|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
9-444 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 540.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 9 PATARHSQALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIrkEGDVWIINGVGNGCLL 88
Cdd:PRK02427 4 MLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI--EDDEVVVEGVGGGGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 89 QPEAPLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPIAYR 168
Cdd:PRK02427 82 EPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIEYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 169 VPMASAQVKSAVLLAGLNTPG--VTTVIEPVMTRDHTE---KMLQGFGADLTVEtDKDGVRHIRIVGQGKLTGQTIDVPG 243
Cdd:PRK02427 162 GPVSSQFVKSLLLLAPLFAEGdtETTVIEPLPSRPHTEitlRMLRAFGVEVENV-EGWGYRRIVIKGGQRLRGQDITVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 244 DPSSTAFPLVAALLVEGSEVTIRNVLMNPTRTG--LILTLQEMGADIEIIDPRLaGGEDVADLRVKASKLKGVVVPperA 321
Cdd:PRK02427 241 DPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENERE-GGEPVGDIRVRSSELKGIDID---I 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 322 PSMIDEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpggKGLGGGTVATHLDH 401
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIIT-----GGPLAGVVDSYGDH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 514200059 402 RIAMSFLVMGLASEKPVTVDDSTMIATSFPEFMGMMAGLGAKI 444
Cdd:PRK02427 392 RIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANI 434
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
11-440 |
2.03e-176 |
|
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: 500.00 E-value: 2.03e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 11 TARHSQALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARI-RKEGDVWIINGVGnGCLLQ 89
Cdd:COG0128 5 TIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIeELDGGTLRVTGVG-GGLKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 90 PEAPLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRtANPIAYRV 169
Cdd:COG0128 84 PDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGP-LKGGEYEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 170 P-MASAQVKSAVLLAGLNTPG-----VTTVIEPVMTRDHTEKMLQGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPG 243
Cdd:COG0128 163 PgSASSQFKSALLLAGPLAEGgleitVTGELESKPYRDHTERMLRAFGVEVEV----EGYRRFTVPGGQRYRPGDYTVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 244 DPSSTAFPLVAALLVeGSEVTIRNVLMNPT--RTGLILTLQEMGADIEIIDPRlaggedvadLRVKASKLKGVVVPPERA 321
Cdd:COG0128 239 DISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG---------ITVRGSPLKGIDIDLSDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 322 PsmiDEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpGGKGLGGGTVATHLDH 401
Cdd:COG0128 309 P---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIE---GGPKLKGAEVDSYGDH 382
|
410 420 430
....*....|....*....|....*....|....*....
gi 514200059 402 RIAMSFLVMGLASEKPVTVDDSTMIATSFPEFMGMMAGL 440
Cdd:COG0128 383 RIAMAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
18-440 |
1.97e-162 |
|
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: 463.95 E-value: 1.97e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 18 LTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIINGVGnGCLLQPEAPLDFG 97
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 98 NAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGD-RMPLTLIGPRTANPIAYRVPmASAQV 176
Cdd:cd01556 80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGgYPPLIGGGGLKGGEVEIPGA-VSSQF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 177 KSAVLLAGLNTPGVTTVI----EPVMTRDHTEKMLQGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPL 252
Cdd:cd01556 159 KSALLLAAPLAEGPTTIIigelESKPYIDHTERMLRAFGAEVEV----DGYRTITVKGGQKYKGPEYTVEGDASSAAFFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 253 VAALLVeGSEVTIRNVLMNPTRTGLILTLQEMGADIEIIDPRLAGGEDVAdlrvkasKLKGVVVPPERapsMIDEYPVLA 332
Cdd:cd01556 235 AAAAIT-GSEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVVVESGG-------KLKGIDIDGND---IPDEAPTLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 333 IAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrPGGKGLGGGTVATHLDHRIAMSFLVMGL 412
Cdd:cd01556 304 VLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIE--GGPLKGAGVEVYTYGDHRIAMSFAIAGL 381
|
410 420
....*....|....*....|....*...
