|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 780.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER--NGSVHIDARDVN 78
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 79 VFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVM 158
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 159 DKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 239 LVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGkRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 319 GTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
|
410
....*....|....*...
gi 16131079 399 YERIEDKLRALGANIERV 416
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
|
|
| 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: 742.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER--NGSVHIDARDVN 78
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERddGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 79 VFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDgRLKGAHIVM 158
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAG-RLKGARIYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 159 DKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 239 LVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGkRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAE 318
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 319 GTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:COG0766 319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
|
410
....*....|....*...
gi 16131079 399 YERIEDKLRALGANIERV 416
Cdd:COG0766 399 YENLEEKLRALGADIERV 416
|
|
| 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: 701.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNG--SVHIDARDVNVFCAPYDLVKT 89
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGenTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 90 MRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTI 169
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 170 MCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKI 249
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 250 ICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 330 NRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 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: 672.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER-NGSVHIDARDVNV 79
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERdNNTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 80 FCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMD 159
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 160 KVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 240 VAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEG 319
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 320 TGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGY 399
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
|
410
....*....|....*.
gi 16131079 400 ERIEDKLRALGANIER 415
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
2.14e-167 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 475.63 E-value: 2.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 7 QGPTKLQGEVTISG-AKNAALPILFAALLAEEpVEIQNVPKLKDVDTSMKLLSQLGA---KVERNGSVHIDARDVNVFCA 82
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGE-STITNLLDSDDTLTMLEALRALGAeiiKLDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 83 PYDLVKTMRASIWALGPLVARFGQ--GQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVD---GRLKGAHIV 157
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALqsGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 158 MDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTD-RIVIEGVERLGGGVYRVLPDRIETG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 237 TFLVAAAISRGKIICRNAQPDTL---DAVLAKLRDAGADIEVGED-WISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTL 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 313 LNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEK-LSGAQVMAT-DLRASASLVLAGCIAEGTTVVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 16131079 391 RIYHIDRGYERIEDKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 780.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER--NGSVHIDARDVN 78
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 79 VFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVM 158
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 159 DKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 239 LVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGkRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 319 GTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
|
410
....*....|....*...
gi 16131079 399 YERIEDKLRALGANIERV 416
Cdd:PRK09369 400 YERIEEKLRALGADIERV 417
|
|
| 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: 742.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER--NGSVHIDARDVN 78
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERddGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 79 VFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDgRLKGAHIVM 158
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAG-RLKGARIYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 159 DKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 239 LVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGkRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAE 318
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 319 GTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:COG0766 319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
|
410
....*....|....*...
gi 16131079 399 YERIEDKLRALGANIERV 416
Cdd:COG0766 399 YENLEEKLRALGADIERV 416
|
|
| 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: 701.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNG--SVHIDARDVNVFCAPYDLVKT 89
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGenTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 90 MRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTI 169
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 170 MCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKI 249
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 250 ICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 330 NRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 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: 672.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER-NGSVHIDARDVNV 79
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERdNNTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 80 FCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMD 159
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 160 KVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 240 VAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEG 319
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 320 TGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGY 399
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
|
410
....*....|....*.
gi 16131079 400 ERIEDKLRALGANIER 415
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-409 |
0e+00 |
|
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: 552.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERN-GSVHIDARDVNVFCAP---YDLV 87
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKdGVITIQGVGMAGLKAPqnaLNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 88 KTMRASIWALGPLVARfgQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKAS--VDGRLKGAHIVMDKV-SVG 164
Cdd:cd01554 81 NSGTAIRLISGVLAGA--DFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPllKGGKNLGPIHYEDPIaSAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 165 ATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAI 244
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 245 SRGKIICRNAQPDT-LDAVLAKLRDAGADIEVGEDWISLDMHgkRPKAVNVRTAPHPaFPTDMQAQFTLLNLVAEGTGFI 323
Cdd:cd01554 239 APGRLVLQNVGINEtRTGIIDVLRAMGAKIEIGEDTISVESS--DLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 324 TETVF------ENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMAT-DLRASASLVLAGCIAEGTTVVDRIYHID 396
Cdd:cd01554 316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
|
410
....*....|...
gi 16131079 397 RGYERIEDKLRAL 409
Cdd:cd01554 396 TSYPSFFDDLESL 408
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-417 |
1.56e-180 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 509.01 E-value: 1.56e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNG-SVHIDARDVNV 79
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGdTLEIDPTGIQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 80 FCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDgRLKGAHIVMD 159
Cdd:PRK12830 81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD-ELKGAHIYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 160 KVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 240 VAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDwiSLDMHGKRP-KAVNVRTAPHPAFPTDMQAQFTLLNLVAE 318
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNED--SIFVEKQGNlKAVDIKTLPYPGFATDLQQPLTPLLLKAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 319 GTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK12830 318 GRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
|
410
....*....|....*....
