|
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: 780.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER--*GSVWIDASNVN 78
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVM 158
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
|
410
....*....|....*...
1Q3G_K 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: 742.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*--GSVWIDASNVN 78
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdgGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNgRLKGAHIVM 158
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAG-RLKGARIYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:COG0766 319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
|
410
....*....|....*...
1Q3G_K 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: 700.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G--SVWIDASNVNNFSAPYDLVKT 89
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGenTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 90 MRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTI 169
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 170 MSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKI 249
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 250 VCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEGTGVITETIFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 330 NRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRAL 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: 674.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G-SVWIDASNVNN 79
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNnTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 80 FSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMD 159
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 160 KVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 240 VAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEG 319
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 320 TGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGY 399
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
|
410
....*....|....*.
1Q3G_K 400 ERIEDKLRALGANIER 415
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
1.03e-163 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 466.39 E-value: 1.03e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 7 QGPTRLQGEVTISG-AKNAALPILFAALLAEEpVEIQNVPKLKDIDTTMKLLTQLG---TKVER*GSVWIDASNVNNFSA 82
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGE-STITNLLDSDDTLTMLEALRALGaeiIKLDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 83 PYDLVKTMRASIWALGPLVARFGQ--GQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASV---NGRLKGAHIV 157
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALqsGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLkvrGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 158 MDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTD-RITIEGVERLGGGVYRVLPDRIETG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 237 TFLVAAAISGGKIVCRNAQPDTL---DAVLAKLREAGADIETGED-WISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTL 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 313 LNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEK-LSGAQVMAT-DLRASASLVLAGCIAEGTTVVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
1Q3G_K 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: 780.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER--*GSVWIDASNVN 78
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFdgNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVM 158
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHIVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK09369 320 GTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRG 399
|
410
....*....|....*...
1Q3G_K 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: 742.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*--GSVWIDASNVN 78
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdgGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 79 NFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNgRLKGAHIVM 158
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAG-RLKGARIYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 159 DKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTF 238
Cdd:COG0766 160 DFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 239 LVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGkRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:COG0766 240 LVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:COG0766 319 GTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
|
410
....*....|....*...
1Q3G_K 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: 700.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G--SVWIDASNVNNFSAPYDLVKT 89
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGenTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 90 MRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTI 169
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 170 MSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKI 249
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 250 VCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEGTGVITETIFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 330 NRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRAL 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: 674.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G-SVWIDASNVNN 79
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNnTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 80 FSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMD 159
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 160 KVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:TIGR01072 161 KVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 240 VAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTLLNLVAEG 319
Cdd:TIGR01072 241 VAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 320 TGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGY 399
Cdd:TIGR01072 321 TSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGY 400
|
410
....*....|....*.
1Q3G_K 400 ERIEDKLRALGANIER 415
Cdd:TIGR01072 401 EDLEEKLRALGAKIER 416
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-409 |
3.09e-180 |
|
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: 508.30 E-value: 3.09e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER-*GSVWIDASNVNNFSAP---YDLV 87
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDkDGVITIQGVGMAGLKAPqnaLNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 88 KTMRASIWALGPLVARfgQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKAS--VNGRLKGAHIVMDKV-SVG 164
Cdd:cd01554 81 NSGTAIRLISGVLAGA--DFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPllKGGKNLGPIHYEDPIaSAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 165 ATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAI 244
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 245 SGGKIVCRNAQPDT-LDAVLAKLREAGADIETGEDWISLDMHgkRPKAVTVRTAPHPaFPTAMQAQFTLLNLVAEGTGVI 323
Cdd:cd01554 239 APGRLVLQNVGINEtRTGIIDVLRAMGAKIEIGEDTISVESS--DLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 324 TETIF------ENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMAT-DLRASASLVLAGCIAEGTTVVDRIYHID 396
Cdd:cd01554 316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
|
410
....*....|...
1Q3G_K 397 RGYERIEDKLRAL 409
Cdd:cd01554 396 TSYPSFFDDLESL 408
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-417 |
3.94e-180 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 508.24 E-value: 3.94e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*G-SVWIDASNVNN 79
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGdTLEIDPTGIQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 80 FSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNgRLKGAHIVMD 159
Cdd:PRK12830 81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKAD-ELKGAHIYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 160 KVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 240 VAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDwiSLDMHGKRP-KAVTVRTAPHPAFPTAMQAQFTLLNLVAE 318
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNED--SIFVEKQGNlKAVDIKTLPYPGFATDLQQPLTPLLLKAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 319 GTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRG 398
Cdd:PRK12830 318 GRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
|
410
....*....|....*....
