|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
3-415 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 754.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTDMISM 82
Cdd:PRK12830 2 EKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 83 PLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADELIGARIYLDVV 162
Cdd:PRK12830 82 PLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHIYLDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 163 SVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVL 242
Cdd:PRK12830 162 SVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYMIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 243 AAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGSSV 322
Cdd:PRK12830 242 AAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGRSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 323 VTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSKI 402
Cdd:PRK12830 322 VTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYSNI 401
|
410
....*....|...
gi 694157475 403 IEKLAAIGADITR 415
Cdd:PRK12830 402 IEKLKALGADIWR 414
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
3-415 |
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: 656.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYD-NKTAVIDPTDMIS 81
Cdd:COG0766 2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNINS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 82 MPLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADELIGARIYLDV 161
Cdd:COG0766 82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 162 VSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMV 241
Cdd:COG0766 162 PSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 242 LAAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGSS 321
Cdd:COG0766 242 AAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGTS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 322 VVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSK 401
Cdd:COG0766 322 VITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYEN 401
|
410
....*....|....
gi 694157475 402 IIEKLAAIGADITR 415
Cdd:COG0766 402 LEEKLRALGADIER 415
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
13-409 |
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: 585.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 13 LAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNK-TAVIDPTDMISMPLPTGNVKK 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 92 LRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYL-RADELIGARIYLDVVSVGATINI 170
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAkAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 171 MLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVLAAASGKGV 250
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 251 RIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFV-GEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGSSVVTDTIYP 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 330 SRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSKIIEKLAAI 409
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
3-415 |
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: 563.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTDMISM 82
Cdd:TIGR01072 2 DKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 83 PLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADE-LIGARIYLDV 161
Cdd:TIGR01072 82 EAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGrLVGAHIVLDK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 162 VSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMV 241
Cdd:TIGR01072 162 VSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 242 LAAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAI-FVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGS 320
Cdd:TIGR01072 242 AAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIrVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 321 SVVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYS 400
Cdd:TIGR01072 322 SVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGYE 401
|
410
....*....|....*
gi 694157475 401 KIIEKLAAIGADITR 415
Cdd:TIGR01072 402 DLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
8-406 |
7.62e-100 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 303.84 E-value: 7.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 8 RGGKKLAGTMQVDG-AKNSAVALIPAAiLAESEVVLEGLPDISDVYTLYDILEELGGNVR--YDNKTAVIDPTDMISMPL 84
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAA-LAAGESTITNLLDSDDTLTMLEALRALGAEIIklDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 85 PTGNVKKLRASYYLMGAMLGRFKKAV--VGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYL----RADELIGARIY 158
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 159 LDVVSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDT-IRITGVEHLHGCHHTIIPDRIEAG 237
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 238 TFMVLAAASGKGVRIENVIPTHLEG---IIAKLTEMGVPMDIEEDAIFV--GEVEKVKKIDIKTYAYPGFPTDLQQPLTA 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLQGdeaLLEILEKMGAEITQEEDADIVvgPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 313 LLTRAEGSSVVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAK-LQGSKVTAT-DLRAGAALVIAGLLAEGQTEIH 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 694157475 391 GIEHIERGYSKIIEKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
3-415 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 754.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTDMISM 82
Cdd:PRK12830 2 EKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 83 PLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADELIGARIYLDVV 162
Cdd:PRK12830 82 PLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKADELKGAHIYLDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 163 SVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVL 242
Cdd:PRK12830 162 SVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYMIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 243 AAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGSSV 322
Cdd:PRK12830 242 AAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGRSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 323 VTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSKI 402
Cdd:PRK12830 322 VTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRGYSNI 401
|
410
....*....|...
gi 694157475 403 IEKLAAIGADITR 415
Cdd:PRK12830 402 IEKLKALGADIWR 414
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
3-415 |
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: 656.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYD-NKTAVIDPTDMIS 81
Cdd:COG0766 2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKVERDdGGTLTIDASNINS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 82 MPLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADELIGARIYLDV 161
Cdd:COG0766 82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARAGRLKGARIYLDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 162 VSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMV 241
Cdd:COG0766 162 PSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 242 LAAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGSS 321
Cdd:COG0766 242 AAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGTS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 322 VVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSK 401
Cdd:COG0766 322 VITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRGYEN 401
|
410
....*....|....
