|
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: 761.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIK 80
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPaGGLRGGHFF 160
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD-GRLKGAHIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGnRPKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDR 398
|
410
....*....|....*....
gi 15599646 401 GYECIEEKLQLLGAKIRRV 419
Cdd:PRK09369 399 GYERIEEKLRALGADIERV 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: 739.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIK 80
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKapAGGLRGGHFF 160
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEAR--AGRLKGARIY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:COG0766 159 LDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGnRPKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:COG0766 239 FLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:COG0766 318 EGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDR 397
|
410
....*....|....*....
gi 15599646 401 GYECIEEKLQLLGAKIRRV 419
Cdd:COG0766 398 GYENLEEKLRALGADIERV 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: 678.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 12 LDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIKTLVAPYELVKT 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 92 MRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKApAGGLRGGHFFFDTVSVTGTEN 171
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKA-AGRLKGARIYLDFPSVGATEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 172 LMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGTYLVAAAATGGR 251
Cdd:cd01555 160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 252 VKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFISMNAVAEGTGAVIETVF 331
Cdd:cd01555 240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 332 ENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDRGYECIEEKLQL 411
Cdd:cd01555 320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399
|
.
gi 15599646 412 L 412
Cdd:cd01555 400 L 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: 626.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKlNVEVDASSIK 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNN-TLEINTPNIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPaGGLRGGHFF 160
Cdd:TIGR01072 80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAK-GRLVGAHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:TIGR01072 159 LDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:TIGR01072 239 FLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:TIGR01072 319 EGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDR 398
|
410
....*....|....*...
gi 15599646 401 GYECIEEKLQLLGAKIRR 418
Cdd:TIGR01072 399 GYEDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-409 |
4.28e-150 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 431.72 E-value: 4.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 7 TGGNRLDGEIRISG-AKNSALPILAATLLAdTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEV-DASSIKTLVA 84
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVViVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 85 PYELVKTMRASILVLGPMLARFGEA--EVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPAGGLRGG--HFF 160
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQsgEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGgiHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDT-IVIEGVKRLGGARYDVLPDRIETG 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 240 TYLVAAAATGGRVKLKDTDPTIL---EAVLQKLEEAGAHISTG-SNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFIS 315
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEeDADIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 316 MNAVAEGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTA-IVTGVPKLKGAPVMAT-DLRASASLVIAGLVAEGDTLID 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 15599646 394 RIYHIDRGYECIEEKL 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: 761.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIK 80
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPaGGLRGGHFF 160
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKAD-GRLKGAHIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:PRK09369 160 LDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGnRPKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPG-RLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDR 398
|
410
....*....|....*....
gi 15599646 401 GYECIEEKLQLLGAKIRRV 419
Cdd:PRK09369 399 GYERIEEKLRALGADIERV 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: 739.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIK 80
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKapAGGLRGGHFF 160
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEAR--AGRLKGARIY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:COG0766 159 LDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGnRPKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:COG0766 239 FLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPG-RLKAVDIKTAPYPGFPTDLQAQFMALLTQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:COG0766 318 EGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDR 397
|
410
....*....|....*....
gi 15599646 401 GYECIEEKLQLLGAKIRRV 419
Cdd:COG0766 398 GYENLEEKLRALGADIERV 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: 678.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 12 LDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIKTLVAPYELVKT 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 92 MRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKApAGGLRGGHFFFDTVSVTGTEN 171
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKA-AGRLKGARIYLDFPSVGATEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 172 LMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGTYLVAAAATGGR 251
Cdd:cd01555 160 IMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 252 VKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFISMNAVAEGTGAVIETVF 331
Cdd:cd01555 240 ITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 332 ENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDRGYECIEEKLQL 411
Cdd:cd01555 320 ENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRA 399
|
.
gi 15599646 412 L 412
Cdd:cd01555 400 L 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: 626.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKlNVEVDASSIK 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNN-TLEINTPNIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPaGGLRGGHFF 160
Cdd:TIGR01072 80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAK-GRLVGAHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:TIGR01072 159 LDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:TIGR01072 239 FLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:TIGR01072 319 EGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDR 398
|
410
....*....|....*...
gi 15599646 401 GYECIEEKLQLLGAKIRR 418
Cdd:TIGR01072 399 GYEDLEEKLRALGAKIER 416
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 512.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKlNVEVDASSIK 80
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGD-TLEIDPTGIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 81 TLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKApaGGLRGGHFF 160
Cdd:PRK12830 80 SMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKA--DELKGAHIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGT 240
Cdd:PRK12830 158 LDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 241 YLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGNRpKAVNVRTAPYPAFPTDMQAQFISMNAVA 320
Cdd:PRK12830 238 YMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNL-KAVDIKTLPYPGFATDLQQPLTPLLLKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 321 EGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDR 400
Cdd:PRK12830 317 NGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDR 396
|
410
....*....|....*....