1Q3G_K 399 YERIEDKLRALGANIERVK 417
Cdd:PRK12830 398 YSNIIEKLKALGADIWREE 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
1.03e-163 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 466.39 E-value: 1.03e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 7 QGPTRLQGEVTISG-AKNAALPILFAALLAEEpVEIQNVPKLKDIDTTMKLLTQLG---TKVER*GSVWIDASNVNNFSA 82
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAGE-STITNLLDSDDTLTMLEALRALGaeiIKLDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 83 PYDLVKTMRASIWALGPLVARFGQ--GQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASV---NGRLKGAHIV 157
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALqsGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLkvrGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 158 MDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTD-RITIEGVERLGGGVYRVLPDRIETG 236
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 237 TFLVAAAISGGKIVCRNAQPDTL---DAVLAKLREAGADIETGED-WISLDMHGKRPKAVTVRTAPHPAFPTAMQAQFTL 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 313 LNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEK-LSGAQVMAT-DLRASASLVLAGCIAEGTTVVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
1Q3G_K 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 |
4.78e-49 |
|
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: 165.92 E-value: 4.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 230 PDRIETGTFLVAAAISGGKIVCRNAQPDT--------LDAVLAKLREA-GADIETGE---DWISLDMHGkrPKAVTVRTA 297
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTGIRPDRakpgllrqHLTFLKALEKIcGATVEGGElgsDRISFRPGT--VRGGDVRFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 298 PHPA-FPTAMQAQFTLLNLVAEGTGVITETIF----------ENRFMHVPELIRMGAHAEIESN------------TVIC 354
Cdd:cd01553 86 IGSAgSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1Q3G_K 355 HGVEKLSGAQVmatdlRASASLVLAGciaeGTTVVDRIYHIDRGYERIEDKLRAL 409
Cdd:cd01553 166 SPVEKLNTAQL-----RQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-396 |
1.14e-33 |
|
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: 130.21 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAK---NAALpilFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*-GSVWIDASN 76
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL---LLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELdGGTLRVTGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 77 VNNFSAPYDLVK------TMR--ASIWALGPLVARF-GQGQvslpggcaIGARPVDlHIFG-LEKLGAEIK-LEEGYVKA 145
Cdd:COG0128 78 GGGLKEPDAVLDcgnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMG-RLLDpLRQLGARIEsRGGGYLPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 146 SVNG-RLKGAHIVMDkVSVGATVT---IMSAATLAEGTTIIENAAREPEI-VD-TANFLVALGAKISGQGTDRITIEGVE 219
Cdd:COG0128 149 TIRGgPLKGGEYEIP-GSASSQFKsalLLAGPLAEGGLEITVTGELESKPyRDhTERMLRAFGVEVEVEGYRRFTVPGGQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 220 RLGGGVYRVLPDRIETGTFLVAAAISGGKIVCRNAQPDTL---DAVLAKLREAGADIETGEDWISLdmHGKRPKAVTV-- 294
Cdd:COG0128 228 RYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITV--RGSPLKGIDIdl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 295 RTAPHpAFPTamqaqFTLLNLVAEGTGVIT--------ETifeNRF--MhVPELIRMGAHAEIESNTVICHGVEKLSGAQ 364
Cdd:COG0128 306 SDIPD-EAPT-----LAVLAAFAEGTTRIRgaaelrvkES---DRIaaM-ATELRKLGADVEETEDGLIIEGGPKLKGAE 375
|
410 420 430
....*....|....*....|....*....|....*....