gi 694157475 402 IIEKLAAIGADITR 415
Cdd:COG0766 402 LEEKLRALGADIER 415
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
3-415 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 612.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNK-TAVIDPTDMIS 81
Cdd:PRK09369 2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 82 MPLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADE-LIGARIYLD 160
Cdd:PRK09369 82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGrLKGAHIVLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 161 VVSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFM 240
Cdd:PRK09369 162 FPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAGTFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 241 VLAAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGS 320
Cdd:PRK09369 242 VAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQAEGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 321 SVVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYS 400
Cdd:PRK09369 322 SVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHLDRGYE 401
|
410
....*....|....*
gi 694157475 401 KIIEKLAAIGADITR 415
Cdd:PRK09369 402 RIEEKLRALGADIER 416
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
13-409 |
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: 585.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 13 LAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNK-TAVIDPTDMISMPLPTGNVKK 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 92 LRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYL-RADELIGARIYLDVVSVGATINI 170
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAkAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 171 MLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVLAAASGKGV 250
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 251 RIENVIPTHLEGIIAKLTEMGVPMDIEEDAIFV-GEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGSSVVTDTIYP 329
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVdGDGGRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 330 SRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSKIIEKLAAI 409
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLRAL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
3-415 |
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: 563.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTDMISM 82
Cdd:TIGR01072 2 DKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 83 PLPTGNVKKLRASYYLMGAMLGRFKKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYLRADE-LIGARIYLDV 161
Cdd:TIGR01072 82 EAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGrLVGAHIVLDK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 162 VSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMV 241
Cdd:TIGR01072 162 VSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTFLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 242 LAAASGKGVRIENVIPTHLEGIIAKLTEMGVPMDIEEDAI-FVGEVEKVKKIDIKTYAYPGFPTDLQQPLTALLTRAEGS 320
Cdd:TIGR01072 242 AAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIrVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAEGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 321 SVVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYS 400
Cdd:TIGR01072 322 SVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLDRGYE 401
|
410
....*....|....*
gi 694157475 401 KIIEKLAAIGADITR 415
Cdd:TIGR01072 402 DLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
8-406 |
7.62e-100 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 303.84 E-value: 7.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 8 RGGKKLAGTMQVDG-AKNSAVALIPAAiLAESEVVLEGLPDISDVYTLYDILEELGGNVR--YDNKTAVIDPTDMISMPL 84
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAA-LAAGESTITNLLDSDDTLTMLEALRALGAEIIklDDEKSVVIVEGLGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 85 PTGNVKKLRASYYLMGAMLGRFKKAV--VGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYL----RADELIGARIY 158
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAplkvRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 159 LDVVSVGATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDT-IRITGVEHLHGCHHTIIPDRIEAG 237
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 238 TFMVLAAASGKGVRIENVIPTHLEG---IIAKLTEMGVPMDIEEDAIFV--GEVEKVKKIDIKTYAYPGFPTDLQQPLTA 312
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLQGdeaLLEILEKMGAEITQEEDADIVvgPPGLRGKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 313 LLTRAEGSSVVTDTIYPSRFKHIAELERMGGKFKLEGRSAVINGPAK-LQGSKVTAT-DLRAGAALVIAGLLAEGQTEIH 390
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 694157475 391 GIEHIERGYSKIIEKL 406
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
13-409 |
1.71e-73 |
|
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: 235.58 E-value: 1.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 13 LAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTDM---ISMPLPTGNV 89
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMaglKAPQNALNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 90 KKLRASYYLMGAMLGRfkKAVVGLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIY--LRAD-ELIGARIYLD-VVSVG 165
Cdd:cd01554 81 NSGTAIRLISGVLAGA--DFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLppLLKGgKNLGPIHYEDpIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 166 ATINIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVLAAA 245
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 246 SGKGVRIENVIP-THLEGIIAKLTEMGVPMDIEEDAIFVgEVEKVKKIDIKTYAYPgFPTDLQQPLTALLTRAEGSSVVT 324
Cdd:cd01554 239 APGRLVLQNVGInETRTGIIDVLRAMGAKIEIGEDTISV-ESSDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 325 DTIYPS------RFKHIAELERMGGKFKLEGRSAVINGPAKLQGSKVTAT-DLRAGAALVIAGLLAEGQTEIHGIEHIER 397
Cdd:cd01554 317 DAEELKvketdrIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAINT 396
|
410
....*....|..
