|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 752.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKvEFDGNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLAdgaKRLRGAR 159
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD---GRLKGAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 240 GTFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:PRK09369 318 AEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLD 397
|
410 420
....*....|....*....|
gi 746327587 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK09369 398 RGYERIEEKLRALGADIERV 417
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
1-419 |
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: 731.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladgAKRLRGAR 159
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEAR----AGRLKGAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEA 239
Cdd:COG0766 157 IYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 240 GTFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:COG0766 237 GTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:COG0766 317 AEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHID 396
|
410 420
....*....|....*....|
gi 746327587 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:COG0766 397 RGYENLEEKLRALGADIERV 416
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
12-412 |
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: 655.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 12 LSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHN-LTLDAATIHTPEASYDLVKT 90
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENtLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 91 MRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARIVTDMVTVTGT 170
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAK---AAGRLKGARIYLDFPSVGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 171 ENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEAGTFLCAVAAAG 250
Cdd:cd01555 158 ENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 251 GDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAIAEGSATVTET 329
Cdd:cd01555 238 GDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 330 IFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLDRGYDRIEDKL 409
Cdd:cd01555 318 IFENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKL 397
|
...
gi 746327587 410 SAV 412
Cdd:cd01555 398 RAL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
1-418 |
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: 615.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHT 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 81 PEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARI 160
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYAS---AKGRLVGAHI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 161 VTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 241 TFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
|
410
....*....|....*....
gi 746327587 400 RGYDRIEDKLSAVGAKIRR 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-409 |
1.91e-127 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 374.33 E-value: 1.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 7 EGNGPLSGEIRVSG-AKNAALPIMCAALLTAEPLaLSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLT--LDAATIHTPEA 83
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGEST-ITNLLDSDDTLTMLEALRALGAEIIKLDDEKSvvIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 84 SYDLVKTMRASILVLGPLLARFGHAR--VSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIV 161
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 162 TDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTD-RLVIQSVEALHGAAHTVIADRIEAG 240
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 241 TFLCAVAAAGGDVTLRAVPPGIL---DAVLDKLREAGVTLTTGDD-WIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMM 315
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 316 LNAIAEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQ-LSGATVMAT-DLRASASLVIAGLIAQGETLVD 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 746327587 394 RIYHLDRGYDRIEDKL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 752.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKvEFDGNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLAdgaKRLRGAR 159
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD---GRLKGAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEA 239
Cdd:PRK09369 158 IVLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 240 GTFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:PRK09369 238 GTFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:PRK09369 318 AEGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLD 397
|
410 420
....*....|....*....|
gi 746327587 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK09369 398 RGYERIEEKLRALGADIERV 417
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
1-419 |
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: 731.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLDAATIH 79
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 80 TPEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladgAKRLRGAR 159
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEAR----AGRLKGAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 160 IVTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEA 239
Cdd:COG0766 157 IYLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 240 GTFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:COG0766 237 GTFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:COG0766 317 AEGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHID 396
|
410 420
....*....|....*....|
gi 746327587 400 RGYDRIEDKLSAVGAKIRRI 419
Cdd:COG0766 397 RGYENLEEKLRALGADIERV 416
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
12-412 |
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: 655.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 12 LSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHN-LTLDAATIHTPEASYDLVKT 90
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENtLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 91 MRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARIVTDMVTVTGT 170
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAK---AAGRLKGARIYLDFPSVGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 171 ENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEAGTFLCAVAAAG 250
Cdd:cd01555 158 ENIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 251 GDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAIAEGSATVTET 329
Cdd:cd01555 238 GDITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 330 IFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLDRGYDRIEDKL 409
Cdd:cd01555 318 IFENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKL 397
|
...
gi 746327587 410 SAV 412
Cdd:cd01555 398 RAL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
1-418 |
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: 615.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHT 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 81 PEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladGAKRLRGARI 160
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYAS---AKGRLVGAHI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 161 VTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 241 TFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMMLNAI 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
|
410
....*....|....*....