1Q3G_K 365 V-------MATdlrasaSLVLAGCIAEGTTVVDRIYHID 396
Cdd:COG0128 376 VdsygdhrIAM------AFAVAGLRAEGPVTIDDAECVA 408
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-396 |
7.52e-31 |
|
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: 122.28 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 12 LQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIDASNVNNFSAPYDLVK--- 88
Cdd:cd01556 1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLGLPPEAVLDcgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 89 ---TMRASIwalgPLVArFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKL--EEGYVKASVNGRLKGAHIVMDkVSV 163
Cdd:cd01556 81 sgtTMRLLT----GLLA-LQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGreGGGYPPLIGGGGLKGGEVEIP-GAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 164 GATVT--IMSAATLAEGTTIIENAAREPEI-VD-TANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFL 239
Cdd:cd01556 155 SSQFKsaLLLAAPLAEGPTTIIIGELESKPyIDhTERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSAAFFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 240 VAAAISGGKIVCRNAQPDTLDAVLAK-LREAGADIETGEDWIsLDMHGKRP-KAVTVRTAPHP-AFPTAmqaqfTLLNLV 316
Cdd:cd01556 235 AAAAITGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIGNEDT-VVVESGGKlKGIDIDGNDIPdEAPTL-----AVLAAF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 317 AEGTGVIT--------ETifeNRF--MHVpELIRMGAHAEIESNTVICHGVEKLSGAQVMAT--DLRASASLVLAGCIAE 384
Cdd:cd01556 309 AEGPTRIRnaaelrvkES---DRIaaMAT-ELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAMSFAIAGLVAE 384
|
410
....*....|..
1Q3G_K 385 GTTVVDRIYHID 396
Cdd:cd01556 385 GGVTIEDPECVA 396
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-412 |
5.80e-30 |
|
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: 119.69 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 14 GEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIdaSNVNNFSAPYDLVKtMRAS 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAV--IEGVGGKEPQAELD-LGNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 94 IWALGPL--VARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEI--KLEEGYVKASVNGRLKGAHIVMDKV--SVGATV 167
Cdd:TIGR01356 78 GTTARLLtgVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEIssLEGGGSLPLTISGPLPGGIVYISGSasSQYKSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 168 TIMSAATLAEG--TTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAIS 245
Cdd:TIGR01356 158 LLLAAPALQAVgiTIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAAIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 246 GGKIVCRNAQPDTL---DAVLAKLREAGADIETGEDWISLDMHGKRpKAVTVRTAPHP-AFPTAmqaqfTLLNLVAEGTG 321
Cdd:TIGR01356 238 GGRVTLENLGINPTqgdKAIIIVLEEMGADIEVEEDDLIVEGASGL-KGIKIDMDDMIdELPTL-----AVLAAFAEGVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 322 VIT--------ETifeNRF--MHVpELIRMGAHAEIESNTVICHGVEKLSGAqVMAT--DLRASASLVLAGCIAEGTTVV 389
Cdd:TIGR01356 312 RITgaeelrvkES---DRIaaIAE-ELRKLGVDVEEFEDGLYIRGKKELKGA-VVDTfgDHRIAMAFAVAGLVAEGEVLI 386
|
410 420
....*....|....*....|...
1Q3G_K 390 DRIYHIDRGYERIEDKLRALGAN 412
Cdd:TIGR01356 387 DDPECVAKSFPSFFDVLERLGAN 409
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-414 |
7.48e-24 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 102.91 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAK---NAALpiLFAALlAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIDASNV 77
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLAAL-AEGETTITNLLRSEDTLATLNALRALGVEIED-DEVVVEGVGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 78 NNFSAPYDLVK------TMR--ASIWALGPLVARFgQGQVSLpggcaiGARPVDlHIF-GLEKLGAEIKL-EEGYVKASV 147
Cdd:PRK02427 78 GGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVL-TGDESL------RKRPMG-RLLdPLRQMGAKIEGrDEGYLPLTI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 148 NGRLKGAHIVMD-KVSvGATVT--IMSAATLAEG---TTIIENAAREPEIVDTANFLVALGAKISGQGTD---RITIEGV 218
Cdd:PRK02427 150 RGGKKGGPIEYDgPVS-SQFVKslLLLAPLFAEGdteTTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWgyrRIVIKGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 219 ERLGGGVYRVLPDRIETGTFLVAAAISGG-KIVCRN-----AQPDtlDAVLAKLREAGADIETGEDWISL----DMHGKR 288
Cdd:PRK02427 229 QRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNvglnsTQGG--KAIIDVLEKMGADIEIENEREGGepvgDIRVRS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 289 P--KAVTVrTAPH-P-AFPTAmqaqfTLLNLVAEGTGVIT--------ETifeNRF--MHVpELIRMGAHAEIESNTVIC 354
Cdd:PRK02427 307 SelKGIDI-DIPDiIdEAPTL-----AVLAAFAEGTTVIRnaeelrvkET---DRIaaMAT-ELRKLGAEVEETEDGLII 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1Q3G_K 355 HGVEKlsGAQV-------MATdlrasaSLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIE 414
Cdd:PRK02427 377 TGGPL--AGVVdsygdhrIAM------AFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANIE 435
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
8-323 |
3.07e-09 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 58.95 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 8 GP-TRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVER*GSVWIDASNVNNFSAPYDL 86
Cdd:PRK11861 246 GPfSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAFTAKTAD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 87 VKTMRASIwALGPLVARFG--QGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLE--EGYVKAsvngRLKGAHIVMD--- 159
Cdd:PRK11861 326 LFLGNAGT-AVRPLTAALAvnGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEgnEGFPPL----RIRPATISVDapi 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 160 KVSVGATVTIMSAATLA-------EGTTIIE---NAAREPEIVDTANFLVALGAKISGQGTDRITI-EGVERLGGGVYRV 228
Cdd:PRK11861 401 RVRGDVSSQFLTALLMTlplvkakDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGTIMV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 229 LPDRIETGTFLVAAAISGGKIVCRNAQPDTLDAVLA---KLREAGADIETGEDWISL----DMHGK-RPKAVTVRTAPHP 300
Cdd:PRK11861 481 EGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGfanALMQMGANVTMGDDWIEVrgigHDHGRlAPIDMDFNLIPDA 560
|
330 340
....*....|....*....|...
