|
Name |
Accession |
Description |
Interval |
E-value |
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
1-416 |
0e+00 |
|
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: 682.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFV-NDEVTVDATGE 79
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTD-GPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 80 ITSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAEKLVGAKVYL 159
Cdd:COG0766 80 NSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 160 DFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTF 239
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 240 MIAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSEG 319
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 320 TSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVaatdlraaaalilagLVAD--------------- 384
Cdd:COG0766 320 TSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPV---------------MATDlragaalvlaglaae 384
|
410 420 430
....*....|....*....|....*....|..
gi 489825469 385 GYTQVTELKYLDRGYNNFHGKLQALGADVERV 416
Cdd:COG0766 385 GETVIDNIYHIDRGYENLEEKLRALGADIERV 416
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
1-416 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 678.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFV-NDEVTVDATGE 79
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAE-EPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 80 ITSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE-KLVGAKVY 158
Cdd:PRK09369 80 NNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAHIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 159 LDFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGT 238
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 239 FMIAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSE 318
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 319 GTSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVaatdlraaaalilagLVAD-------------- 384
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPV---------------MATDlrasaslvlaglva 384
|
410 420 430
....*....|....*....|....*....|...
gi 489825469 385 -GYTQVTELKYLDRGYNNFHGKLQALGADVERV 416
Cdd:PRK09369 385 eGTTIVDRIYHLDRGYERIEEKLRALGADIERV 417
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
12-409 |
0e+00 |
|
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: 594.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 12 LNGSVKMEGAKNAVLPVIAATLLAsKGTSVLKNVPNLSDVFTINEVLKYLNADVSFVN-DEVTVDATGEITSDAPFEYVR 90
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 91 KMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEAT-AEKLVGAKVYLDFPSVGATQN 169
Cdd:cd01555 80 KMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKaAGRLKGARIYLDFPSVGATEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 170 IMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTFMIAAAITGGN 249
Cdd:cd01555 160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 250 VLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDK-LKAVDVKTMPHPGFPTDMQSQMMVIQMLSEGTSIMTETVF 328
Cdd:cd01555 240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 329 ENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVAATDLRAAAALILAGLVADGYTQVTELKYLDRGYNNFHGKLQA 408
Cdd:cd01555 320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399
|
.
gi 489825469 409 L 409
Cdd:cd01555 400 L 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
1-415 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 162190 [Multi-domain] Cd Length: 416 Bit Score: 588.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDEVTVDATGEI 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTD-EPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 81 TSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE-KLVGAKVYL 159
Cdd:TIGR01072 80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKgRLVGAHIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 160 DFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTF 239
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 240 MIAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIG-PDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSE 318
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMrQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 319 GTSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVAATDLRAAAALILAGLVADGYTQVTELKYLDRG 398
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
|
410
....*....|....*..
gi 489825469 399 YNNFHGKLQALGADVER 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
3.25e-115 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 343.51 E-value: 3.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 7 RGGKQLNGSVKMEG-AKNAVLPVIAATLLAskGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDE--VTVDATGEITSD 83
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAA--GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEksVVIVEGLGGSFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 84 APFEYVRKMRASIVVMGPLLARTG--SARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE----KLVGAKV 157
Cdd:pfam00275 79 APEDLVLDMGNSGTALRPLTGRLAlqSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrglRLGGIHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 158 YLDFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTE-VIRIEGVKELTATEHSIIPDRIEA 236
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 237 GTFMIAAAITGGNVLIEDAVPEHI---SSLIAKLEEMGVQIIEEENGIRVIGPDKL--KAVDVKTMPHPGFPTDMQSQMM 311
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 312 VIQMLSEGTSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAK-LQGAEVAATD-LRAAAALILAGLVADGYTQV 389
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGdHRIAMALALAGLVAEGETII 398
|
410
....*....|....*..
gi 489825469 390 TELKYLDRGYNNFHGKL 406
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
1-416 |
0e+00 |
|
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: 682.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFV-NDEVTVDATGE 79
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTD-GPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 80 ITSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAEKLVGAKVYL 159
Cdd:COG0766 80 NSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 160 DFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTF 239
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 240 MIAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSEG 319
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 320 TSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVaatdlraaaalilagLVAD--------------- 384
Cdd:COG0766 320 TSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPV---------------MATDlragaalvlaglaae 384
|
410 420 430
....*....|....*....|....*....|..