gi 694157475 398 GYSKIIEKLAAI 409
Cdd:cd01554 397 SYPSFFDDLESL 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
5-395 |
5.70e-26 |
|
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: 108.64 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 5 LVIRGGKKLAGTMQVDGAKN-SAVALIPAAiLAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIdptdmIsmp 83
Cdd:COG0128 4 LTIAPPSPLKGTVRVPGSKSiSHRALLLAA-LAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLR-----V--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 84 lpTGNVKKLRA------------SYYLMGAMLGRFKKAVVgLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGA---IYLR 148
Cdd:COG0128 75 --TGVGGGLKEpdavldcgnsgtTMRLLTGLLALQPGEVV-LTGDESLRKRPMGRLLDPLRQLGARIESRGGGylpLTIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 149 ADELIGARIYLD-VVS---VGAtinIMLAAVRAKGKTIIENAAKEPEI--IDVaTL--LSNMGAIIKGAGTDTIRITGVE 220
Cdd:COG0128 152 GGPLKGGEYEIPgSASsqfKSA---LLLAGPLAEGGLEITVTGELESKpyRDH-TErmLRAFGVEVEVEGYRRFTVPGGQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 221 HLHGCHHTIIPDRIEAGTFMVLAAASGKGVRIENVIPTHLEG---IIAKLTEMGVPMDIEEDAIFVgEVEKVKKIDIKTY 297
Cdd:COG0128 228 RYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGdtgILDILKEMGADIEIENDGITV-RGSPLKGIDIDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 298 AYPgfptDLQQPLTALLTRAEGSSVVTDtIYPSRFKH-------IAELERMGGKFKLEGRSAVINGPAKLQGSKV-TATD 369
Cdd:COG0128 307 DIP----DEAPTLAVLAAFAEGTTRIRG-AAELRVKEsdriaamATELRKLGADVEETEDGLIIEGGPKLKGAEVdSYGD 381
|
410 420
....*....|....*....|....*.
gi 694157475 370 LRAGAALVIAGLLAEGQTEIHGIEHI 395
Cdd:COG0128 382 HRIAMAFAVAGLRAEGPVTIDDAECV 407
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
28-395 |
9.80e-24 |
|
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: 102.25 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 28 ALIPAAiLAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTDMI----SMPLPTGN---VKKLrasyyLMG 100
Cdd:cd01556 17 ALLLAA-LAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGGGLglppEAVLDCGNsgtTMRL-----LTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 101 AMLGRFKKAVvgLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGAIYL---RADELIGARIYLD------VVSVgatinIM 171
Cdd:cd01556 91 LLALQGGDSV--LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPpliGGGGLKGGEVEIPgavssqFKSA-----LL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 172 LAAVRAKGKTIIENAAKEPEI-IDVaTL--LSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVLAAASGK 248
Cdd:cd01556 164 LAAPLAEGPTTIIIGELESKPyIDH-TErmLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGDASSAAFFLAAAAITGS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 249 GVRIENV-IPTHLEGIIAKLTEMGVpmDIE---EDAIFVGEVEKVKKIDIKTYAYPgfptDLQQPLTALLTRAEGSSVVT 324
Cdd:cd01556 243 EIVIKNVgLNSGDTGIIDVLKEMGA--DIEignEDTVVVESGGKLKGIDIDGNDIP----DEAPTLAVLAAFAEGPTRIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 325 DtIYPSRFKH-------IAELERMGGKFKLEGRSAVING-PAKLQGSKV-TATDLRAGAALVIAGLLAEGQTEIHGIEHI 395
Cdd:cd01556 317 N-AAELRVKEsdriaamATELRKLGADVEETEDGLIIEGgPLKGAGVEVyTYGDHRIAMSFAIAGLVAEGGVTIEDPECV 395