gi 514200059 413 ASEKPVTVDDSTMIATSFPEFMGMMAGL 440
Cdd:cd01556 382 VAEGGVTIEDPECVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
20-443 |
1.93e-157 |
|
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: 451.34 E-value: 1.93e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 20 GEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIINGVGNgclLQPEAPLDFGNA 99
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGG---KEPQAELDLGNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 100 GTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGD-RMPLTLIGPRTANPIaYRVPMASAQVKS 178
Cdd:TIGR01356 78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGgSLPLTISGPLPGGIV-YISGSASSQYKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 179 AVLLAG--LNTPGVTTVIEPVMTRDHTEKMLQGFGADLtVETDKDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPLVAAL 256
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFG-VEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 257 LVeGSEVTIRNVLMNPTRTG--LILTLQEMGADIEIIDprlaggedvADLRVK-ASKLKGVVVppeRAPSMIDEYPVLAI 333
Cdd:TIGR01356 236 IT-GGRVTLENLGINPTQGDkaIIIVLEEMGADIEVEE---------DDLIVEgASGLKGIKI---DMDDMIDELPTLAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 334 AASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpGGKGLGGGTVATHLDHRIAMSFLVMGLA 413
Cdd:TIGR01356 303 LAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIR---GKKELKGAVVDTFGDHRIAMAFAVAGLV 379
|
410 420 430
....*....|....*....|....*....|
gi 514200059 414 SEKPVTVDDSTMIATSFPEFMGMMAGLGAK 443
Cdd:TIGR01356 380 AEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
15-433 |
2.00e-104 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 316.55 E-value: 2.00e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 15 SQALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGA---RIRKEGDVWIINGVGNGCLLQPE 91
Cdd:pfam00275 3 GSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeiiKLDDEKSVVIVEGLGGSFEAPED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 92 APLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPIAYRVPM 171
Cdd:pfam00275 83 LVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHIDGDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 172 ASAQVKSAVLLAGLNTPGVTTVIEPV--MTRDHTEKMLQGFGADLTVETDKDGvrhIRIVGQGKLTGQTIDVPGDPSSTA 249
Cdd:pfam00275 163 SSQFVTSLLMLAALLAEGTTTIENLAsePYIDDTENMLKKFGAKIEGSGTELS---ITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 250 FPLVAALLVEGsEVTIRNVLMNPTRTGLIL--TLQEMGADIEiidprlagGEDVADLRVKASKLKGVvvpPERAPSMIDE 327
Cdd:pfam00275 240 YFLVAAAITGG-TVTVENVGINSLQGDEALleILEKMGAEIT--------QEEDADIVVGPPGLRGK---AVDIRTAPDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 328 YPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrPGGKGLGGGTVATHLDHRIAMSF 407
Cdd:pfam00275 308 APTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIII--PAVKELKGAEVDSYGDHRIAMAL 385
|
410 420
....*....|....*....|....*.