gi 489825469 385 GYTQVTELKYLDRGYNNFHGKLQALGADVERV 416
Cdd:COG0766 385 GETVIDNIYHIDRGYENLEEKLRALGADIERV 416
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
1-416 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 678.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFV-NDEVTVDATGE 79
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAE-EPVTLTNVPDLSDVRTMIELLRSLGAKVEFDgNGTVTIDASNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 80 ITSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE-KLVGAKVY 158
Cdd:PRK09369 80 NNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAHIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 159 LDFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGT 238
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 239 FMIAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSE 318
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 319 GTSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVaatdlraaaalilagLVAD-------------- 384
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPV---------------MATDlrasaslvlaglva 384
|
410 420 430
....*....|....*....|....*....|...
gi 489825469 385 -GYTQVTELKYLDRGYNNFHGKLQALGADVERV 416
Cdd:PRK09369 385 eGTTIVDRIYHLDRGYERIEEKLRALGADIERV 417
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
12-409 |
0e+00 |
|
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: 594.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 12 LNGSVKMEGAKNAVLPVIAATLLAsKGTSVLKNVPNLSDVFTINEVLKYLNADVSFVN-DEVTVDATGEITSDAPFEYVR 90
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGeNTLVIDASNINSTEAPYELVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 91 KMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEAT-AEKLVGAKVYLDFPSVGATQN 169
Cdd:cd01555 80 KMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKaAGRLKGARIYLDFPSVGATEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 170 IMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTFMIAAAITGGN 249
Cdd:cd01555 160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 250 VLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDK-LKAVDVKTMPHPGFPTDMQSQMMVIQMLSEGTSIMTETVF 328
Cdd:cd01555 240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 329 ENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVAATDLRAAAALILAGLVADGYTQVTELKYLDRGYNNFHGKLQA 408
Cdd:cd01555 320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399
|
.
gi 489825469 409 L 409
Cdd:cd01555 400 L 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
1-415 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 162190 [Multi-domain] Cd Length: 416 Bit Score: 588.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDEVTVDATGEI 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTD-EPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 81 TSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE-KLVGAKVYL 159
Cdd:TIGR01072 80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKgRLVGAHIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 160 DFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTF 239
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 240 MIAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIG-PDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSE 318
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMrQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 319 GTSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVAATDLRAAAALILAGLVADGYTQVTELKYLDRG 398
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
|
410
....*....|....*..
gi 489825469 399 YNNFHGKLQALGADVER 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIER 416
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-418 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 526.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKNAVLPVIAATLLAsKGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDEVTVDATGEI 80
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILA-DGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 81 TSDAPFEYVRKMRASIVVMGPLLARTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAEKLVGAKVYLD 160
Cdd:PRK12830 80 SMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHIYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 161 FPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTFM 240
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 241 IAAAITGGNVLIEDAVPEHISSLIAKLEEMGVQIIEEENGIRVIGPDKLKAVDVKTMPHPGFPTDMQSQMMVIQMLSEGT 320
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 321 SIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVAATDLRAAAALILAGLVADGYTQVTELKYLDRGYN 400
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYS 399
|
410
....*....|....*...
gi 489825469 401 NFHGKLQALGADVERVDD 418
Cdd:PRK12830 400 NIIEKLKALGADIWREED 417
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
3.25e-115 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 343.51 E-value: 3.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 7 RGGKQLNGSVKMEG-AKNAVLPVIAATLLAskGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDE--VTVDATGEITSD 83
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAA--GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEksVVIVEGLGGSFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 84 APFEYVRKMRASIVVMGPLLARTG--SARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE----KLVGAKV 157
Cdd:pfam00275 79 APEDLVLDMGNSGTALRPLTGRLAlqSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrglRLGGIHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 158 YLDFPSVGATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTE-VIRIEGVKELTATEHSIIPDRIEA 236
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 237 GTFMIAAAITGGNVLIEDAVPEHI---SSLIAKLEEMGVQIIEEENGIRVIGPDKL--KAVDVKTMPHPGFPTDMQSQMM 311
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 312 VIQMLSEGTSIMTETVFENRFMHVEEMRRMNADMKIEGHSVIISGPAK-LQGAEVAATD-LRAAAALILAGLVADGYTQV 389
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGdHRIAMALALAGLVAEGETII 398
|
410
....*....|....*..