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
28-412 |
7.34e-23 |
|
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: 99.66 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 28 ALIPAAiLAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPtdmISMPLPtGNVKKLRASYYLMgamlgRFK 107
Cdd:TIGR01356 15 ALILAA-LAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEG---VGGKEP-QAELDLGNSGTTA-----RLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 108 KAVVGLPGGCY-------LGPRPIDQHIKGFEALGAKVTNEQGAIYLRADelIGARIYLDVVSVGATIN------IMLAA 174
Cdd:TIGR01356 85 TGVLALADGEVvltgdesLRKRPMGRLVDALRQLGAEISSLEGGGSLPLT--ISGPLPGGIVYISGSASsqyksaLLLAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 175 VRAKGKTI---IENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHLHGCHHTIIPDRIEAGTFMVLAAASGKGVR 251
Cdd:TIGR01356 163 PALQAVGItivGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAAAITGGRVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 252 IENVIPTHLEG---IIAKLTEMGVPMDIEEDAIFVGEVEKVKKIDIKTyayPGFPtDLQQPLTALLTRAEGSSVVTDtIY 328
Cdd:TIGR01356 243 LENLGINPTQGdkaIIIVLEEMGADIEVEEDDLIVEGASGLKGIKIDM---DDMI-DELPTLAVLAAFAEGVTRITG-AE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 329 PSRFKH-------IAELERMGGKFKLEGRSAVINGPAKLQGSKV-TATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYS 400
Cdd:TIGR01356 318 ELRVKEsdriaaiAEELRKLGVDVEEFEDGLYIRGKKELKGAVVdTFGDHRIAMAFAVAGLVAEGEVLIDDPECVAKSFP 397
|
410
....*....|..
gi 694157475 401 KIIEKLAAIGAD 412
Cdd:TIGR01356 398 SFFDVLERLGAN 409
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-413 |
3.07e-14 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 74.02 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 1 MTEKLVIRGGKKLAGTMQVDGAKN-SAVALIPAAiLAESEVVLEGLPDISDVYTLYDILEELGgnVRYDNKTAVIDPTDM 79
Cdd:PRK02427 1 MMMMLLIIPPSPLSGTVRVPGSKSiSHRALLLAA-LAEGETTITNLLRSEDTLATLNALRALG--VEIEDDEVVVEGVGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 80 ISMPLPT-----GN---VkkLRasyYLMGAMLGRFKKAVvgLPGGCYLGPRPIDQHIKGFEALGAKVTNEQGA---IYLR 148
Cdd:PRK02427 78 GGLKEPEdvldcGNsgtT--MR---LLTGLLALQPGEVV--LTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGylpLTIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 149 -ADELIGARIYLDV----VSvGAtinIMLAAVRAKGKTIIEnaAKEPEI----IDV-ATLLSNMGAIIK---GAGTDTIR 215
Cdd:PRK02427 151 gGKKGGPIEYDGPVssqfVK-SL---LLLAPLFAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWGYRRIV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 216 ITGVEHLHGCHHTIIPDRIEAGTFMVLAA-ASGKGVRIENVIPTHLEG---IIAKLTEMGVpmDIEEDAIFVGeVEKVKK 291
Cdd:PRK02427 225 IKGGQRLRGQDITVPGDPSSAAFFLAAAAiTGGSEVTITNVGLNSTQGgkaIIDVLEKMGA--DIEIENEREG-GEPVGD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 292 IDIKTYAY-------PGFPtDLQQPLTALLTRAEGSSVVTDtIYPSRFKH-------IAELERMGGKFKLEGRSAVINGP 357
Cdd:PRK02427 302 IRVRSSELkgididiPDII-DEAPTLAVLAAFAEGTTVIRN-AEELRVKEtdriaamATELRKLGAEVEETEDGLIITGG 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 694157475 358 AKlqGSKV-TATDLRAGAALVIAGLLAEGQTEIHGIEHIERGYSKIIEKLAAIGADI 413
Cdd:PRK02427 380 PL--AGVVdSYGDHRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANI 434