gi 746327587 400 RGYDRIEDKLSAVGAKIRR 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-420 |
1.23e-173 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 491.68 E-value: 1.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHT 80
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 81 PEASYDLVKTMRASILVLGPLLARFGHARVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKladgAKRLRGARI 160
Cdd:PRK12830 81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLK----ADELKGAHI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 161 VTDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEAG 240
Cdd:PRK12830 157 YLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 241 TFLCAVAAAGGDVTLRAVPPGILDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTSEYPAFPTDMQAQFMMLNAIA 320
Cdd:PRK12830 237 TYMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 321 EGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMATDLRASASLVIAGLIAQGETLVDRIYHLDR 400
Cdd:PRK12830 317 NGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDR 396
|
410 420
....*....|....*....|
gi 746327587 401 GYDRIEDKLSAVGAKIRRIQ 420
Cdd:PRK12830 397 GYSNIIEKLKALGADIWREE 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-409 |
1.91e-127 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 374.33 E-value: 1.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 7 EGNGPLSGEIRVSG-AKNAALPIMCAALLTAEPLaLSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLT--LDAATIHTPEA 83
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGEST-ITNLLDSDDTLTMLEALRALGAEIIKLDDEKSvvIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 84 SYDLVKTMRASILVLGPLLARFGHAR--VSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIV 161
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 162 TDMVTVTGTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTD-RLVIQSVEALHGAAHTVIADRIEAG 240
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 241 TFLCAVAAAGGDVTLRAVPPGIL---DAVLDKLREAGVTLTTGDD-WIRVQMTG-RPKAVSFRTSEYPAFPTDMQAQFMM 315
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 316 LNAIAEGSATVTETIFENRFMHVQELNRLGANIVIEGKTAVVTGVEQ-LSGATVMAT-DLRASASLVIAGLIAQGETLVD 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 746327587 394 RIYHLDRGYDRIEDKL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-412 |
1.71e-111 |
|
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: 333.42 E-value: 1.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 12 LSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDA---ATIHTPEASYDLV 88
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGvgmAGLKAPQNALNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 89 KTMRASILVLGPLLARFGhaRVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIVTDMVTVT 168
Cdd:cd01554 81 NSGTAIRLISGVLAGADF--EVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 169 GTENLLMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGTDRLVIQSVEALHGAAHTVIADRIEAGTFLCAVAA 248
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 249 AGGDVTLRAVPPG-ILDAVLDKLREAGVTLTTGDDWIRVQMtGRPKAVSFRTSEYPaFPTDMQAQFMMLNAIAEGSATVT 327
Cdd:cd01554 239 APGRLVLQNVGINeTRTGIIDVLRAMGAKIEIGEDTISVES-SDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 328 ETIF------ENRFMHVQELNRLGANIVIEGKTAVVTGVEQLSGATVMAT-DLRASASLVIAGLIAQGETLVDRIYHLDR 400
Cdd:cd01554 317 DAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAINT 396
|
410
....*....|..
gi 746327587 401 GYDRIEDKLSAV 412
Cdd:cd01554 397 SYPSFFDDLESL 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-393 |
1.16e-30 |
|
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: 122.12 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAK---NAALpiMCAALltAE-PLALSNVPNLQDVRTMLKLLRQMGVE-GVLDGHNLTLD- 74
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEgESTIRNLLESDDTLATLEALRALGAEiEELDGGTLRVTg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 75 -AATIHTPEASYDlVK----TMR--ASILVLGPLLARF-GHARvslpggcgIGARPVDQHIKGLQLMGAEIV-IEHGYie 145
Cdd:COG0128 77 vGGGLKEPDAVLD-CGnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQLGARIEsRGGGY-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 146 AKLADGAKRLRGARIVTDMVT----VTGtenLLMAAALADGETVLE-NAAREPEVT-DLA-NLLVKMGARIEGIGTDRLV 218
Cdd:COG0128 146 LPLTIRGGPLKGGEYEIPGSAssqfKSA---LLLAGPLAEGGLEITvTGELESKPYrDHTeRMLRAFGVEVEVEGYRRFT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 219 IQSVEALHGAAHTVIADRIEAGTFLCAVAAAGGDVTLRAVPPGIL---DAVLDKLREAGVTLTTGDDWIRVQmTGRPKAV 295
Cdd:COG0128 223 VPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITVR-GSPLKGI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 296 SFRTSEYP-AFPTdmqaqFMMLNAIAEGsatvtETIFEN----RF--------MhVQELNRLGANIVIEGKTAVVTGVEQ 362
Cdd:COG0128 302 DIDLSDIPdEAPT-----LAVLAAFAEG-----TTRIRGaaelRVkesdriaaM-ATELRKLGADVEETEDGLIIEGGPK 370
|
410 420 430
....*....|....*....|....*....|....*...