gi 15599646 401 GYECIEEKLQLLGAKIRRV 419
Cdd:PRK12830 397 GYSNIIEKLKALGADIWRE 415
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-409 |
4.28e-150 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 431.72 E-value: 4.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 7 TGGNRLDGEIRISG-AKNSALPILAATLLAdTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEV-DASSIKTLVA 84
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVViVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 85 PYELVKTMRASILVLGPMLARFGEA--EVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPAGGLRGG--HFF 160
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQsgEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGgiHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 161 FDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDT-IVIEGVKRLGGARYDVLPDRIETG 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 240 TYLVAAAATGGRVKLKDTDPTIL---EAVLQKLEEAGAHISTG-SNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFIS 315
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEeDADIVVGPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 316 MNAVAEGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTA-IVTGVPKLKGAPVMAT-DLRASASLVIAGLVAEGDTLID 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 15599646 394 RIYHIDRGYECIEEKL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-412 |
7.08e-112 |
|
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: 334.19 E-value: 7.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 12 LDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQpIIDEKLNVEVDASSIKTLVAP---YEL 88
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVE-IEDKDGVITIQGVGMAGLKAPqnaLNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 89 VKTMRASILVLGPMLARFGEaeVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPAGG-LRGGHFFFD-TVSV 166
Cdd:cd01554 80 GNSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGkNLGPIHYEDpIASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 167 TGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGTYLVAAA 246
Cdd:cd01554 158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 247 ATGGRVKLKDTDP-TILEAVLQKLEEAGAHISTGSNWIELDMkgNRPKAVNVRTAPYPaFPTDMQAQFISMNAVAEGTGA 325
Cdd:cd01554 238 IAPGRLVLQNVGInETRTGIIDVLRAMGAKIEIGEDTISVES--SDLKATEICGALIP-RLIDELPIIALLALQAQGTTV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 326 VIETVF------ENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMAT-DLRASASLVIAGLVAEGDTLIDRIYHI 398
Cdd:cd01554 315 IKDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAI 394
|
410
....*....|....
gi 15599646 399 DRGYECIEEKLQLL 412
Cdd:cd01554 395 NTSYPSFFDDLESL 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-399 |
8.25e-32 |
|
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: 125.20 E-value: 8.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAK---NSALpILAAtlLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDaS 77
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL-LLAA--LAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVT-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 78 SIKTLVAPYELVK------TMR--ASILVLGPMLARF-GEAevalpggcAIGSRPVDLHIRGLEAMGAQIE-VEGGYika 147
Cdd:COG0128 77 VGGGLKEPDAVLDcgnsgtTMRllTGLLALQPGEVVLtGDE--------SLRKRPMGRLLDPLRQLGARIEsRGGGY--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 148 kAP----AGGLRGGHFFFDTVS----VTGtenLMMAAALANGRTVLQNAAREPEV--VDLA-NCLNAMGANVQGAGSDTI 216
Cdd:COG0128 146 -LPltirGGPLKGGEYEIPGSAssqfKSA---LLLAGPLAEGGLEITVTGELESKpyRDHTeRMLRAFGVEVEVEGYRRF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 217 VIEGVKRLGGARYDVLPDRIETGTYLVAAAATGGRVKLKD--TDPTILE-AVLQKLEEAGAHISTGSNWIELdmKGNRPK 293
Cdd:COG0128 222 TVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGvgLNSTQGDtGILDILKEMGADIEIENDGITV--RGSPLK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 294 AVNVRTAPYP-AFPTdmqaqfIS-MNAVAEGTgavieTVFEN----RF--------MhVYEMNRMGAQILVEGNTAIVTG 359