gi 514200059 408 LVMGLASEKPVTVDDSTMIATSFPEF 433
Cdd:pfam00275 386 ALAGLVAEGETIIDDIECTDRSFPDF 411
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
9-444 |
0e+00 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 540.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 9 PATARHSQALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIrkEGDVWIINGVGNGCLL 88
Cdd:PRK02427 4 MLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI--EDDEVVVEGVGGGGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 89 QPEAPLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPIAYR 168
Cdd:PRK02427 82 EPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKGGPIEYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 169 VPMASAQVKSAVLLAGLNTPG--VTTVIEPVMTRDHTE---KMLQGFGADLTVEtDKDGVRHIRIVGQGKLTGQTIDVPG 243
Cdd:PRK02427 162 GPVSSQFVKSLLLLAPLFAEGdtETTVIEPLPSRPHTEitlRMLRAFGVEVENV-EGWGYRRIVIKGGQRLRGQDITVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 244 DPSSTAFPLVAALLVEGSEVTIRNVLMNPTRTG--LILTLQEMGADIEIIDPRLaGGEDVADLRVKASKLKGVVVPperA 321
Cdd:PRK02427 241 DPSSAAFFLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENERE-GGEPVGDIRVRSSELKGIDID---I 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 322 PSMIDEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpggKGLGGGTVATHLDH 401
Cdd:PRK02427 317 PDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIIT-----GGPLAGVVDSYGDH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 514200059 402 RIAMSFLVMGLASEKPVTVDDSTMIATSFPEFMGMMAGLGAKI 444
Cdd:PRK02427 392 RIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANI 434
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
11-440 |
2.03e-176 |
|
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: 500.00 E-value: 2.03e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 11 TARHSQALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARI-RKEGDVWIINGVGnGCLLQ 89
Cdd:COG0128 5 TIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIeELDGGTLRVTGVG-GGLKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 90 PEAPLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRtANPIAYRV 169
Cdd:COG0128 84 PDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGP-LKGGEYEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 170 P-MASAQVKSAVLLAGLNTPG-----VTTVIEPVMTRDHTEKMLQGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPG 243
Cdd:COG0128 163 PgSASSQFKSALLLAGPLAEGgleitVTGELESKPYRDHTERMLRAFGVEVEV----EGYRRFTVPGGQRYRPGDYTVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 244 DPSSTAFPLVAALLVeGSEVTIRNVLMNPT--RTGLILTLQEMGADIEIIDPRlaggedvadLRVKASKLKGVVVPPERA 321
Cdd:COG0128 239 DISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG---------ITVRGSPLKGIDIDLSDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 322 PsmiDEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpGGKGLGGGTVATHLDH 401
Cdd:COG0128 309 P---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIE---GGPKLKGAEVDSYGDH 382
|
410 420 430
....*....|....*....|....*....|....*....
gi 514200059 402 RIAMSFLVMGLASEKPVTVDDSTMIATSFPEFMGMMAGL 440
Cdd:COG0128 383 RIAMAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
18-440 |
1.97e-162 |
|
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: 463.95 E-value: 1.97e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 18 LTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIINGVGnGCLLQPEAPLDFG 97
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 98 NAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGD-RMPLTLIGPRTANPIAYRVPmASAQV 176
Cdd:cd01556 80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGgYPPLIGGGGLKGGEVEIPGA-VSSQF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 177 KSAVLLAGLNTPGVTTVI----EPVMTRDHTEKMLQGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPL 252
Cdd:cd01556 159 KSALLLAAPLAEGPTTIIigelESKPYIDHTERMLRAFGAEVEV----DGYRTITVKGGQKYKGPEYTVEGDASSAAFFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 253 VAALLVeGSEVTIRNVLMNPTRTGLILTLQEMGADIEIIDPRLAGGEDVAdlrvkasKLKGVVVPPERapsMIDEYPVLA 332
Cdd:cd01556 235 AAAAIT-GSEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVVVESGG-------KLKGIDIDGND---IPDEAPTLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 333 IAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrPGGKGLGGGTVATHLDHRIAMSFLVMGL 412
Cdd:cd01556 304 VLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIE--GGPLKGAGVEVYTYGDHRIAMSFAIAGL 381
|
410 420
....*....|....*....|....*...