gi 746327587 363 LSGATV-------MATdlrasaSLVIAGLIAQGETLVD 393
Cdd:COG0128 371 LKGAEVdsygdhrIAM------AFAVAGLRAEGPVTID 402
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
235-412 |
7.83e-21 |
|
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: 90.03 E-value: 7.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 235 DRIEAGTFLCAVAAAGGDVTLRAVPPG--------ILDAVLDKLREA-GVTL---TTGDDWIRVQMtGRPKAVSFRTSEY 302
Cdd:cd01553 9 GGQILRSFLVLAAISGGPITVTGIRPDrakpgllrQHLTFLKALEKIcGATVeggELGSDRISFRP-GTVRGGDVRFAIG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 303 PA-FPTDMQAQFMMLNAIAEGSATVTETIF----------ENRFMHVQELNRLGANIVIE------------GKTAVVTG 359
Cdd:cd01553 88 SAgSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETllrhgfypagggVVATEVSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 746327587 360 VEQLSGAtvmatDLRASASLVIAGliaqGETLVDRIYHLDRGYDRIEDKLSAV 412
Cdd:cd01553 168 VEKLNTA-----QLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-397 |
4.61e-18 |
|
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: 85.30 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 12 LSGEIRVSGAK---NAALpiMCAALLTAEplalSNVPNL---QDVRTMLKLLRQMGVEgvLDGHNLTLdaaTIHTPEASY 85
Cdd:cd01556 1 LSGEITVPGSKsisHRAL--LLAALAEGE----SRIENLldsDDTLATLEALRALGAK--IEEEGGTV---EIVGGGGLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 86 DLVK----------TMRasiLVLGPLLARFGHARVSlpGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKrL 155
Cdd:cd01556 70 LPPEavldcgnsgtTMR---LLTGLLALQGGDSVLT--GDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGG-L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 156 RGARIVTDMVT----VTGtenLLMAAALADGETVLENAAREPEVT-DL-ANLLVKMGARIEGIGTDRLVIQSVEALHGAA 229
Cdd:cd01556 144 KGGEVEIPGAVssqfKSA---LLLAAPLAEGPTTIIIGELESKPYiDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 230 HTVIADRIEAGTFLCAVAAAGGDVTLRAVPPGILD-AVLDKLREAGVTLTTGD-DWIRVQMTGRPKAVSFRTSEYP-AFP 306
Cdd:cd01556 221 YTVEGDASSAAFFLAAAAITGSEIVIKNVGLNSGDtGIIDVLKEMGADIEIGNeDTVVVESGGKLKGIDIDGNDIPdEAP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 307 TdmqaqFMMLNAIAEGSATVT--------ETifeNRF--MhVQELNRLGANI-------VIEGKTAVVTGVEQLSGatvm 369
Cdd:cd01556 301 T-----LAVLAAFAEGPTRIRnaaelrvkES---DRIaaM-ATELRKLGADVeetedglIIEGGPLKGAGVEVYTY---- 367
|
410 420
....*....|....*....|....*...
gi 746327587 370 aTDLRASASLVIAGLIAQGETLVDRIYH 397
Cdd:cd01556 368 -GDHRIAMSFAIAGLVAEGGVTIEDPEC 394
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-395 |
1.28e-12 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 69.02 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAK---NAALpiMCAALLTAEplalSNVPNL---QDVRTMLKLLRQMGVEgvLDGHNLTLD 74
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLAALAEGE----TTITNLlrsEDTLATLNALRALGVE--IEDDEVVVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 75 AATIHTPEASYDLVK------TMR--ASILVLGPLLARF-GHARvslpggcgIGARPVDQHIKGLQLMGAEIV-IEHGYI 144