gi 489825469 390 TELKYLDRGYNNFHGKL 406
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-409 |
3.34e-78 |
|
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: 248.29 E-value: 3.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 12 LNGSVKMEGAKNAVLPVIAATLLAsKGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDEVTVDATGEITSDAP---FEY 88
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLA-EGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPqnaLNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 89 VRKMRASIVVMGPLLARTGsaRVALPGGCAIGSRPVDLHLKGFEAMGAVVKIENGYIEATAE---KLVGAKVYLD-FPSV 164
Cdd:cd01554 80 GNSGTAIRLISGVLAGADF--EVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLkggKNLGPIHYEDpIASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 165 GATQNIMMAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTFMIAAA 244
Cdd:cd01554 158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 245 ITGGNVLIEDAVP-EHISSLIAKLEEMGVQIIEEENGIRVIGPDkLKAVDVKTMPHPgFPTDMQSQMMVIQMLSEGTSIM 323
Cdd:cd01554 238 IAPGRLVLQNVGInETRTGIIDVLRAMGAKIEIGEDTISVESSD-LKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 324 TETVF------ENRFMHVEEMRRMNADMKIEGHSVIISGPAKLQGAEVAATD-LRAAAALILAGLVADGYTQVTELKYLD 396
Cdd:cd01554 316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGdHRIGMMTALAALVADGEVELDRAEAIN 395
|
410
....*....|...
gi 489825469 397 RGYNNFHGKLQAL 409
Cdd:cd01554 396 TSYPSFFDDLESL 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-365 |
1.34e-20 |
|
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: 93.23 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAK---NAVLpvIAATLlaSKGTSVLKNVPNLSDVFTINEVLKYLNADVSFVND-EVTVDA 76
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEGESTIRNLLESDDTLATLEALRALGAEIEELDGgTLRVTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 77 TGeitsdapfeyvRKMRASIVV------------MGPLLArTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVK-IENG 143
Cdd:COG0128 77 VG-----------GGLKEPDAVldcgnsgttmrlLTGLLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIEsRGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 144 Y--IEATAEKLVGAKVYLdfPSVGATQ---NIMMAATLAEGTTVIEnVAREPE---IVDLA-NFLNQMGARVIGAGTEVI 214
Cdd:COG0128 145 YlpLTIRGGPLKGGEYEI--PGSASSQfksALLLAGPLAEGGLEIT-VTGELEskpYRDHTeRMLRAFGVEVEVEGYRRF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 215 RIEGVKELTATEHSIIPDRIEAGTFMIAAAITGGNVLIEDAVPEHI---SSLIAKLEEMGVQIIEEENGIRVIGpDKLKA 291
Cdd:COG0128 222 TVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITVRG-SPLKG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 292 VDVktmphPG------FPTdmqsqMMVIQMLSEGTSIMT--------ETvfeNRF--MhVEEMRRMNADMKIEGHSVIIS 355
Cdd:COG0128 301 IDI-----DLsdipdeAPT-----LAVLAAFAEGTTRIRgaaelrvkES---DRIaaM-ATELRKLGADVEETEDGLIIE 366
|
410
....*....|
gi 489825469 356 GPAKLQGAEV 365
Cdd:COG0128 367 GGPKLKGAEV 376
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
28-365 |
1.36e-16 |
|
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: 81.06 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 28 VIAATLlaSKGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDEVTVdaTGEITSDAPFEYVRKMRASIVVMGPL--LAR 105
Cdd:cd01556 18 LLLAAL--AEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEI--VGGGGLGLPPEAVLDCGNSGTTMRLLtgLLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 106 TGSARVALPGGCAIGSRPVDLHLKGFEAMGAVV--KIENGYIEATA-EKLVGAKVYLDFPS----VGAtqnIMMAATLAE 178
Cdd:cd01556 94 LQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIegREGGGYPPLIGgGGLKGGEVEIPGAVssqfKSA---LLLAAPLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 179 GTTVIENVAREPEI-VDL-ANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTFMIAAAITGGNVLIEDaV 256
Cdd:cd01556 171 GPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSAAFFLAAAAITGSEIVIKN-V 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 257 PEH--ISSLIAKLEEMGVQI-IEEENGIRVIGPDKLKAVDVKTMPHPG-FPTdmqsqMMVIQMLSEGTSIMT-------- 324
Cdd:cd01556 250 GLNsgDTGIIDVLKEMGADIeIGNEDTVVVESGGKLKGIDIDGNDIPDeAPT-----LAVLAAFAEGPTRIRnaaelrvk 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489825469 325 ETvfeNRF--MhVEEMRRMNADMKIEGHSVIISG-PAKLQGAEV 365
Cdd:cd01556 325 ES---DRIaaM-ATELRKLGADVEETEDGLIIEGgPLKGAGVEV 364
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
231-365 |
7.47e-16 |
|
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: 76.16 E-value: 7.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 231 PDRIEAGTFMIAAAITGGNVLIEDAVPE---------HISSLiAKLEEM-GVQIIEEENGIRVIG--PDKLKAVDVKTMP 298
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTGIRPDrakpgllrqHLTFL-KALEKIcGATVEGGELGSDRISfrPGTVRGGDVRFAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 299 HP-GFPTDMQSQMMVIQMLSEGTSIMTETVF----------ENRFMHVEEMRRMNADMKIE------------GHSVIIS 355
Cdd:cd01553 87 GSaGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETllrhgfypagggVVATEVS 166
|
170
....*....|
gi 489825469 356 GPAKLQGAEV 365
Cdd:cd01553 167 PVEKLNTAQL 176
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-365 |
3.48e-12 |
|
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: 67.69 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 14 GSVKMEGAKNAVLPVIAATLLASkGTSVLKNVPNLSDVFTINEVLKYLNADVSFVNDEVTVDATGEITSDAPFeyvrKMR 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAE-GETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGKEPQAEL----DLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 94 ASIVVMGPLLARTGSAR--VALPGGCAIGSRPVDLHLKGFEAMGAVV--KIENGYIEATAE-KLVGAKVYLDfPSVGAtQ 168
Cdd:TIGR01356 76 NSGTTARLLTGVLALADgeVVLTGDESLRKRPMGRLVDALRQLGAEIssLEGGGSLPLTISgPLPGGIVYIS-GSASS-Q 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 169 ---NIMMAATLAEG---TTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIRIEGVKELTATEHSIIPDRIEAGTFMIA 242
Cdd:TIGR01356 154 yksALLLAAPALQAvgiTIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 243 AAITGGNVLIEDaVPEHI----SSLIAKLEEMGVQIIEEENGIRVIGPDKLKAV--DVKTMPHPgFPTdmqsqMMVIQML 316
Cdd:TIGR01356 234 AAITGGRVTLEN-LGINPtqgdKAIIIVLEEMGADIEVEEDDLIVEGASGLKGIkiDMDDMIDE-LPT-----LAVLAAF 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489825469 317 SEGTSIMT--------ETvfeNRFMHV-EEMRRMNADMKIEGHSVIISGPAKLQGAEV 365
Cdd:TIGR01356 307 AEGVTRITgaeelrvkES---DRIAAIaEELRKLGVDVEEFEDGLYIRGKKELKGAVV 361
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
132-261 |
1.57e-11 |
|
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: 65.49 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 132 EAMGAVVKIENGYIEATAEKLVGAKVYLD-----FPSvgatqnIMMAATLAEGTTVIENVA--REPE---IVDLANFLNQ 201
Cdd:COG0128 278 KEMGADIEIENDGITVRGSPLKGIDIDLSdipdeAPT------LAVLAAFAEGTTRIRGAAelRVKEsdrIAAMATELRK 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489825469 202 MGARVIgAGTEVIRIEGVKELTATE------HsiipdRIeAGTFMIAAAITGGNVLIEDavPEHIS 261
Cdd:COG0128 352 LGADVE-ETEDGLIIEGGPKLKGAEvdsygdH-----RI-AMAFAVAGLRAEGPVTIDD--AECVA 408
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
119-296 |
7.99e-11 |
|
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: 63.35 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 119 IGSRP-VDLHLKGFEAMGAVVKIE--NGYIEATAEKLVGAKVYL--DFPSVGAtqnIMMAATLAEGTTVIENVAREPEIV 193
Cdd:cd01556 180 LESKPyIDHTERMLRAFGAEVEVDgyRTITVKGGQKYKGPEYTVegDASSAAF---FLAAAAITGSEIVIKNVGLNSGDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 194 DLANFLNQMGARVIGAGTEVIRIEGVKELTATE--HSIIPDriEAGTFMIAAAITGGNVLIEDAvpEH--------ISSL 263
Cdd:cd01556 257 GIIDVLKEMGADIEIGNEDTVVVESGGKLKGIDidGNDIPD--EAPTLAVLAAFAEGPTRIRNA--AElrvkesdrIAAM 332
|
170 180 190
....*....|....*....|....*....|....