Cdd:COG0128 300 GIDIDLSDIPdEAPT------LAvLAAFAEGT-----TRIRGaaelRVkesdriaaM-ATELRKLGADVEETEDGLIIEG 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15599646 360 VPKLKGAPV-------MATdlrasaSLVIAGLVAEGDTLIDRIYHID 399
Cdd:COG0128 368 GPKLKGAEVdsygdhrIAM------AFAVAGLRAEGPVTIDDAECVA 408
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-399 |
6.26e-26 |
|
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: 108.41 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 12 LDGEIRISGAK---NSALpILAAtlLADTPVTVCNLPHLHDITTMIELFGRMGVQpIIDEKLNVEVDASSIKTLVAPYEL 88
Cdd:cd01556 1 LSGEITVPGSKsisHRAL-LLAA--LAEGESRIENLLDSDDTLATLEALRALGAK-IEEEGGTVEIVGGGGLGLPPEAVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 89 V-----KTMRasiLVLGpmLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIE-VEGGYIKAKAPAGGLRGGHFFFD 162
Cdd:cd01556 77 DcgnsgTTMR---LLTG--LLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEgREGGGYPPLIGGGGLKGGEVEIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 163 -TVS---VTGtenLMMAAALANGRTVLQNAAREPEV-VDL-ANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDrI 236
Cdd:cd01556 152 gAVSsqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 237 ETGTY-LVAAAATGGRVKLK-----DTDPTILEAvlqkLEEAGAHIS-TGSNWIELDmKGNRPKAVNVRTAPYP-AFPTd 308
Cdd:cd01556 228 SSAAFfLAAAAITGSEIVIKnvglnSGDTGIIDV----LKEMGADIEiGNEDTVVVE-SGGKLKGIDIDGNDIPdEAPT- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 309 mqaqfIS-MNAVAEGTGaVIETVFENRF--------MHVyEMNRMGAQILVEGNTAIVTGVPKLKGAPVMAT--DLRASA 377
Cdd:cd01556 302 -----LAvLAAFAEGPT-RIRNAAELRVkesdriaaMAT-ELRKLGADVEETEDGLIIEGGPLKGAGVEVYTygDHRIAM 374
|
410 420
....*....|....*....|..
gi 15599646 378 SLVIAGLVAEGDTLIDRIYHID 399
Cdd:cd01556 375 SFAIAGLVAEGGVTIEDPECVA 396
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
233-412 |
5.37e-24 |
|
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: 98.89 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 233 PDRIETGTYLVAAAATGGRVKLK-----DTDPTILE---AVLQKLEEA-GAHI---STGSNWIELDMKGnrPKAVNVRTA 300
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTgirpdRAKPGLLRqhlTFLKALEKIcGATVeggELGSDRISFRPGT--VRGGDVRFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 301 PYPA-FPTDMQAQFISMNAVAEGTGAVIETVF----------ENRFMHVYEMNRMGAQILVE------------GNTAIV 357
Cdd:cd01553 86 IGSAgSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEETllrhgfypagggVVATEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15599646 358 TGVPKLKGApvmatDLRASASLVIAGlvaeGDTLIDRIYHIDRGYECIEEKLQLL 412
Cdd:cd01553 166 SPVEKLNTA-----QLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-415 |
1.60e-20 |
|
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: 92.72 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 14 GEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQpIIDEKLNVEVDASSIKTLVAPYELVK--- 90
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAK-IEDGGEVAVIEGVGGKEPQAELDLGNsgt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 91 TMRASILVLGpmLARFgeaEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGyiKAKAP---AGGLRGGHfffdtVSVT 167
Cdd:TIGR01356 80 TARLLTGVLA--LADG---EVVLTGDESLRKRPMGRLVDALRQLGAEISSLEG--GGSLPltiSGPLPGGI-----VYIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 168 GTEN------LMMAAALANG---RTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDrIET 238
Cdd:TIGR01356 148 GSASsqyksaLLLAAPALQAvgiTIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGD-YSS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 239 GTYLVAAAA-TGGRVKLKD---TDPTILEAVLQKLEEAGAHISTGSNWIELdmKGNRP-KAVNVRTAPYP-AFPTdmqaq 312
Cdd:TIGR01356 227 AAFFLAAAAiTGGRVTLENlgiNPTQGDKAIIIVLEEMGADIEVEEDDLIV--EGASGlKGIKIDMDDMIdELPT----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 313 FISMNAVAEGTgAVIETVFENRF--------MHVyEMNRMGAQILVEGNTAIVTGVPKLKGAPVMA-TDLRASASLVIAG 383
Cdd:TIGR01356 300 LAVLAAFAEGV-TRITGAEELRVkesdriaaIAE-ELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAG 377
|
410 420 430
....*....|....*....|....*....|..