gi 514200059 413 ASEKPVTVDDSTMIATSFPEFMGMMAGL 440
Cdd:cd01556 382 VAEGGVTIEDPECVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
20-443 |
1.93e-157 |
|
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: 451.34 E-value: 1.93e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 20 GEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIINGVGNgclLQPEAPLDFGNA 99
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGG---KEPQAELDLGNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 100 GTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGD-RMPLTLIGPRTANPIaYRVPMASAQVKS 178
Cdd:TIGR01356 78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGgSLPLTISGPLPGGIV-YISGSASSQYKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 179 AVLLAG--LNTPGVTTVIEPVMTRDHTEKMLQGFGADLtVETDKDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPLVAAL 256
Cdd:TIGR01356 157 ALLLAApaLQAVGITIVGEPLKSRPYIEITLDLLGSFG-VEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 257 LVeGSEVTIRNVLMNPTRTG--LILTLQEMGADIEIIDprlaggedvADLRVK-ASKLKGVVVppeRAPSMIDEYPVLAI 333
Cdd:TIGR01356 236 IT-GGRVTLENLGINPTQGDkaIIIVLEEMGADIEVEE---------DDLIVEgASGLKGIKI---DMDDMIDELPTLAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 334 AASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpGGKGLGGGTVATHLDHRIAMSFLVMGLA 413
Cdd:TIGR01356 303 LAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIR---GKKELKGAVVDTFGDHRIAMAFAVAGLV 379
|
410 420 430
....*....|....*....|....*....|
gi 514200059 414 SEKPVTVDDSTMIATSFPEFMGMMAGLGAK 443
Cdd:TIGR01356 380 AEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
17-449 |
1.56e-150 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 445.21 E-value: 1.56e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 17 ALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARI--RKEGDVwIINGVGNGCLLQPEAPL 94
Cdd:PRK14806 311 AVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIegPHNGRV-TIHGVGLHGLKAPPGPL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 95 DFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPIAYRVPMASA 174
Cdd:PRK14806 390 YMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEGRPPLSIRGGQRLKGIHYDLPMASA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 175 QVKSAVLLAGLNTPGVTTVIEPVMTRDHTEKMLQGFGADLTVETDKdgvrhIRIVGQGKLTGQTIDVPGDPSSTAFPLVA 254
Cdd:PRK14806 470 QVKSCLLLAGLYAEGETSVTEPAPTRDHTERMLRGFGYPVKVEGNT-----ISVEGGGKLTATDIEVPADISSAAFFLVA 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 255 ALLVEGSEVTIRNVLMNPTRTGLILTLQEMGADIEIIDPRLAGGEDVADLRVKASKLKGVVVPPERAPSMIDEYPVLAIA 334
Cdd:PRK14806 545 ASIAEGSELTLEHVGINPTRTGVIDILKLMGADITLENEREVGGEPVADIRVRGARLKGIDIPEDQVPLAIDEFPVLFVA 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 335 ASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrpgGKGLGGGTVATHLDHRIAMSFLVMGLAS 414
Cdd:PRK14806 625 AACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIE----GGIFGGGEVESHGDHRIAMSFSVASLRA 700
|
410 420 430
....*....|....*....|....*....|....*
gi 514200059 415 EKPVTVDDSTMIATSFPEFMGMMAGLGAKIAESGA 449
Cdd:PRK14806 701 SGPITIHDCANVATSFPNFLELANQVGIRIEVEQS 735
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
15-433 |
2.00e-104 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 316.55 E-value: 2.00e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 15 SQALTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGA---RIRKEGDVWIINGVGNGCLLQPE 91
Cdd:pfam00275 3 GSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeiiKLDDEKSVVIVEGLGGSFEAPED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 92 APLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPIAYRVPM 171
Cdd:pfam00275 83 LVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHIDGDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 172 ASAQVKSAVLLAGLNTPGVTTVIEPV--MTRDHTEKMLQGFGADLTVETDKDGvrhIRIVGQGKLTGQTIDVPGDPSSTA 249
Cdd:pfam00275 163 SSQFVTSLLMLAALLAEGTTTIENLAsePYIDDTENMLKKFGAKIEGSGTELS---ITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 250 FPLVAALLVEGsEVTIRNVLMNPTRTGLIL--TLQEMGADIEiidprlagGEDVADLRVKASKLKGVvvpPERAPSMIDE 327
Cdd:pfam00275 240 YFLVAAAITGG-TVTVENVGINSLQGDEALleILEKMGAEIT--------QEEDADIVVGPPGLRGK---AVDIRTAPDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 328 YPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRgrPGGKGLGGGTVATHLDHRIAMSF 407
Cdd:pfam00275 308 APTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIII--PAVKELKGAEVDSYGDHRIAMAL 385
|
410 420
....*....|....*....|....*.