1Q3G_K 301 AFPTAMQAQFtllnlvAEGTGVI 323
Cdd:PRK11861 561 AMTIAVAALF------ADGPSTL 577
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
172-415 |
4.03e-07 |
|
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: 52.01 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 172 AATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVerlgGGVYRVLPDRIE-----TGTFLVAAAISG 246
Cdd:COG0128 31 LAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGV----GGGLKEPDAVLDcgnsgTTMRLLTGLLAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 247 GKIVCR-------NAQPdtLDAVLAKLREAGADIE-TGEDWISLDMHGKRPKAVTVRTaphpafPTAMQAQFT----LLN 314
Cdd:COG0128 107 QPGEVVltgdeslRKRP--MGRLLDPLRQLGARIEsRGGGYLPLTIRGGPLKGGEYEI------PGSASSQFKsallLAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 315 LVAEGTGVITetifenrfmHVPEL---------IRM----GAHAEIE-SNTVICHGVEKLSGAQVM-ATDLRASASLVLA 379
Cdd:COG0128 179 PLAEGGLEIT---------VTGELeskpyrdhtERMlrafGVEVEVEgYRRFTVPGGQRYRPGDYTvPGDISSAAFFLAA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
1Q3G_K 380 GCIAEGTTVVDRI----YHIDRGyerIEDKLRALGANIER 415
Cdd:COG0128 250 AAITGSEVTVEGVglnsTQGDTG---ILDILKEMGADIEI 286
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-390 |
4.22e-06 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 48.59 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 1 MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVE--R*GSVWIDASNVN 78
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEedSENNRAVVEGCGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 79 NFSAPYDLVKTMRASI----WALGPL----VARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGY----VKAS 146
Cdd:PLN02338 81 KFPVSGDSKEDVELFLgnagTAMRPLtaavTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTncppVRVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 147 VNGRLKGAHIVMD-KVSVGATVTIMSAATLAEGT---TIIENAAREPEIVDTANFLVALGAKISGQGT-DRITIEGVERL 221
Cdd:PLN02338 161 AAGGLPGGKVKLSgSISSQYLTALLMAAPLALGDveiEIVDKLISVPYVEMTLKLMERFGVSVEHSDSwDRFFIKGGQKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 222 G--GGVYrVLPDRIETGTFLVAAAISGGKIVCRNAQPDTL--DAVLAKLREA-GADIETGEDWISL------DMHGKRPK 290
Cdd:PLN02338 241 KspGNAY-VEGDASSASYFLAGAAITGGTVTVEGCGTTSLqgDVKFAEVLEKmGAKVEWTENSVTVtgpprdAFGGKHLK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 291 AVTVRTAPHPafPTAMqaQFTLLNLVAEGTGVI--------TETifENRFMHVPELIRMGAHAEIESNTVICHGVEKLSG 362
Cdd:PLN02338 320 AIDVNMNKMP--DVAM--TLAVVALFADGPTAIrdvaswrvKET--ERMIAICTELRKLGATVEEGPDYCIITPPKKLKP 393
|
410 420
....*....|....*....|....*....
