTTRLLLGLLAGQSFNTCLVGDASLSKRPMYRVTNPITEVGGEFSLTGNGTLPITVIGHPSLKAfdyHLPIA- 166
Cdd:PRK11860 90 LFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRL---DAPIRv 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 167 ----SAQVKSALIFSALQADEPSIIFE---KEATRNHLEIMLN---DFGADIKTNGLCITVMP---RPKLSGrTISIPGD 233
Cdd:PRK11860 167 rgdvSSQFLTALLMALPLVARRDITIEvvgELISKPYIEITLNllaRFGIAVQREGWQRFTIPagsRYRSPG-EIHVEGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 234 ISSAAFFMVAASLLPNSCICLKKVGLNPTR--IGIISVLKRMNANIEVKKTSNEAEAygdiivRSSNLHAVEITAKEIPn 311
Cdd:PRK11860 246 ASSASYFIAAGAIAGGAPVRIEGVGRDSIQgdIRFAEAARAMGAQVTSGPNWLEVRR------GAWPLKAIDLDCNHIP- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 312 viDELPILTLAASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDgcPKLQIPENNLA---THGDH 388
Cdd:PRK11860 319 --DAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVT--PPAQAADWKAAaihTYDDH 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 488911987 389 RIGMMLAVAALlvDTSKT-ITLNNPEAIKISYPNFFRDL 426
Cdd:PRK11860 395 RMAMCFSLAAF--NPAGLpVRINDPKCVAKTFPDYFEAL 431
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
12-426 |
1.61e-21 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 96.36 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 12 LNGSLLLPGDKSISHRSIMVASISWGISRIKNFSNSTDCLSTLNAFLDLGVEIKKYGRD--LIVYGSG--LDAFKDPKKP 87
Cdd:PLN02338 12 ISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENnrAVVEGCGgkFPVSGDSKED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 88 --LNMGNSGTTTRLLLGLLAGQSFNTCLVGD--ASLSKRPMYRVTNPITEVGGEFSLT-GNGTLPITVIGHPSLKAFDYH 162
Cdd:PLN02338 92 veLFLGNAGTAMRPLTAAVTAAGGNASYVLDgvPRMRERPIGDLVDGLKQLGADVECTlGTNCPPVRVNAAGGLPGGKVK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 163 LP-IASAQVKSALIFSALQA--DEPSIIFEKEATRNHLEI---MLNDFGADIKTNGlcitVMPRPKLSG-------RTIS 229
Cdd:PLN02338 172 LSgSISSQYLTALLMAAPLAlgDVEIEIVDKLISVPYVEMtlkLMERFGVSVEHSD----SWDRFFIKGgqkykspGNAY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 230 IPGDISSAAFFMVAASLLPNScICLKKVGLNPTR--IGIISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEITAK 307
Cdd:PLN02338 248 VEGDASSASYFLAGAAITGGT-VTVEGCGTTSLQgdVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKAIDVNMN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 308 EIPNVidelpILTLA--ASLAKGRTIISGAGELRVKETDRISVVAAELKKLGARIQEKSDGMVIDGCPKLQIPEnnLATH 385
Cdd:PLN02338 327 KMPDV-----AMTLAvvALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAE--IDTY 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 488911987 386 GDHRIGMMLAVAAlLVDTSktITLNNPEAIKISYPNFFRDL 426
Cdd:PLN02338 400 DDHRMAMAFSLAA-CGDVP--VTINDPGCTRKTFPTYFDVL 437
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
200-399 |
7.64e-09 |
|
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: 57.10 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 200 MLNDFGADIK---TNGLCIT-VmprPKLSGRTISIPGDISSAAFFMVAASLLpNSCICLKKVglNPTRIG-IISVLKRMN 274
Cdd:cd01555 188 FLNKMGAKIEgagTDTIRIEgV---ERLHGAEHTVIPDRIEAGTFLVAAAIT-GGDITVENV--IPEHLEaVLAKLREMG 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 275 ANIEVKKTSneaeaygdIIVRSS--NLHAVEITAKEIPNVI-DELPILTLAASLAKGRTIISgagelrvkET---DRISV 348
Cdd:cd01555 262 AKIEIGEDG--------IRVDGDggRLKAVDIETAPYPGFPtDLQAQFMALLTQAEGTSVIT--------ETifeNRFMH 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488911987 349 VAaELKKLGARIQEKSDGMVIDGCPKLQIPEnNLAThgDHRIGMMLAVAAL 399
Cdd:cd01555 326 VD-ELNRMGADIKVEGNTAIIRGVTKLSGAP-VMAT--DLRAGAALVLAGL 372
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
181-421 |
