|
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: 738.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVD 80
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARAT-RLKGASIRT 159
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAHIVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 160 DMVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTF 239
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 240 LCAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHGRPRAVGARTHEYPGFATDMQAQLMALDTVADG 319
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 320 TAVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGY 399
Cdd:PRK09369 321 TSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGY 400
|
410
....*....|....*..
gi 499229682 400 DRMEVKLRALGASIQRV 416
Cdd:PRK09369 401 ERIEEKLRALGADIERV 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: 726.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVD 80
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARATRLKGASIRTD 160
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 161 MVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTFL 240
Cdd:COG0766 161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 241 CAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHGRPRAVGARTHEYPGFATDMQAQLMALDTVADGT 320
Cdd:COG0766 241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 321 AVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGYD 400
Cdd:COG0766 321 SVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYE 400
|
410
....*....|....*.
gi 499229682 401 RMEVKLRALGASIQRV 416
Cdd:COG0766 401 NLEEKLRALGADIERV 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: 630.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 12 LRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVDNLEAPYELVKT 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 92 MRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVA-RATRLKGASIRTDMVTVTGTENL 170
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAkAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 171 LMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTFLCAVGAAGGDI 250
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 251 TLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHG-RPRAVGARTHEYPGFATDMQAQLMALDTVADGTAVIVENIFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 330 NRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGYDRMEVKLRAL 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: 586.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDgTVTLQADQVD 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNN-TLEINTPNIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARA-TRLKGASIRT 159
Cdd:TIGR01072 80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAkGRLVGAHIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 160 DMVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTF 239
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 240 LCAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHG-RPRAVGARTHEYPGFATDMQAQLMALDTVAD 318
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 319 GTAVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRG 398
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
|
410
....*....|....*..
gi 499229682 399 YDRMEVKLRALGASIQR 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
4.31e-116 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 345.44 E-value: 4.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 7 TGGSPLRGEVTVSG-AKNAALPILCASLLtAEPLVLGNVPQLNDTSTTLRLLGRMGVRAER-AGDGTVTLQADQVDNLEA 84
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALA-AGESTITNLLDSDDTLTMLEALRALGAEIIKlDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 85 PYELVKTMRASILVLGPLLARFGQAR--VSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVA----RATRLKGASIR 158
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 159 TDMVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTD-RIVVDGVARLHGARHDVIADRIEAG 237
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 238 TFLCAVGAAGGDITLRGAAPDTM---GATLDKLVEAGLTIETGPD-WIRGAMHG-RPRAVGARTHEYPGFATDMQAQLMA 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 313 LDTVADGTAVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVA-RLSGATVMAT-DLRASASLVIAGLAAEGETLVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 499229682 391 RIYHLDRGYDRMEVKL 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: 738.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVD 80
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGTVTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARAT-RLKGASIRT 159
Cdd:PRK09369 81 NTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADgRLKGAHIVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 160 DMVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTF 239
Cdd:PRK09369 161 DFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 240 LCAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHGRPRAVGARTHEYPGFATDMQAQLMALDTVADG 319
Cdd:PRK09369 241 LVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 320 TAVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGY 399
Cdd:PRK09369 321 TSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGY 400
|
410
....*....|....*..
gi 499229682 400 DRMEVKLRALGASIQRV 416
Cdd:PRK09369 401 ERIEEKLRALGADIERV 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: 726.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVD 80
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGTLTIDASNIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARATRLKGASIRTD 160
Cdd:COG0766 81 STEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 161 MVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTFL 240
Cdd:COG0766 161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 241 CAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHGRPRAVGARTHEYPGFATDMQAQLMALDTVADGT 320
Cdd:COG0766 241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 321 AVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGYD 400
Cdd:COG0766 321 SVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYE 400
|
410
....*....|....*.