Cdd:PRK02427 74 GVGGGGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQMGAKIEgRDEGYL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 145 EAKLaDGAKRLRGARIVTDMVT--VTGtenLLMAAAL-ADGETVLEnaAREPEV----TDL-ANLLVKMGARIEGIGTDR 216
Cdd:PRK02427 146 PLTI-RGGKKGGPIEYDGPVSSqfVKS---LLLLAPLfAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVENVEGWG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 217 LVIQSVEA---LHGAAHTVIADRIEAGTFLCAVAAAGG-DVTLRAVP-----PGilDAVLDKLREAGVTLTTGDDW---- 283
Cdd:PRK02427 220 YRRIVIKGgqrLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGlnstqGG--KAIIDVLEKMGADIEIENERegge 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 284 ----IRVQmTGRPKAVSFRTSEYP-AFPTdmqaqFMMLNAIAEGsatvtETIFEN----RF--------MhVQELNRLGA 346
Cdd:PRK02427 298 pvgdIRVR-SSELKGIDIDIPDIIdEAPT-----LAVLAAFAEG-----TTVIRNaeelRVketdriaaM-ATELRKLGA 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 746327587 347 NIVIEGKTAVVTGVEqlSGATV-------MATdlrasaSLVIAGLIAQGETLVDRI 395
Cdd:PRK02427 366 EVEETEDGLIITGGP--LAGVVdsygdhrIAM------AFAIAGLAAEGPVTIDDP 413
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
174-419 |
1.77e-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: 65.27 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 174 LMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGtDRLVIQSVEALHGAAHTVIaDRIEAGT---FLCAVAAAG 250
Cdd:cd01556 18 LLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG-GTVEIVGGGGLGLPPEAVL-DCGNSGTtmrLLTGLLALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 251 -------GDVTLRAVPpgiLDAVLDKLREAGVTLTTGDDWIRVQMTGRPKAVSFRTsEYPAfptDMQAQF----MMLNAI 319
Cdd:cd01556 96 ggdsvltGDESLRKRP---MGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEV-EIPG---AVSSQFksalLLAAPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 320 AEGSATVTETIFEN---RFMHVQELNRLGANI-VIEGKTAVVTGVEQLSGA--TVMAtDLRASASLVIAGLIAQGETLVd 393
Cdd:cd01556 169 AEGPTTIIIGELESkpyIDHTERMLRAFGAEVeVDGYRTITVKGGQKYKGPeyTVEG-DASSAAFFLAAAAITGSEIVI- 246
|
250 260
....*....|....*....|....*.
gi 746327587 394 RIYHLDRGYDRIEDKLSAVGAKIRRI 419
Cdd:cd01556 247 KNVGLNSGDTGIIDVLKEMGADIEIG 272
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
174-419 |
5.15e-09 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 57.85 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 174 LMAAALADGETVLENAAREPEVTDLANLLVKMGARIEgigTDRLVIQSVEALHGAAHTVIADRIEAGT---FLCAVAAAG 250
Cdd:PRK02427 30 LLLAALAEGETTITNLLRSEDTLATLNALRALGVEIE---DDEVVVEGVGGGGLKEPEDVLDCGNSGTtmrLLTGLLALQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 251 -------GDVTLRAVPpgiLDAVLDKLREAGVTLTTGDDW---IRVQMTGRPKAVSFRTSEYPAFPTDMqaqfMM---LN 317
Cdd:PRK02427 107 pgevvltGDESLRKRP---MGRLLDPLRQMGAKIEGRDEGylpLTIRGGKKGGPIEYDGPVSSQFVKSL----LLlapLF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 318 AIAEGSATVTETI-----FEnrfMHVQELNRLGANIVIEGKTAVVTGVEQlSGATVMATDLR-----ASAS-LVIAGLIA 386
Cdd:PRK02427 180 AEGDTETTVIEPLpsrphTE---ITLRMLRAFGVEVENVEGWGYRRIVIK-GGQRLRGQDITvpgdpSSAAfFLAAAAIT 255
|
250 260 270
....*....|....*....|....*....|....*..