gi 15599646 384 LVAEGDTLIDRIYHIDRGYECIEEKLQLLGAK 415
Cdd:TIGR01356 378 LVAEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-417 |
4.57e-20 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 91.74 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 1 MDKLIITGGNRLDGEIRISGAK---NSALpILAAtlLADTPVTVCNLPHLHDITTMIELFGRMGVQpiIDEKlNVEVDAS 77
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL-LLAA--LAEGETTITNLLRSEDTLATLNALRALGVE--IEDD-EVVVEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 78 SIKTLVAPYELVK------TMR--ASILVLGPMLARF-GEAevalpggcAIGSRPVDLHIRGLEAMGAQIEVEGGyikAK 148
Cdd:PRK02427 76 GGGGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVLtGDE--------SLRKRPMGRLLDPLRQMGAKIEGRDE---GY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 149 AP---AGGLRGGHFFFDT-VS---VTGtenLMMAAAL-ANGRTVLQnaAREPEV----VDL-ANCLNAMGANVQ---GAG 212
Cdd:PRK02427 145 LPltiRGGKKGGPIEYDGpVSsqfVKS---LLLLAPLfAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 213 SDTIVIEGVKRLGGARYDVLPDrIETGTY-LVAAAATGG-RVKLKD-------TDPTILEAvlqkLEEAGAHISTGSNWI 283
Cdd:PRK02427 220 YRRIVIKGGQRLRGQDITVPGD-PSSAAFfLAAAAITGGsEVTITNvglnstqGGKAIIDV----LEKMGADIEIENERE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 284 ELDMKGNrpkaVNVRTAPYPAFPTDMqAQFI-------SMNAVAEGTgavieTVFEN----RF--------MHVyEMNRM 344
Cdd:PRK02427 295 GGEPVGD----IRVRSSELKGIDIDI-PDIIdeaptlaVLAAFAEGT-----TVIRNaeelRVketdriaaMAT-ELRKL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 345 GAQILVEGNTAIVTGVPKlkgAPVMAT--DLRASASLVIAGLVAEGDTLIDRIyhidrgyECI-------EEKLQLLGAK 415
Cdd:PRK02427 364 GAEVEETEDGLIITGGPL---AGVVDSygDHRIAMAFAIAGLAAEGPVTIDDP-------ECVaksfpdfFEDLASLGAN 433
|
..
gi 15599646 416 IR 417
Cdd:PRK02427 434 IE 435
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
174-417 |
1.46e-09 |
|
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: 59.49 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 174 MAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGsDTIVIEGVKRLGGARYDVLpDRIETGT---YLVAAAATGG 250
Cdd:cd01556 19 LLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG-GTVEIVGGGGLGLPPEAVL-DCGNSGTtmrLLTGLLALQG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 251 RVKLKDTDPTILE----AVLQKLEEAGAHIstgsnwielDMKGNRPKAVNVRTAPYPAFPTDMQ----AQFIS---MNA- 318
Cdd:cd01556 97 GDSVLTGDESLRKrpmgRLVDALRQLGAEI---------EGREGGGYPPLIGGGGLKGGEVEIPgavsSQFKSallLAAp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 319 VAEGTGAVIETVFEN---RFMHVYEMNRMGAQILVEGNTAI-VTGVPKLKGAPV-MATDLRASASLVIAGLVAEGDTLId 393
Cdd:cd01556 168 LAEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDGYRTItVKGGQKYKGPEYtVEGDASSAAFFLAAAAITGSEIVI- 246
|
250 260
....*....|....*....|....
gi 15599646 394 RIYHIDRGYECIEEKLQLLGAKIR 417
Cdd:cd01556 247 KNVGLNSGDTGIIDVLKEMGADIE 270
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
174-421 |
1.00e-07 |
|
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: 53.82 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 174 MAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGsDTIVIEGVkrlGGARYDVLPDRIETGT----YLVAAAATG 249
Cdd:TIGR01356 17 ILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGG-EVAVIEGV---GGKEPQAELDLGNSGTtarlLTGVLALAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 250 GRVKLkDTDPTI----LEAVLQKLEEAGAHIS--TGSNWIELDMKGNRPKAVnVRTAPypafptDMQAQFIS--MNAVAE 321
Cdd:TIGR01356 93 GEVVL-TGDESLrkrpMGRLVDALRQLGAEISslEGGGSLPLTISGPLPGGI-VYISG------SASSQYKSalLLAAPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599646 322 GTGAVIETVFENRFMHVY------EMNRMGAQILVE-GNTAIVTGVPKLKGAPV-MATDLRASASLVIAGLVAEGDTLID 393
Cdd:TIGR01356 165 LQAVGITIVGEPLKSRPYieitldLLGSFGVEVERSdGRKIVVPGGQKYGPQGYdVPGDYSSAAFFLAAAAITGGRVTLE 244
|
250 260
....*....|....*....|....*....
gi 15599646 394 RIYHID-RGYECIEEKLQLLGAKIRRVPG 421
Cdd:TIGR01356 245 NLGINPtQGDKAIIIVLEEMGADIEVEED 273
|
|
| |