1Q3G_K 363 AQV-MATDLRASASLVLAGCIAEGTTVVD 390
Cdd:PLN02338 394 AEIdTYDDHRMAMAFSLAACGDVPVTIND 422
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
169-415 |
6.11e-06 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 48.22 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 169 IMSAAtLAEGTTIIENAAREPEIVDTANFLVALGAKIsgqGTDRITIEGVerlGGGVYRVLPDRIET---GT---FLVA- 241
Cdd:PRK02427 30 LLLAA-LAEGETTITNLLRSEDTLATLNALRALGVEI---EDDEVVVEGV---GGGGLKEPEDVLDCgnsGTtmrLLTGl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 242 AAISGGKIV--------CRnaqPdtLDAVLAKLREAGADIETGED-WISLDMHG-KRPKAVTVRtAPHP-AFPTAMqaqF 310
Cdd:PRK02427 103 LALQPGEVVltgdeslrKR---P--MGRLLDPLRQMGAKIEGRDEgYLPLTIRGgKKGGPIEYD-GPVSsQFVKSL---L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 311 TLLNLVAEGTGVITetifenrfmHVPEL---------IRM--GAHAEIESNTVICHGVEKLSGAQVM-ATDLR-----AS 373
Cdd:PRK02427 174 LLAPLFAEGDTETT---------VIEPLpsrphteitLRMlrAFGVEVENVEGWGYRRIVIKGGQRLrGQDITvpgdpSS 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
1Q3G_K 374 AS-LVLAGCIAEGTTVvdRIYHID----RGYERIEDKLRALGANIER 415
Cdd:PRK02427 245 AAfFLAAAAITGGSEV--TITNVGlnstQGGKAIIDVLEKMGADIEI 289
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
4-274 |
6.73e-06 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 48.45 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 4 FRVQGPTRLQGEVTISGAKNAA-LPILFAALlAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVE--R*GSVWIDASNVNNF 80
Cdd:PRK14806 304 YSVLPGGAVKGTIRVPGDKSIShRSIMLGSL-AEGVTEVEGFLEGEDALATLQAFRDMGVVIEgpHNGRVTIHGVGLHGL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 81 SAP----YdlVKTMRASIWALGPLVArfGQG-QVSLPGGCAIGARPVDLHIFGLEKLGAEIKL-EEGYVKASVNG--RLK 152
Cdd:PRK14806 383 KAPpgplY--MGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETgEEGRPPLSIRGgqRLK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 153 GAHIVMDKVSVGATVTIMSAATLAEGTTIIenaaREPEIV--DTANFLVALGAKISGQGtDRITIEGVERLGGGVYRVLP 230
Cdd:PRK14806 459 GIHYDLPMASAQVKSCLLLAGLYAEGETSV----TEPAPTrdHTERMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPA 533
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
1Q3G_K 231 DRIETGTFLVAAAISGG-KIVCRNAQPD-TLDAVLAKLREAGADIE 274
Cdd:PRK14806 534 DISSAAFFLVAASIAEGsELTLEHVGINpTRTGVIDILKLMGADIT 579
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
169-414 |
5.29e-03 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 39.21 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 169 IMSAAtLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLG-----GGVYRVlpdriETGT--FLVA 241
Cdd:PRK14806 329 IMLGS-LAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGPHNGRVTIHGVGLHGlkappGPLYMG-----NSGTsmRLLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 242 AAISGGKIvcrnaqPDTL--DAVLAK---------LREAGADIETGEDwisldmhGKRPKAVT---VRTAPHPAFPTAmQ 307
Cdd:PRK14806 403 GLLAAQSF------DSVLtgDASLSKrpmervakpLREMGAVIETGEE-------GRPPLSIRggqRLKGIHYDLPMA-S 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q3G_K 308 AQFT----LLNLVAEGTGVITETifENRFMHVPELIR-MGAHAEIESNTVICHGVEKLSGAQ-VMATDLRASASLVLAGC 381
Cdd:PRK14806 469 AQVKscllLAGLYAEGETSVTEP--APTRDHTERMLRgFGYPVKVEGNTISVEGGGKLTATDiEVPADISSAAFFLVAAS 546
|
250 260 270
....*....|....*....|....*....|...
1Q3G_K 382 IAEGTTVVDRIYHIDRGYERIEDKLRALGANIE 414
Cdd:PRK14806 547 IAEGSELTLEHVGINPTRTGVIDILKLMGADIT 579
|
|
| |