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
231-409 |
7.53e-10 |
|
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: 58.44 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 231 PDRIEAGTFMVLAAASGKGVRIENVIP--------THLEGIIAKLTEMgVPMDIEE----DAIFVGEVEKVKKIDIKTYA 298
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTGIRPdrakpgllRQHLTFLKALEKI-CGATVEGgelgSDRISFRPGTVRGGDVRFAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 299 YP-GFPTDLQQPLTALLTRAEGSSVVTDTIYPS----------RFKHIAELERMGGKFKLE------------GRSAVIN 355
Cdd:cd01553 87 GSaGSCTDVLQTILPLLLFAKGPTRLTVTGGTDnpsappadfiRFVLEPELAKIGAHQEETllrhgfypagggVVATEVS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694157475 356 GPAKLQGSKVTATdlragaalvIAGLLAEGQTEIHGIEHIERGYSKIIEKLAAI 409
Cdd:cd01553 167 PVEKLNTAQLRQL---------VLPMLLASGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
309-417 |
6.94e-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: 47.94 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 309 PLTALLTRAEGSSVVTDTIYPSR--FKHIAE-LERMGGKFKL--EGRSAVINGPAKLQGSKVTatdLRAGA------ALV 377
Cdd:cd01556 87 LLTGLLALQGGDSVLTGDESLRKrpMGRLVDaLRQLGAEIEGreGGGYPPLIGGGGLKGGEVE---IPGAVssqfksALL 163
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 694157475 378 IAGLLAEGQTEIHGIEHIERGYSKIIEK-LAAIGADITRSS 417
Cdd:cd01556 164 LAAPLAEGPTTIIIGELESKPYIDHTERmLRAFGAEVEVDG 204
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
3-278 |
3.70e-05 |
|
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: 45.63 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 3 EKLVIRGGKKLAGTMQVD-GAKNSAVA---LIPAAILAESEVVLEGLPDISD--VYTLYDILEELGGNVRYDNKTAVidP 76
Cdd:cd01556 58 GTVEIVGGGGLGLPPEAVlDCGNSGTTmrlLTGLLALQGGDSVLTGDESLRKrpMGRLVDALRQLGAEIEGREGGGY--P 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 77 TDMISMPLPTGNVKkLRA-------SYYLMGAML--GRFKKAVVglpggcYLGPRP-IDQHIKGFEALGAKVTNEQGAIY 146
Cdd:cd01556 136 PLIGGGGLKGGEVE-IPGavssqfkSALLLAAPLaeGPTTIIIG------ELESKPyIDHTERMLRAFGAEVEVDGYRTI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 147 LradELIGARIYLDVVSVGATI----NIMLAAVRAKGKTIIENAAKEPEIIDVATLLSNMGAIIKGAGTDTIRITGVEHL 222
Cdd:cd01556 209 T---VKGGQKYKGPEYTVEGDAssaaFFLAAAAITGSEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDTVVVESGGKL 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694157475 223 HGChhTIIPDRI--EAGTFMVLAAASGKGVRIENV--IPTH----LEGIIAKLTEMGVpmDIEE 278
Cdd:cd01556 286 KGI--DIDGNDIpdEAPTLAVLAAFAEGPTRIRNAaeLRVKesdrIAAMATELRKLGA--DVEE 345
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
170-415 |
5.34e-05 |
|
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: 45.08 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 170 IMLAAVrAKGKTIIENAAKEPEIIdvATL--LSNMGAIIKGAGTDTIRITGVEH-LHGCHHTIipDRIEAGTFM-----V 241
Cdd:COG0128 29 LLLAAL-AEGESTIRNLLESDDTL--ATLeaLRALGAEIEELDGGTLRVTGVGGgLKEPDAVL--DCGNSGTTMrlltgL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 242 LAAASGkgvrienviPTHLEG-----------IIAKLTEMGV----------PMDIEEDAIFVGEVEkvkkIDIKTYAyp 300