gi 746327587 387 QGETLvdRIYHLD----RGYDRIEDKLSAVGAKIRRI 419
Cdd:PRK02427 256 GGSEV--TITNVGlnstQGGKAIIDVLEKMGADIEIE 290
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
10-290 |
6.04e-07 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 51.63 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 10 GPLS---GEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTLDAATIHTPEASYD 86
Cdd:PRK11861 246 GPFShaqGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTAD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 87 L--------VKTMRASILVLGpllarfGHARVSlpGGCGIGARPVDQHIKGLQLMGAEIVIE--HGYIEAKL------AD 150
Cdd:PRK11861 326 LflgnagtaVRPLTAALAVNG------GEYRIH--GVPRMHERPIGDLVDGLRQIGARIDYEgnEGFPPLRIrpatisVD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 151 GAKRLRGARIVTDMVTVTGTENLLMAaalADGETVLE---NAAREPEVTDLANLLVKMGARIEGIGTDRLVIQS-VEALH 226
Cdd:PRK11861 398 APIRVRGDVSSQFLTALLMTLPLVKA---KDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVPAgVRYRS 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 746327587 227 GAAHTVIADRIEAGTFLCAVAAAGGDVTLRAVPPGILD---AVLDKLREAGVTLTTGDDWIRVQMTG 290
Cdd:PRK11861 475 PGTIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQgdvGFANALMQMGANVTMGDDWIEVRGIG 541
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
10-278 |
1.62e-05 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 47.30 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 10 GPLSGEIRVSGAKNAA-LPIMCAALltAEPLA-LSNVPNLQDVRTMLKLLRQMGV--EGVLDGHnLTLDAATIH--TPEA 83
Cdd:PRK14806 310 GAVKGTIRVPGDKSIShRSIMLGSL--AEGVTeVEGFLEGEDALATLQAFRDMGVviEGPHNGR-VTIHGVGLHglKAPP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 84 SYDLVKTMRASILVLGPLLArfGHA-RVSLPGGCGIGARPVDQHIKGLQLMGAEIVIEHGYIEAKLADGAKRLRGARIVT 162
Cdd:PRK14806 387 GPLYMGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEGRPPLSIRGGQRLKGIHYDL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 163 DMVTVTGTENLLMAAALADGETvlenAAREPEVT--DLANLLVKMGARIEGIGtDRLVIQSVEALHGAAHTVIADRIEAG 240
Cdd:PRK14806 465 PMASAQVKSCLLLAGLYAEGET----SVTEPAPTrdHTERMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPADISSAA 539
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 746327587 241 TFLCAVA-AAGGDVTLRAVppGI---LDAVLDKLREAGVTLT 278
Cdd:PRK14806 540 FFLVAASiAEGSELTLEHV--GInptRTGVIDILKLMGADIT 579
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
174-418 |
1.86e-04 |
|
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: 43.42 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 174 LMAAALADGETVLENAAREPEVTDLANLLVKMGARIEGIGtDRLVIQSVEALHGAAHTVIAdriEAGT---FLCAVAAAG 250
Cdd:TIGR01356 16 LILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGG-EVAVIEGVGGKEPQAELDLG---NSGTtarLLTGVLALA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 251 -------GDVTLRAVPpgiLDAVLDKLREAGVTL--TTGDDWIRVQMTGRPKAVSFRTSeypafpTDMQAQF---MMLNA 318
Cdd:TIGR01356 92 dgevvltGDESLRKRP---MGRLVDALRQLGAEIssLEGGGSLPLTISGPLPGGIVYIS------GSASSQYksaLLLAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 319 IAEGSATVTETIFENR-----FMHVQELNRLGANIVIE-GKTAVVTGVEQLSGATV-MATDLRASASLVIAGLIAQGETl 391
Cdd:TIGR01356 163 PALQAVGITIVGEPLKsrpyiEITLDLLGSFGVEVERSdGRKIVVPGGQKYGPQGYdVPGDYSSAAFFLAAAAITGGRV- 241
|
250 260 270
....*....|....*....|....*....|.
gi 746327587 392 vdRIYHL----DRGYDRIEDKLSAVGAKIRR 418
Cdd:TIGR01356 242 --TLENLginpTQGDKAIIIVLEEMGADIEV 270
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-256 |
8.13e-03 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 38.19 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 1 MDKLLIEGNGPLSGEIRVSGAKNAALPIMCAALLTAEPLALSNVPNLQDVRTMLKLLRQMGVEGVLDGHNLTldaATIHT 80
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNR---AVVEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 81 PEASYDLVKTMRASI-LVLG-------PLLARF----GHARVSLPGGCGIGARPVDQHIKGLQLMGAEI--VIEHGYIEA 146
Cdd:PLN02338 78 CGGKFPVSGDSKEDVeLFLGnagtamrPLTAAVtaagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVecTLGTNCPPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746327587 147 KLaDGAKRLRGARI-VTDMVTVTGTENLLMAAALADGE---TVLENAAREPEVTDLANLLVKMGARIEGIGT-DRLVIQS 221
Cdd:PLN02338 158 RV-NAAGGLPGGKVkLSGSISSQYLTALLMAAPLALGDveiEIVDKLISVPYVEMTLKLMERFGVSVEHSDSwDRFFIKG 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 746327587 222 VEALH--GAAHtVIADRIEAGTFLCAVAAAGGDVTLR 256
Cdd:PLN02338 237 GQKYKspGNAY-VEGDASSASYFLAGAAITGGTVTVE 272
|
|
| |