gi 499229682 401 RMEVKLRALGASIQRV 416
Cdd:COG0766 401 NLEEKLRALGADIERV 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: 630.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 12 LRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVDNLEAPYELVKT 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGENTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 92 MRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVA-RATRLKGASIRTDMVTVTGTENL 170
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAkAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 171 LMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTFLCAVGAAGGDI 250
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 251 TLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHG-RPRAVGARTHEYPGFATDMQAQLMALDTVADGTAVIVENIFE 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 330 NRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGYDRMEVKLRAL 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: 586.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDgTVTLQADQVD 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNN-TLEINTPNIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARA-TRLKGASIRT 159
Cdd:TIGR01072 80 STEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAkGRLVGAHIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 160 DMVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTF 239
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 240 LCAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHG-RPRAVGARTHEYPGFATDMQAQLMALDTVAD 318
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 319 GTAVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRG 398
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRG 399
|
410
....*....|....*..
gi 499229682 399 YDRMEVKLRALGASIQR 415
Cdd:TIGR01072 400 YEDLEEKLRALGAKIER 416
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-417 |
1.20e-168 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 478.97 E-value: 1.20e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDgTVTLQADQVD 80
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGD-TLEIDPTGIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGQARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVARATRLKGASIRTD 160
Cdd:PRK12830 80 SMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHIYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 161 MVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTFL 240
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 241 CAVGAAGGDITLRGAAPDTMGATLDKLVEAGLTIETGPDWIRGAMHGRPRAVGARTHEYPGFATDMQAQLMALDTVADGT 320
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 321 AVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMATDLRASASLVIAGLAAEGETLVDRIYHLDRGYD 400
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYS 399
|
410
....*....|....*..
gi 499229682 401 RMEVKLRALGASIQRVT 417
Cdd:PRK12830 400 NIIEKLKALGADIWREE 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-406 |
4.31e-116 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 345.44 E-value: 4.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 7 TGGSPLRGEVTVSG-AKNAALPILCASLLtAEPLVLGNVPQLNDTSTTLRLLGRMGVRAER-AGDGTVTLQADQVDNLEA 84
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALA-AGESTITNLLDSDDTLTMLEALRALGAEIIKlDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 85 PYELVKTMRASILVLGPLLARFGQAR--VSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVA----RATRLKGASIR 158
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 159 TDMVTVTGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTD-RIVVDGVARLHGARHDVIADRIEAG 237
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTElSITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 238 TFLCAVGAAGGDITLRGAAPDTM---GATLDKLVEAGLTIETGPD-WIRGAMHG-RPRAVGARTHEYPGFATDMQAQLMA 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDaDIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 313 LDTVADGTAVIVENIFENRYMHVQELCRLGADIDIDGHTAVVRGVA-RLSGATVMAT-DLRASASLVIAGLAAEGETLVD 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVkELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 499229682 391 RIYHLDRGYDRMEVKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-409 |
5.85e-98 |
|
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: 298.75 E-value: 5.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 12 LRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAgDGTVTLQADQVDNLEAP---YEL 88
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDK-DGVITIQGVGMAGLKAPqnaLNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 89 VKTMRASILVLGPLLARFGQarVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVA---RATRLKGASIRTD-MVTV 164
Cdd:cd01554 80 GNSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPpllKGGKNLGPIHYEDpIASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 165 TGTENLLMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADRIEAGTFLCAVG 244
Cdd:cd01554 158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 245 AAGGDITLRGAAPDT-MGATLDKLVEAGLTIETGPDWIRGAMHgRPRAVGARTHEYPgFATDMQAQLMALDTVADGTAVI 323
Cdd:cd01554 238 IAPGRLVLQNVGINEtRTGIIDVLRAMGAKIEIGEDTISVESS-DLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 324 VENIF------ENRYMHVQELCRLGADIDIDGHTAVVRGVARLSGATVMAT-DLRASASLVIAGLAAEGETLVDRIYHLD 396
Cdd:cd01554 316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
|
410
....*....|...