gi 16131079 399 YERIEDKLRALGANIERVK 417
Cdd:PRK12830 398 YSNIIEKLKALGADIWREE 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
2.14e-167 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 475.63 E-value: 2.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 7 QGPTKLQGEVTISG-AKNAALPILFAALLAEEpVEIQNVPKLKDVDTSMKLLSQLGA---KVERNGSVHIDARDVNVFCA 82
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGE-STITNLLDSDDTLTMLEALRALGAeiiKLDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 83 PYDLVKTMRASIWALGPLVARFGQ--GQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVD---GRLKGAHIV 157
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALqsGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 158 MDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTD-RIVIEGVERLGGGVYRVLPDRIETG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 237 TFLVAAAISRGKIICRNAQPDTL---DAVLAKLRDAGADIEVGED-WISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTL 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 313 LNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEK-LSGAQVMAT-DLRASASLVLAGCIAEGTTVVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 16131079 391 RIYHIDRGYERIEDKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
230-409 |
3.16e-54 |
|
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: 179.40 E-value: 3.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 230 PDRIETGTFLVAAAISRGKIICRNAQPDT--------LDAVLAKLRDA-GADIEVGE---DWISLDMHGkrPKAVNVRTA 297
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTGIRPDRakpgllrqHLTFLKALEKIcGATVEGGElgsDRISFRPGT--VRGGDVRFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 298 PHPA-FPTDMQAQFTLLNLVAEGTGFITETVF----------ENRFMHVPELSRMGAHAEIESN------------TVIC 354
Cdd:cd01553 86 IGSAgSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131079 355 HGVEKLSGAQVmatdlRASASLVLAGciaeGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01553 166 SPVEKLNTAQL-----RQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-396 |
3.66e-31 |
|
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: 123.27 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAK---NAALpilFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER--NGSVHID-- 73
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL---LLAALAEGESTIRNLLESDDTLATLEALRALGAEIEEldGGTLRVTgv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 74 -----ARDVNVFCapydlvK----TMR--ASIWALGPLVARF-GQGQvslpggctIGARPVDLHISGLEQLGATIK-LEE 140
Cdd:COG0128 78 ggglkEPDAVLDC------GnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQLGARIEsRGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 141 GYVKASVDG-RLKGAHIVMDKVS----VGAtvtIMCAATLAE-GTTIIENAAREPEI-VD-TANFLITLGAKISGQGTDR 212
Cdd:COG0128 144 GYLPLTIRGgPLKGGEYEIPGSAssqfKSA---LLLAGPLAEgGLEITVTGELESKPyRDhTERMLRAFGVEVEVEGYRR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 213 IVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTL---DAVLAKLRDAGADIEVGEDWISLdmHGKRP 289
Cdd:COG0128 221 FTVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITV--RGSPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 290 KAVNV--RTAPHpAFPTdmqaqFTLLNLVAEGTgfiteTVFEN----RF--------MhVPELSRMGAHAEIESNTVICH 355
Cdd:COG0128 299 KGIDIdlSDIPD-EAPT-----LAVLAAFAEGT-----TRIRGaaelRVkesdriaaM-ATELRKLGADVEETEDGLIIE 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16131079 356 GVEKLSGAQV-------MATdlrasaSLVLAGCIAEGTTVVDRIYHID 396
Cdd:COG0128 367 GGPKLKGAEVdsygdhrIAM------AFAVAGLRAEGPVTIDDAECVA 408
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-396 |
1.04e-30 |
|
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: 121.90 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNG-SVHIDARDVNVFCAPYDLV--- 87
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGgTVEIVGGGGLGLPPEAVLDcgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 88 --KTMRASIwalgPLVArFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKL--EEGYVKASVDGRLKGAHIVMDkVSV 163
Cdd:cd01556 81 sgTTMRLLT----GLLA-LQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGreGGGYPPLIGGGGLKGGEVEIP-GAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 164 GATVT--IMCAATLAEGTTIIENAAREPEI-VD-TANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:cd01556 155 SSQFKsaLLLAAPLAEGPTTIIIGELESKPyIDhTERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSAAFFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 240 VAAAISRGKIICRNAQPDTLDAVLAK-LRDAGADIEVGEDWIsLDMHGKRP-KAVNVRTAPHP-AFPTdmqaqFTLLNLV 316
Cdd:cd01556 235 AAAAITGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIGNEDT-VVVESGGKlKGIDIDGNDIPdEAPT-----LAVLAAF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 317 AEGTGFIT--------ETvfeNRF--MHVpELSRMGAHAEIESNTVICHGVEKLSGAQVMAT--DLRASASLVLAGCIAE 384
Cdd:cd01556 309 AEGPTRIRnaaelrvkES---DRIaaMAT-ELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAMSFAIAGLVAE 384
|
410
....*....|..