gi 489825469 264 IAKLEEMGVQIIEEENGIRVIG-PDKLKAVDVKT 296
Cdd:cd01556 333 ATELRKLGADVEETEDGLIIEGgPLKGAGVEVYT 366
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-365 |
1.25e-07 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 53.60 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAK---NAVLpviaatLLA--SKGTSVLKNVPNLSDVFTINEVLKYLNADVSfvndEVTVD 75
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKslsNRIL------LLAalSEGTTVVDNLLDSDDIRYMLGALKTLGLNVE----EDSEN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 76 ATGEITSDA---PFEYVRKMRASIVV------MGPLLART----GSARVALPGGCAIGSRPVDLHLKGFEAMGAVVKIEN 142
Cdd:PLN02338 71 NRAVVEGCGgkfPVSGDSKEDVELFLgnagtaMRPLTAAVtaagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 143 G------YIEAtAEKLVGAKVYLDfPSVGAT--QNIMMAATLAEGTTVIENVAREPEI--VDLA-NFLNQMGARV-IGAG 210
Cdd:PLN02338 151 GtncppvRVNA-AGGLPGGKVKLS-GSISSQylTALLMAAPLALGDVEIEIVDKLISVpyVEMTlKLMERFGVSVeHSDS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 211 TEVIRIEGVKELTATEHSIIP-DRIEAGTFMIAAAITGGNVLIEDAVPEHISSLIA---KLEEMGVQIIEEENGIRVIGP 286
Cdd:PLN02338 229 WDRFFIKGGQKYKSPGNAYVEgDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKfaeVLEKMGAKVEWTENSVTVTGP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 287 D-------KLKAVDV--KTMPhpgfptDMQSQMMVIQMLSEG-TSImtETVFENRFMHVEEMRRMNADMKIEGHSV---- 352
Cdd:PLN02338 309 PrdafggkHLKAIDVnmNKMP------DVAMTLAVVALFADGpTAI--RDVASWRVKETERMIAICTELRKLGATVeegp 380
|
410
....*....|....*.
gi 489825469 353 ---IISGPAKLQGAEV 365
Cdd:PLN02338 381 dycIITPPKKLKPAEI 396
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-324 |
2.12e-07 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 52.84 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 1 MEKIIVRGGKQLNGSVKMEGAKN----AVLpvIAAtlLAsKGTSVLKNVPNLSDVF-TINeVLKYLNADVSfvNDEVTVD 75
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSishrALL--LAA--LA-EGETTITNLLRSEDTLaTLN-ALRALGVEIE--DDEVVVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 76 ATGEITSDAPfeyvrkmrASIVVMG----------PLLArTGSARVALPGGCAIGSRPVDLHLKGFEAMGAVVK-IENGY 144
Cdd:PRK02427 74 GVGGGGLKEP--------EDVLDCGnsgttmrlltGLLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEgRDEGY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 145 ----IEATAeKLVGAKVYLDFPSVGATQNIMMAATLAEG---TTVIENVAREPEIVDLANFLNQMGARVI---GAGTEVI 214
Cdd:PRK02427 145 lpltIRGGK-KGGPIEYDGPVSSQFVKSLLLLAPLFAEGdteTTVIEPLPSRPHTEITLRMLRAFGVEVEnveGWGYRRI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 215 RIEGVKELTATEHSIIPDRIEAGTFMIAAAITGG------NVLIEDAVPEHisSLIAKLEEMGVQI--------IEEENG 280
Cdd:PRK02427 224 VIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsevtitNVGLNSTQGGK--AIIDVLEKMGADIeieneregGEPVGD 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489825469 281 IRVIGPdKLKAVDVkTMPHPG--FPTdmqsqMMVIQMLSEGTSIMT 324
Cdd:PRK02427 302 IRVRSS-ELKGIDI-DIPDIIdeAPT-----LAVLAAFAEGTTVIR 340
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
121-293 |
1.08e-06 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 50.53 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 121 SRP-VDLHLKGFEAMGAVVKIENG-----YIEATAEKLVGAKVYL--DFPSVGAtqnIMMAATLAEGTTV-IENVAREP- 190