gi 514200059 408 LVMGLASEKPVTVDDSTMIATSFPEF 433
Cdd:pfam00275 386 ALAGLVAEGETIIDDIECTDRSFPDF 411
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
18-440 |
1.21e-84 |
|
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: 265.62 E-value: 1.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 18 LTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIINGVGNGCLLQPEAPLDFG 97
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 98 NAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPIAYRVPMASAQVK 177
Cdd:cd01554 81 NSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 178 SAVLLAGLNTPGVTTVIEPVM--TRDHTEKMLQGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPLVAA 255
Cdd:cd01554 161 SALMFAALLAKGETVIIEAAKepTINHTENMLQTFGGHISV----QGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 256 lLVEGSEVTIRNVLMNPTRTGLILTLQEMGADIEIidprlagGEDVadLRVKASKLKGVVVPPERAPSMIDEYPVLAIAA 335
Cdd:cd01554 237 -AIAPGRLVLQNVGINETRTGIIDVLRAMGAKIEI-------GEDT--ISVESSDLKATEICGALIPRLIDELPIIALLA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 336 SFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRGRPGGKGLGggtVATHLDHRIAMSFLVMGLASE 415
Cdd:cd01554 307 LQAQGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGAR---VNTFGDHRIGMMTALAALVAD 383
|
410 420
....*....|....*....|....*
gi 514200059 416 KPVTVDDSTMIATSFPEFMGMMAGL 440
Cdd:cd01554 384 GEVELDRAEAINTSYPSFFDDLESL 408
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
19-433 |
1.01e-38 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 148.27 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 19 TGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIINGVGnGCLLQPEAPLDFGN 98
Cdd:PRK11860 16 GGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYRITGLG-GQFPVKQADLFLGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 99 AGTGAR-LTMGLV---GTYDMKtsfiGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGP---RTANPIAYRVPM 171
Cdd:PRK11860 95 AGTAMRpLTAALAllgGEYELS----GVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPaplRLDAPIRVRGDV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 172 aSAQVKSAVLLAGLNTPGVTTVIEPV---MTRDHTE---KMLQGFGadltVETDKDGVRHIRIVGQGKL-TGQTIDVPGD 244
Cdd:PRK11860 171 -SSQFLTALLMALPLVARRDITIEVVgelISKPYIEitlNLLARFG----IAVQREGWQRFTIPAGSRYrSPGEIHVEGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 245 PSSTAFPLVAALLVEGSEVTIRNVLMNPTRTGL--ILTLQEMGADIEiidprlaGGEDVADLRVKASKLKGVVVPPERAP 322
Cdd:PRK11860 246 ASSASYFIAAGAIAGGAPVRIEGVGRDSIQGDIrfAEAARAMGAQVT-------SGPNWLEVRRGAWPLKAIDLDCNHIP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 323 smiDEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRGRPGGKGLGGGTVATHLDHR 402
Cdd:PRK11860 319 ---DAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADWKAAAIHTYDDHR 395
|
410 420 430
....*....|....*....|....*....|..