gi 16131079 385 GTTVVDRIYHID 396
Cdd:cd01556 385 GGVTIEDPECVA 396
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-412 |
2.19e-29 |
|
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: 118.15 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 14 GEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVER-NGSVHIDArdvnVFCAPYDLVKTMRA 92
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDgGEVAVIEG----VGGKEPQAELDLGN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 93 SIWALGPL--VARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATI--KLEEGYVKASVDGRLKGAHIVMDKV--SVGAT 166
Cdd:TIGR01356 77 SGTTARLLtgVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIssLEGGGSLPLTISGPLPGGIVYISGSasSQYKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 167 VTIMCAATLAEGTTIIENAarepEIVDTANFLITL------GAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLV 240
Cdd:TIGR01356 157 ALLLAAPALQAVGITIVGE----PLKSRPYIEITLdllgsfGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 241 AAAISRGKIICRNAQPDTL---DAVLAKLRDAGADIEVGEDWISLDMHGKRpKAVNVRTAPHP-AFPTdmqaqFTLLNLV 316
Cdd:TIGR01356 233 AAAITGGRVTLENLGINPTqgdKAIIIVLEEMGADIEVEEDDLIVEGASGL-KGIKIDMDDMIdELPT-----LAVLAAF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 317 AEGTGFIT--------ETvfeNRF--MHVpELSRMGAHAEIESNTVICHGVEKLSGAqVMAT--DLRASASLVLAGCIAE 384
Cdd:TIGR01356 307 AEGVTRITgaeelrvkES---DRIaaIAE-ELRKLGVDVEEFEDGLYIRGKKELKGA-VVDTfgDHRIAMAFAVAGLVAE 381
|
410 420
....*....|....*....|....*...
gi 16131079 385 GTTVVDRIYHIDRGYERIEDKLRALGAN 412
Cdd:TIGR01356 382 GEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-414 |
2.81e-23 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 100.99 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAK---NAALpiLFAALlAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERnGSVHIDARDV 77
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLAAL-AEGETTITNLLRSEDTLATLNALRALGVEIED-DEVVVEGVGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 78 NVFCAPYDLVK------TMR--ASIWALGPLVARFgQGQVSLpggctiGARPVDLHISGLEQLGATIKL-EEGYVKASVD 148
Cdd:PRK02427 78 GGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVL-TGDESL------RKRPMGRLLDPLRQMGAKIEGrDEGYLPLTIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 149 GRLKGAHIVMD-KVSvGATVT--IMCAATLAEG---TTIIENAAREPEIVDTANFLITLGAKISGQGTD---RIVIEGVE 219
Cdd:PRK02427 151 GGKKGGPIEYDgPVS-SQFVKslLLLAPLFAEGdteTTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWgyrRIVIKGGQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 220 RLGGGVYRVLPDRIETGTFLVAAAISRG-KIICRN-----AQPDtlDAVLAKLRDAGADIEVGEDWISL----DMHGKRP 289
Cdd:PRK02427 230 RLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNvglnsTQGG--KAIIDVLEKMGADIEIENEREGGepvgDIRVRSS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 290 --KAVNVrTAPH-P-AFPTdmqaqFTLLNLVAEGTgfiteTVFEN----RF--------MHVpELSRMGAHAEIESNTVI 353
Cdd:PRK02427 308 elKGIDI-DIPDiIdEAPT-----LAVLAAFAEGT-----TVIRNaeelRVketdriaaMAT-ELRKLGAEVEETEDGLI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131079 354 CHGVEKlsGAQV-------MATdlrasaSLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIE 414
Cdd:PRK02427 376 ITGGPL--AGVVdsygdhrIAM------AFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-390 |
1.12e-07 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 53.60 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 1 MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNgsvHIDARDVNVF 80
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEED---SENNRAVVEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 81 CA---PYDLVKTMRASIW------ALGPL----VARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGY----V 143
Cdd:PLN02338 78 CGgkfPVSGDSKEDVELFlgnagtAMRPLtaavTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTncppV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 144 KASVDGRLKGAHIVMD-KVSVGATVTIMCAATLAEGT---TIIENAAREPEIVDTANFLITLGAKISGQGT-DRIVIEGV 218