gi 499229682 397 RGYDRMEVKLRAL 409
Cdd:cd01554 396 TSYPSFFDDLESL 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-390 |
3.70e-27 |
|
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: 112.10 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAK---NAALpiLCASLltAE-PLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQA 76
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEgESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 77 dQVDNLEAPYELVK------TMR--ASILVLGPLLARF-GQARvslpggcaIGQRPVDQHIKGLAALGAEIE-IEHGF-- 144
Cdd:COG0128 77 -VGGGLKEPDAVLDcgnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQLGARIEsRGGGYlp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 145 VVARATRLKGASIRTDMVT----VTGtenLLMAAVLAEGQTVLENAAREPEV--VDLAE-LLIKMGARIQGHGTDRIVVD 217
Cdd:COG0128 148 LTIRGGPLKGGEYEIPGSAssqfKSA---LLLAGPLAEGGLEITVTGELESKpyRDHTErMLRAFGVEVEVEGYRRFTVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 218 GVARLHGARHDVIADRIEAGTFLCAVGAAGGDITLRGA-APDTMGAT--LDKLVEAGLTIETGPDWIRgAMHGRPRAV-- 292
Cdd:COG0128 225 GGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVgLNSTQGDTgiLDILKEMGADIEIENDGIT-VRGSPLKGIdi 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 293 -GARTH-EYPGFAtdmqaqlmALDTVADGTAVIvENIFENRY--------MhVQELCRLGADIDIDGHTAVVRGVARLSG 362
Cdd:COG0128 304 dLSDIPdEAPTLA--------VLAAFAEGTTRI-RGAAELRVkesdriaaM-ATELRKLGADVEETEDGLIIEGGPKLKG 373
|
410 420 430
....*....|....*....|....*....|....*
gi 499229682 363 ATV-------MATdlrasaSLVIAGLAAEGETLVD 390
Cdd:COG0128 374 AEVdsygdhrIAM------AFAVAGLRAEGPVTID 402
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
232-409 |
1.45e-15 |
|
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: 75.01 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 232 DRIEAGTFLCAVGAAGGDITLRGAAPDTMG--------ATLDKLVEA-GLTIETGP---DWIRGAMHGrPRAVGART-HE 298
Cdd:cd01553 9 GGQILRSFLVLAAISGGPITVTGIRPDRAKpgllrqhlTFLKALEKIcGATVEGGElgsDRISFRPGT-VRGGDVRFaIG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 299 YPGFATDMQAQLMALDTVADGTAVIVENIF----------ENRYMHVQELCRLGADIDI------------DGHTAVVRG 356
Cdd:cd01553 88 SAGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGAHQEEtllrhgfypaggGVVATEVSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499229682 357 VARLSGAtvmatDLRASASLVIAGlaaeGETLVDRIYHLDRGYDRMEVKLRAL 409
Cdd:cd01553 168 VEKLNTA-----QLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-394 |
1.66e-13 |
|
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: 71.82 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 12 LRGEVTVSGAK---NAALpiLCASLlTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERaGDGTVTLQADQVDNLEAPYEL 88
Cdd:cd01556 1 LSGEITVPGSKsisHRAL--LLAAL-AEGESRIENLLDSDDTLATLEALRALGAKIEE-EGGTVEIVGGGGLGLPPEAVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 89 V-----KTMRasiLVLGPLLARFGqaRVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFvvARATRLKGASIRTDMVT 163
Cdd:cd01556 77 DcgnsgTTMR---LLTGLLALQGG--DSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGG--GYPPLIGGGGLKGGEVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 164 VTGTEN------LLMAAVLAEGQTVLENAAREPEV-VDLAE-LLIKMGARIQGHGTDRIVVDGVARLHGARHDVIADrIE 235
Cdd:cd01556 150 IPGAVSsqfksaLLLAAPLAEGPTTIIIGELESKPyIDHTErMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-AS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 236 AGTFLCAVGA-AGGDITLRG---AAPDT--------MGATLDKLVEAGLTIEtGPDWIRG---AMHGRPRAVgartheyP 300
Cdd:cd01556 229 SAAFFLAAAAiTGSEIVIKNvglNSGDTgiidvlkeMGADIEIGNEDTVVVE-SGGKLKGidiDGNDIPDEA-------P 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 301 GFAtdmqaqlmALDTVADGTAVIvENIFENRY--------MhVQELCRLGADID--IDGhtAVVRGVARLSGATVMAT-- 368
Cdd:cd01556 301 TLA--------VLAAFAEGPTRI-RNAAELRVkesdriaaM-ATELRKLGADVEetEDG--LIIEGGPLKGAGVEVYTyg 368
|
410 420
....*....|....*....|....*.