1.07e-05 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 47.54 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 181 ADEPSIIfeKEATrnhleiMLNDFGADIKTNGL-CITVMPRPKLSGRTISIPGDISSAAFFMVAASllpnscICLKKVGL 259
Cdd:PRK12830 186 AKEPEII--DVAT------LLNNMGANIKGAGTdVIRIEGVDELHGCRHTVIPDRIEAGTYMILAA------ACGGGVTI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 260 N---PTRI-GIISVLKRMNANIEVKKTSneaeaygdIIVRSS-NLHAVEITAKEIPNVIDEL--PILTLAaSLAKGRTII 332
Cdd:PRK12830 252 NnviPEHLeSFIAKLEEMGVRVEVNEDS--------IFVEKQgNLKAVDIKTLPYPGFATDLqqPLTPLL-LKANGRSVV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 333 SGA-GELRVKETDrisvvaaELKKLGARIQEKSDGMVIDGCPKLQIPENNlAThgDHRIGMMLAVAALLVDTSKTITlnN 411
Cdd:PRK12830 323 TDTiYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGAKVK-AT--DLRAGAALVIAGLMAEGVTEIT--N 390
|
250
....*....|
gi 488911987 412 PEAIKISYPN 421
Cdd:PRK12830 391 IEHIDRGYSN 400
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
267-390 |
1.13e-04 |
|
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: 44.21 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 267 ISVLKRMNANIEVKKtsneaeayGDIIVRSSNLHAVEI-------TAKEipNVIdelpiltLAASLAKGRTIISGAGelr 339
Cdd:COG0766 128 LKGLEALGAEIEIEH--------GYIEARAGRLKGARIyldfpsvGATE--NIM-------MAAVLAEGTTVIENAA--- 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488911987 340 vKE---TDrisvVAAELKKLGARIQ-EKSDGMVIDGCPKLqipennlatHG-DHRI 390
Cdd:COG0766 188 -REpeiVD----LANFLNAMGAKIEgAGTDTITIEGVEKL---------HGaEHTV 229
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
267-411 |
3.51e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 42.71 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 267 ISVLKRMNANIEVKKTSNEAEAYGdiivrssNLHAVEI-------TAKEipNVIdelpiltLAASLAKGRTIISGAGelr 339
Cdd:PRK09369 128 LKGLEALGAEIEIEHGYVEAKADG-------RLKGAHIvldfpsvGATE--NIL-------MAAVLAEGTTVIENAA--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 340 vKETDrisVV--AAELKKLGARIQ-EKSDGMVIDGCPKLqipennlatHG-DHRIG---------MMLAVAallvdTSKT 406
Cdd:PRK09369 189 -REPE---IVdlANFLNKMGAKISgAGTDTITIEGVERL---------HGaEHTVIpdrieagtfLVAAAI-----TGGD 250
|
....*
gi 488911987 407 ITLNN 411
Cdd:PRK09369 251 VTIRG 255
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
195-361 |
1.84e-03 |
|
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: 40.35 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 195 NHLEIMLN---DFGADIKTNGLCITVMPRPKLSgrtisiPGDISSA----------AFFMVAASLLPNSCICLKKVglNP 261
Cdd:COG0766 258 EHLEAVLAklrEAGVEIEEGDDGIRVRGPGRLK------AVDIKTApypgfptdlqAQFMALLTQAEGTSVITETV--FE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 262 TRIGIISVLKRMNANIEVKKTSneaeaygdIIVR-SSNLHAVEITAkeipnvidelPI------LTLAASLAKGRTIISG 334
Cdd:COG0766 330 NRFMHVDELNRMGADIKLDGHT--------AIVRgVTKLSGAPVMA----------TDlragaaLVLAGLAAEGETVIDN 391
|
170 180 190
....*....|....*....|....*....|.
gi 488911987 335 AGELrvketDR----IsvvAAELKKLGARIQ 361
Cdd:COG0766 392 IYHI-----DRgyenL---EEKLRALGADIE 414
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
267-376 |
5.23e-03 |
|
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: 38.99 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488911987 267 ISVLKRMNANIEVKKTSNEAEAYGDIIVRSSNLHAVEITAKEipNVIdelpiltLAASLAKGRTIISGAGelrvKETDrI 346
Cdd:cd01555 117 LKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATE--NIM-------MAAVLAEGTTVIENAA----REPE-I 182
|
90 100 110
....*....|....*....|....*....|.
gi 488911987 347 SVVAAELKKLGARIQ-EKSDGMVIDGCPKLQ 376
Cdd:cd01555 183 VDLANFLNKMGAKIEgAGTDTIRIEGVERLH 213
|
|
|