Cdd:COG0128 104 LALQPG---------EVVLTGdeslrkrpmgrLLDPLRQLGAriesrgggylPLTIRGGPLKGGEYE----IPGSASS-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 301 gfptdlqQPLTALL---TRAEGSSV--VTDTIYPSRFKHIAE--LERMGGKFKLEG-RSAVINGPAKLQGSKVT-ATDLR 371
Cdd:COG0128 169 -------QFKSALLlagPLAEGGLEitVTGELESKPYRDHTErmLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTvPGDIS 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 694157475 372 AGAALVIAGLLAEGQTEIHGI-EHIERGYSKIIEKLAAIGADITR 415
Cdd:COG0128 242 SAAFFLAAAAITGSEVTVEGVgLNSTQGDTGILDILKEMGADIEI 286
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
170-395 |
5.60e-05 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 45.37 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 170 IMLAAVRAKGKTIIenaaKEPEIIDVAT--LLSNMGAIIKGAGtDTIRITGVEHLHGCHHTIIPDRIEAGTFMVLAA-AS 246
Cdd:PRK14806 475 LLLAGLYAEGETSV----TEPAPTRDHTerMLRGFGYPVKVEG-NTISVEGGGKLTATDIEVPADISSAAFFLVAASiAE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 247 GKGVRIENV--IPTHLeGIIAKLTEMGVPMDIEEDAIFVGevEKVKKIDIKTYAYPGF--PTDlQQPLT-----ALLTR- 316
Cdd:PRK14806 550 GSELTLEHVgiNPTRT-GVIDILKLMGADITLENEREVGG--EPVADIRVRGARLKGIdiPED-QVPLAidefpVLFVAa 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 317 --AEGSSVVTDT----IYPS-RFKHIAE-LERMGGKFKLEGRSAVINGPAKLQGSKVTATDLRAGAALVIAGLLAEGQTE 388
Cdd:PRK14806 626 acAEGRTVLTGAeelrVKESdRIQVMADgLKTLGIDCEPTPDGIIIEGGIFGGGEVESHGDHRIAMSFSVASLRASGPIT 705
|
....*..
gi 694157475 389 IHGIEHI 395
Cdd:PRK14806 706 IHDCANV 712
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
15-283 |
2.90e-04 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 43.16 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 15 GTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYDNKTAVIDPTdmismplpTGNVKKLRA 94
Cdd:PRK11861 253 GTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGT--------RGAFTAKTA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 95 SYYLMGAMLG-RFKKAVVGLPGGCY-------LGPRPIDQHIKGFEALGAKVTNE--QGAIYLR---ADELIGA--RIYL 159
Cdd:PRK11861 325 DLFLGNAGTAvRPLTAALAVNGGEYrihgvprMHERPIGDLVDGLRQIGARIDYEgnEGFPPLRirpATISVDApiRVRG 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 160 DVVSVGATINIM-LAAVRAK-GKTIIE---NAAKEPEIIDVATLLSNMGAIIKGAGTDTIRI-TGVEHLHGCHHTIIPDR 233
Cdd:PRK11861 405 DVSSQFLTALLMtLPLVKAKdGASVVEidgELISKPYIEITIKLMARFGVTVERDGWQRFTVpAGVRYRSPGTIMVEGDA 484
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 694157475 234 IEAGTFMVLAAASGKGVRIENVIPTHLEGIIA---KLTEMGVPMDIEEDAIFV 283
Cdd:PRK11861 485 SSASYFLAAGALGGGPLRVEGVGRASIQGDVGfanALMQMGANVTMGDDWIEV 537
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
2-139 |
1.15e-03 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 40.89 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 2 TEKLVIRGGKKLAGTMQVDGAKNSAVALIPAAILAESEVVLEGLPDISDVYTLYDILEELGGNVRYD--NKTAVIDPTdm 79
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDseNNRAVVEGC-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694157475 80 iSMPLPTGNVKKLRASYYL--MGAMLGRFKKAVVG--------LPGGCYLGPRPIDQHIKGFEALGAKVT 139
Cdd:PLN02338 79 -GGKFPVSGDSKEDVELFLgnAGTAMRPLTAAVTAaggnasyvLDGVPRMRERPIGDLVDGLKQLGADVE 147
|
|
| |