gi 499229682 369 DLRASASLVIAGLAAEGETLVDRIYH 394
Cdd:cd01556 369 DHRIAMSFAIAGLVAEGGVTIEDPEC 394
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
14-411 |
7.55e-13 |
|
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: 69.61 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 14 GEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDgTVTLQAdqvDNLEAPYELVKtMR 93
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGE-VAVIEG---VGGKEPQAELD-LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 94 ASILVLGPLLARFGQAR--VSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHGFVVArATRLKGaSIRTDMVTVTGTEN-- 169
Cdd:TIGR01356 76 NSGTTARLLTGVLALADgeVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSL-PLTISG-PLPGGIVYISGSASsq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 170 ----LLMAAVLAEGQTVLENAAREPEvVDLAELLIKM----GARIQGHGTDRIVVDGVARLHGARHDVIADrIEAGTFLC 241
Cdd:TIGR01356 154 yksaLLLAAPALQAVGITIVGEPLKS-RPYIEITLDLlgsfGVEVERSDGRKIVVPGGQKYGPQGYDVPGD-YSSAAFFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 242 AVGA-AGGDITLRG-AAPDTMG--ATLDKLVEAGLTIETGPDWI--RGAMHGRPRAVGARTheypgfATDMQAQLMALDT 315
Cdd:TIGR01356 232 AAAAiTGGRVTLENlGINPTQGdkAIIIVLEEMGADIEVEEDDLivEGASGLKGIKIDMDD------MIDELPTLAVLAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 316 VADGTAVIvENIFENRYMH-------VQELCRLGADIDIDGHTAVVRGVARLSGATVMA-TDLRASASLVIAGLAAEGET 387
Cdd:TIGR01356 306 FAEGVTRI-TGAEELRVKEsdriaaiAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTfGDHRIAMAFAVAGLVAEGEV 384
|
410 420
....*....|....*....|....
gi 499229682 388 LVDRIYHLDRGYDRMEVKLRALGA 411
Cdd:TIGR01356 385 LIDDPECVAKSFPSFFDVLERLGA 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
4-256 |
4.95e-12 |
|
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: 67.04 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 4 LRITGGSPLRGEVTVSGAKNA----ALpiLCASLLTAEPLVLGNVPQLNDTST---TLRLLGRMGVRAERAGDGTVTLQA 76
Cdd:COG0128 148 LTIRGGPLKGGEYEIPGSASSqfksAL--LLAGPLAEGGLEITVTGELESKPYrdhTERMLRAFGVEVEVEGYRRFTVPG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 77 DQvdnleaPYELvKTMR-------ASILVLGPLLArfgQARVSLPGgcaIGQRPVdQHIKG----LAALGAEIEIEHGFV 145
Cdd:COG0128 226 GQ------RYRP-GDYTvpgdissAAFFLAAAAIT---GSEVTVEG---VGLNST-QGDTGildiLKEMGADIEIENDGI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 146 VARATRLKGASIR----TDMVTVtgtenLLMAAVLAEGQTVLENAA--REPE---VVDLAELLIKMGARIQGHGtDRIVV 216
Cdd:COG0128 292 TVRGSPLKGIDIDlsdiPDEAPT-----LAVLAAFAEGTTRIRGAAelRVKEsdrIAAMATELRKLGADVEETE-DGLII 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499229682 217 DGVARLHGAR----HDviaDRIeAGTFLCAVGAAGGDITLRGAA 256