Cdd:PLN02338 158 RVNAAGGLPGGKVKLSgSISSQYLTALLMAAPLALGDveiEIVDKLISVPYVEMTLKLMERFGVSVEHSDSwDRFFIKGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 219 ERLG--GGVYrVLPDRIETGTFLVAAAISRGKIICRNAQPDTL--DAVLAK-LRDAGADIEVGEDWISL------DMHGK 287
Cdd:PLN02338 238 QKYKspGNAY-VEGDASSASYFLAGAAITGGTVTVEGCGTTSLqgDVKFAEvLEKMGAKVEWTENSVTVtgpprdAFGGK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 288 RPKAVNVRTAPHPafptDMQAQFTLLNLVAEGTGFITET----VFENRFMH--VPELSRMGAHAEIESNTVICHGVEKLS 361
Cdd:PLN02338 317 HLKAIDVNMNKMP----DVAMTLAVVALFADGPTAIRDVaswrVKETERMIaiCTELRKLGATVEEGPDYCIITPPKKLK 392
|
410 420 430
....*....|....*....|....*....|
gi 16131079 362 GAQV-MATDLRASASLVLAGCIAEGTTVVD 390
Cdd:PLN02338 393 PAEIdTYDDHRMAMAFSLAACGDVPVTIND 422
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
8-346 |
5.73e-07 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 51.63 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 8 GP-TKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDL 86
Cdd:PRK11861 246 GPfSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTAD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 87 VKTMRASIwALGPLVARFG--QGQVSLPGGCTIGARPVDLHISGLEQLGATIKLE--EGY-------VKASVDG--RLKG 153
Cdd:PRK11861 326 LFLGNAGT-AVRPLTAALAvnGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEgnEGFpplrirpATISVDApiRVRG 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 154 AHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVI-EGVERLGGGVYRVLPDR 232
Cdd:PRK11861 405 DVSSQFLTALLMTLPLVKAKDGASVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGTIMVEGDA 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 233 IETGTFLVAAAISRGKIICRNAQPDTLDAVLA---KLRDAGADIEVGEDWISL----DMHGK-RPKAVNVRTAPHPAFPT 304
Cdd:PRK11861 485 SSASYFLAAGALGGGPLRVEGVGRASIQGDVGfanALMQMGANVTMGDDWIEVrgigHDHGRlAPIDMDFNLIPDAAMTI 564
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16131079 305 DMQAQF-----TLLNLvaeGTGFITETvfENRFMHVPELSRMGAHAE 346
Cdd:PRK11861 565 AVAALFadgpsTLRNI---GSWRVKET--DRIAAMATELRKVGATVE 606
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
4-275 |
5.98e-04 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 42.29 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 4 FRVQGPTKLQGEVTISGAKNAA-LPILFAALlAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVE--RNGSVHIDARDVNVF 80
Cdd:PRK14806 304 YSVLPGGAVKGTIRVPGDKSIShRSIMLGSL-AEGVTEVEGFLEGEDALATLQAFRDMGVVIEgpHNGRVTIHGVGLHGL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 81 CAP----YdlVKTMRASIWALGPLVArfGQG-QVSLPGGCTIGARPVDLHISGLEQLGATIKL-EEGYVKASVDG--RLK 152
Cdd:PRK14806 383 KAPpgplY--MGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETgEEGRPPLSIRGgqRLK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 153 GAHIVMDKVSVGATVTIMCAATLAEGTTIIenaaREPEIV--DTANFLITLGAKISGQGtDRIVIEGVERLGGGVYRVLP 230
Cdd:PRK14806 459 GIHYDLPMASAQVKSCLLLAGLYAEGETSV----TEPAPTrdHTERMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPA 533
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16131079 231 DRIETGTFLVAAAISRG-KIICRNAQPD-TLDAVLAKLRDAGADIEV 275
Cdd:PRK14806 534 DISSAAFFLVAASIAEGsELTLEHVGINpTRTGVIDILKLMGADITL 580
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
239-415 |
2.55e-03 |
|
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: 39.85 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 239 LVAAAISRGKIICRNA--QPDTLDAVLAkLRDAGADIEVGEDwiSLDMHGkrpkavNVRTAPHPAFPTDMQ----AQFTL 312
Cdd:cd01556 18 LLLAALAEGESRIENLldSDDTLATLEA-LRALGAKIEEEGG--TVEIVG------GGGLGLPPEAVLDCGnsgtTMRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131079 313 LNLVAEGTGFITETVFE---NRFMH--VPELSRMGAHAE--IESNTVICHGVEKLSGAQVmatDLRASAS------LVLA 379
Cdd:cd01556 89 TGLLALQGGDSVLTGDEslrKRPMGrlVDALRQLGAEIEgrEGGGYPPLIGGGGLKGGEV---EIPGAVSsqfksaLLLA 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131079 380 GCIAEGTTVVDRIYHIDRGYERI-EDKLRALGANIER 415
Cdd:cd01556 166 APLAEGPTTIIIGELESKPYIDHtERMLRAFGAEVEV 202
|
|
| |