Cdd:PRK02427 194 SRPhTEITLRMLRAFGVEVENVEGwgyrrIVIKGGQRLRGQDITVpgDPSSAAF---FLAAAAITGGSEVtITNVGLNSt 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 191 ----EIVDLanfLNQMGA-------RVIGAGTEVIRIEGvKELTATEHSI--IPDriEAGTFMIAAAITGGNVLIEDAvp 257
Cdd:PRK02427 271 qggkAIIDV---LEKMGAdieieneREGGEPVGDIRVRS-SELKGIDIDIpdIID--EAPTLAVLAAFAEGTTVIRNA-- 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489825469 258 EH--------ISSLIAKLEEMGVQIIEEENGIRVIGPDKLKAVD 293
Cdd:PRK02427 343 EElrvketdrIAAMATELRKLGAEVEETEDGLIITGGPLAGVVD 386
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
172-365 |
6.79e-06 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 48.22 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 172 MAATLAEGTTVIENVAREPEIVDLANFLNQMGARvIGAGTEVIRIEGVKELTATEHSIipDRIEAGT---FMIAAAITGG 248
Cdd:PRK02427 31 LLAALAEGETTITNLLRSEDTLATLNALRALGVE-IEDDEVVVEGVGGGGLKEPEDVL--DCGNSGTtmrLLTGLLALQP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 249 N--VLIEDavpEHISS-----LIAKLEEMGVQIIEEENG---IRVIGPDKLKAVDVKtmphpgfpTDMQSQ-----MMVI 313
Cdd:PRK02427 108 GevVLTGD---ESLRKrpmgrLLDPLRQMGAKIEGRDEGylpLTIRGGKKGGPIEYD--------GPVSSQfvkslLLLA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489825469 314 QMLSEGTsimTETVFENRFM---HVEE----MRRMNADMKIEG----HSVIISGPAKLQGAEV 365
Cdd:PRK02427 177 PLFAEGD---TETTVIEPLPsrpHTEItlrmLRAFGVEVENVEgwgyRRIVIKGGQRLRGQDI 236
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
131-261 |
5.94e-05 |
|
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: 44.86 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 131 FEAMGAVVKIEN-GYIEATA-EKLVGAKVYLD-FPSvgATQNIMMAATLAEGTTVIENVA--REPE---IVDLANFLNQM 202
Cdd:cd01556 262 LKEMGADIEIGNeDTVVVESgGKLKGIDIDGNdIPD--EAPTLAVLAAFAEGPTRIRNAAelRVKEsdrIAAMATELRKL 339
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489825469 203 GARVigagTEV---IRIEGVK-ELTATEHSIIPD-RIeAGTFMIAAAITGGNVLIEDavPEHIS 261
Cdd:cd01556 340 GADV----EETedgLIIEGGPlKGAGVEVYTYGDhRI-AMSFAIAGLVAEGGVTIED--PECVA 396
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
172-429 |
5.10e-04 |
|
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: 42.16 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 172 MAATLAEGTTVIENVAREPEIVDLANFLNQMGARVIGAGTEVIrIEGVKELTATEHSIIpDRIEAGTFM-----IAAAIT 246
Cdd:cd01556 19 LLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVE-IVGGGGLGLPPEAVL-DCGNSGTTMrlltgLLALQG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 247 GGNVLIEDAV----PehISSLIAKLEEMGVQI--IEEENGIRVIGPDKLKAVDVKtmphpgFPTDMQSQ----MMVIQML 316
Cdd:cd01556 97 GDSVLTGDESlrkrP--MGRLVDALRQLGAEIegREGGGYPPLIGGGGLKGGEVE------IPGAVSSQfksaLLLAAPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489825469 317 SEGTSIMTETVFEN---RFMHVEEMRRMNADMKIEGHSVI-ISGPAKLQGAEVA-------------ATDLRAAAALILA 379
Cdd:cd01556 169 AEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDGYRTItVKGGQKYKGPEYTvegdassaafflaAAAITGSEIVIKN 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489825469 380 GLVADGYTQVTELkyldrgynnfhgkLQALGADVERVDDSKIDVTNLASL 429
Cdd:cd01556 249 VGLNSGDTGIIDV-------------LKEMGADIEIGNEDTVVVESGGKL 285
|
|
| |