Cdd:COG0128 366 EGGPKLKGAEvdsyGD---HRI-AMAFAVAGLRAEGPVTIDDAE 405
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-392 |
7.79e-11 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 63.62 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAK---NAALpiLCASLltAE-PLVLGNVPQLNDTSTTLRLLGRMGVRAEragDGTVTLQA 76
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKsisHRAL--LLAAL--AEgETTITNLLRSEDTLATLNALRALGVEIE---DDEVVVEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 77 DQVDNLEAPYELVK------TMR--ASILVLGPLLARF-GQARvslpggcaIGQRPVDQHIKGLAALGAEIEIEHG---- 143
Cdd:PRK02427 75 VGGGGLKEPEDVLDcgnsgtTMRllTGLLALQPGEVVLtGDES--------LRKRPMGRLLDPLRQMGAKIEGRDEgylp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 144 FVVARATRLKGASIRTDMVT--VTGtenLLM-AAVLAEGQTVLEnaAREPEV----VDL-AELLIKMGARIQ---GHGTD 212
Cdd:PRK02427 147 LTIRGGKKGGPIEYDGPVSSqfVKS---LLLlAPLFAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWGYR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 213 RIVVDGVARLHGARHDVIADRIEAGTFLCAVGAAGG-DITLRGAAPDTM---GATLDKLVEAGLTIETGPDWIRGAMHGR 288
Cdd:PRK02427 222 RIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTqggKAIIDVLEKMGADIEIENEREGGEPVGD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 289 PRAVGARTHeypGFATDMQAQ------LMALDTVADGTAVIvENIFENRY--------MhVQELCRLGADIDIDGHTAVV 354
Cdd:PRK02427 302 IRVRSSELK---GIDIDIPDIideaptLAVLAAFAEGTTVI-RNAEELRVketdriaaM-ATELRKLGAEVEETEDGLII 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 499229682 355 RGVARlsGATV-------MATdlrasaSLVIAGLAAEGETLVDRI 392
Cdd:PRK02427 377 TGGPL--AGVVdsygdhrIAM------AFAIAGLAAEGPVTIDDP 413
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
171-415 |
3.70e-06 |
|
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: 48.93 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 171 LMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGARHDVIaDRIEAGT---FLCAVGA-A 246
Cdd:COG0128 29 LLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGVGGGLKEPDAVL-DCGNSGTtmrLLTGLLAlQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 247 GGDITLRGAA-----PdtMGATLDKLVEAGLTIEtgpdwirGAMHGRP----RAVGARTHEY--PGFATdmqAQ-----L 310
Cdd:COG0128 108 PGEVVLTGDEslrkrP--MGRLLDPLRQLGARIE-------SRGGGYLpltiRGGPLKGGEYeiPGSAS---SQfksalL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 311 MALDTVADGTAVIVENIFEN---RYMHVQELCRLGADIDIDG-HTAVVRGVARLSGATVM-ATDLRASASLVIAGLAAEG 385
Cdd:COG0128 176 LAGPLAEGGLEITVTGELESkpyRDHTERMLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTvPGDISSAAFFLAAAAITGS 255
|
250 260 270
....*....|....*....|....*....|....