gi 514200059 403 IAMSFLVMGLASEK-PVTVDDSTMIATSFPEF 433
Cdd:PRK11860 396 MAMCFSLAAFNPAGlPVRINDPKCVAKTFPDY 427
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
9-433 |
1.29e-29 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 122.12 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 9 PATARHSQALT--------GEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGDVWIIN 80
Cdd:PRK11861 234 SGTGSHMEHLDlgpfshaqGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 81 GVgNGCLLQPEAPLDFGNAGTGARLTMGLVGTYDMKTSFIGDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPR 160
Cdd:PRK11861 314 GT-RGAFTAKTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 161 TAN---PIAYRVPMAS----AQVKSAVLLAGLNTPGVTTVIEPVMTRDHTE---KMLQGFGadltVETDKDGVRHIRI-V 229
Cdd:PRK11861 393 TISvdaPIRVRGDVSSqfltALLMTLPLVKAKDGASVVEIDGELISKPYIEitiKLMARFG----VTVERDGWQRFTVpA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 230 GQGKLTGQTIDVPGDPSSTAFPLVAALLvEGSEVTIRNVLMNPTR--TGLILTLQEMGADIEIidprlagGEDVADLRVK 307
Cdd:PRK11861 469 GVRYRSPGTIMVEGDASSASYFLAAGAL-GGGPLRVEGVGRASIQgdVGFANALMQMGANVTM-------GDDWIEVRGI 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 308 ASKlKGVVVPPERAPSMI-DEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVrgRPG 386
Cdd:PRK11861 541 GHD-HGRLAPIDMDFNLIpDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVV--TPP 617
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 514200059 387 GKGLGGGTVATHLDHRIAMSFLVMGLASeKPVTVDDSTMIATSFPEF 433
Cdd:PRK11861 618 AQLTPNASIDTYDDHRMAMCFSLVSLGG-VPVRINDPKCVGKTFPDY 663
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
18-438 |
2.00e-24 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 104.83 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 18 LTGEIRIPGDKSISHRSFMFGGLASGKTRITGLLEGEDVINTGRAMQAMGARIR--KEGDVWIINGVGN----GCLLQPE 91
Cdd:PLN02338 12 ISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEedSENNRAVVEGCGGkfpvSGDSKED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 92 APLDFGNAGTGARLTMGLVGTYDMKTSFI--GDASLSKRPMGRVLNPLREMGVQVEAAEGDRMPLTLIGPRTANPiAYRV 169
Cdd:PLN02338 92 VELFLGNAGTAMRPLTAAVTAAGGNASYVldGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVNAAGGLP-GGKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 170 PMA---SAQVKSAVLLAglnTPGVTTVIEPVMTR--------DHTEKMLQGFGADLTVETDKDgvRHIRIVGQGKLTGQT 238
Cdd:PLN02338 171 KLSgsiSSQYLTALLMA---APLALGDVEIEIVDklisvpyvEMTLKLMERFGVSVEHSDSWD--RFFIKGGQKYKSPGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 239 IDVPGDPSSTAFPLVAAlLVEGSEVTIRNVLMNPTR--TGLILTLQEMGADIEIIDPRLAGGEDVADLRVKaSKLKGVVV 316
Cdd:PLN02338 246 AYVEGDASSASYFLAGA-AITGGTVTVEGCGTTSLQgdVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGG-KHLKAIDV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 317 PPERAPsmiDEYPVLAIAASFAEGETVMDGLDELRVKESDRLAAVARGLEANGVDCTEGEMSLTVRGRPGGKGLGggtVA 396
Cdd:PLN02338 324 NMNKMP---DVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAE---ID 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 514200059 397 THLDHRIAMSFlVMGLASEKPVTVDDSTMIATSFPEFMGMMA 438
Cdd:PLN02338 398 TYDDHRMAMAF-SLAACGDVPVTINDPGCTRKTFPTYFDVLE 438
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
18-316 |
5.75e-07 |
|
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: 51.53 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 18 LTGEIRIPGDK---------SIshrsfmfggLASGKTRITGLLEGEDVINTGRAMQAMGARI-RKEGDVWIINGVGngcL 87
Cdd:COG0766 12 LSGEVRISGAKnaalpilaaAL---------LTDGPVTLRNVPDLSDVRTMLELLESLGVKVeRDDGGTLTIDASN---I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 88 LQPEAPLDfgnagtgarltmgLVGTydMKTSFI---------GDASLSK--------RPMGRVLNPLREMGVQVEAAEG- 149
Cdd:COG0766 80 NSTEAPYE-------------LVRK--MRASILvlgpllarfGEARVSLpggcaigaRPIDLHLKGLEALGAEIEIEHGy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 150 -----DRmpltLIGPR----------TANPIayrvpMAsaqvksAVLLAGlntpgvTTVI-----EPvmtrdhtE----- 204
Cdd:COG0766 145 iearaGR----LKGARiyldfpsvgaTENIM-----MA------AVLAEG------TTVIenaarEP-------Eivdla 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 205 KMLQGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPLVAALlVEGSEVTIRNVlmNPTRTGLIL-TLQE 283
Cdd:COG0766 197 NFLNAMGAKIEG----AGTDTITIEGVEKLHGAEHTVIPDRIEAGTFLVAAA-ITGGDVTVKNV--IPEHLEAVLaKLRE 269
|
330 340 350
....*....|....*....|....*....|....