gi 499229682 386 ETLVDRI----YHLDRGYdrMEVkLRALGASIQR 415
Cdd:COG0128 256 EVTVEGVglnsTQGDTGI--LDI-LKEMGADIEI 286
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
171-414 |
4.15e-06 |
|
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: 48.71 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 171 LMAAVLAEGQTVLENAAREPEVVDLAELLIKMGARIQGHGtDRIVVDGVARLHGARHDVIaDRIEAGT---FLCAV-GAA 246
Cdd:cd01556 18 LLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG-GTVEIVGGGGLGLPPEAVL-DCGNSGTtmrLLTGLlALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 247 GGDITLRGAA-----PdtMGATLDKLVEAGLTIEtGPDWIRGAMHGRPRAVGARTHEYPG-----FATdmqAQLMALdTV 316
Cdd:cd01556 96 GGDSVLTGDEslrkrP--MGRLVDALRQLGAEIE-GREGGGYPPLIGGGGLKGGEVEIPGavssqFKS---ALLLAA-PL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 317 ADGTAVIVENIFEN---RYMHVQELCRLGADIDIDGHTA-VVRGVARLSGA--TVMAtDLRASASLVIAGLAAEGETlvd 390
Cdd:cd01556 169 AEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDGYRTiTVKGGQKYKGPeyTVEG-DASSAAFFLAAAAITGSEI--- 244
|
250 260
....*....|....*....|....*.
gi 499229682 391 RIYHLDRGYDRMEVK--LRALGASIQ 414
Cdd:cd01556 245 VIKNVGLNSGDTGIIdvLKEMGADIE 270
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
5-253 |
9.00e-06 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 48.07 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 5 RITGGSPLRGEVTVSGAKNAA-LPILCASLLTAEPLVLGnVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVDNLE 83
Cdd:PRK14806 305 SVLPGGAVKGTIRVPGDKSIShRSIMLGSLAEGVTEVEG-FLEGEDALATLQAFRDMGVVIEGPHNGRVTIHGVGLHGLK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 84 AP----YelVKTMRASILVLGPLLArfGQA-RVSLPGGCAIGQRPVDQHIKGLAALGAEIEIEHG----FVVARATRLKG 154
Cdd:PRK14806 384 APpgplY--MGNSGTSMRLLSGLLA--AQSfDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEgrppLSIRGGQRLKG 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 155 ASIRTDMVTVTGTENLLMAAVLAEGQTvlenAAREPEVV-DLAE-LLIKMGARIQGHGtDRIVVDGVARLHGARHDVIAD 232
Cdd:PRK14806 460 IHYDLPMASAQVKSCLLLAGLYAEGET----SVTEPAPTrDHTErMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPAD 534
|
250 260
....*....|....*....|..
gi 499229682 233 RIEAGTFLCAVG-AAGGDITLR 253
Cdd:PRK14806 535 ISSAAFFLVAASiAEGSELTLE 556
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-361 |
2.77e-05 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 46.24 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 1 MDKLRITGGSPLRGEVTVSGAKNAALPILCASLLTAEPLVLGNVPQLNDTSTTLRLLGRMGVRAERAGDGTVTLQADQVD 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGTRGAF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 81 NLEAPYELVKTMRASILVLGPLLARFGqARVSLPGGCAIGQRPVDQHIKGLAALGAEIEIE--HGFvvaRATRLKGASIR 158
Cdd:PRK11861 320 TAKTADLFLGNAGTAVRPLTAALAVNG-GEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEgnEGF---PPLRIRPATIS 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 159 TDM-------VTVTGTENLLMAAVLA---EGQTVLE---NAAREPEVVDLAELLIKMGARIQGHGTDRIVVDGVARLHGA 225
Cdd:PRK11861 396 VDApirvrgdVSSQFLTALLMTLPLVkakDGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSP 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499229682 226 RHDVI-ADRIEAGTFLCAVGAAGGDITLRGAAPDTMGATL---DKLVEAGLTIETGPDWIR----GAMHGRPRAVGARTH 297
Cdd:PRK11861 476 GTIMVeGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVgfaNALMQMGANVTMGDDWIEvrgiGHDHGRLAPIDMDFN 555
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499229682 298 EYPGFAtdMQAQLMALdtVADGTAVIvENIFENRYMHVQ-------ELCRLGADIDIDGHTAVVRGVARLS 361
Cdd:PRK11861 556 LIPDAA--MTIAVAAL--FADGPSTL-RNIGSWRVKETDriaamatELRKVGATVEEGADYLVVTPPAQLT 621
|
|
| |