gi 514200059 284 MGADIEIidprlagGEDvaDLRVKAS-KLKGVVV 316
Cdd:COG0766 270 AGVEIEE-------GDD--GIRVRGPgRLKAVDI 294
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
18-316 |
8.81e-04 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 41.55 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 18 LTGEIRIPGDK---------SIshrsfmfggLASGKTRITGLLEGEDVINTGRAMQAMGARIRKEGD-VWIINGVGngcL 87
Cdd:PRK09369 12 LSGEVTISGAKnaalpilaaSL---------LAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASN---I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 88 LQPEAPLDfgnagtgarltmgLVGTydMKTSFI---------GDASLSK--------RPMGRVLNPLREMGVQVEAAEGD 150
Cdd:PRK09369 80 NNTEAPYE-------------LVKK--MRASILvlgpllarfGEAKVSLpggcaigaRPVDLHLKGLEALGAEIEIEHGY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 151 ---RMPLTLIGPR----------TANPIayrvpMAsaqvksAVLLAGlntpgvTTVI-----EPvmtrdhtE-----KML 207
Cdd:PRK09369 145 veaKADGRLKGAHivldfpsvgaTENIL-----MA------AVLAEG------TTVIenaarEP-------EivdlaNFL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 208 QGFGADLTVetdkDGVRHIRIVGQGKLTGQTIDVPGDPSSTAFPLVAALLVeGSEVTIRNVlmNPTRTGLIL-TLQEMGA 286
Cdd:PRK09369 201 NKMGAKISG----AGTDTITIEGVERLHGAEHTVIPDRIEAGTFLVAAAIT-GGDVTIRGA--RPEHLEAVLaKLREAGA 273
|
330 340 350
....*....|....*....|....*....|.
gi 514200059 287 DIEIidprlagGEDvaDLRVKAS-KLKGVVV 316
Cdd:PRK09369 274 EIEE-------GED--GIRVDMPgRLKAVDI 295
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
205-382 |
1.40e-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: 40.92 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 205 KMLQGFGADLTVETDkdgvrHIRIVGQGKLTGQTIDVPgDPSSTAFP--LVAALLVEGsEVTIRNVLMNPTRTGLILTLQ 282
Cdd:cd01555 118 KGLEALGAKIEIEDG-----YVEAKAAGRLKGARIYLD-FPSVGATEniMMAAVLAEG-TTVIENAAREPEIVDLANFLN 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514200059 283 EMGADIEIIdprlagGEDVadLRVK-ASKLKGVvvpperapsmidEYPVLA--I-AASFAEGETVMDGldELRVK--ESD 356
Cdd:cd01555 191 KMGAKIEGA------GTDT--IRIEgVERLHGA------------EHTVIPdrIeAGTFLVAAAITGG--DITVEnvIPE 248
|
170 180
....*....|....*....|....*.
gi 514200059 357 RLAAVARGLEANGVDCTEGEMSLTVR 382
Cdd:cd01555 249 HLEAVLAKLREMGAKIEIGEDGIRVD 274
|
|
| |
