|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
3-421 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 742.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:PRK12830 81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEG--RSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
|
410 420
....*....|....*....|
gi 488391868 402 YTDIVEHLEQLGADIWTEKV 421
Cdd:PRK12830 398 YSNIIEKLKALGADIWREED 417
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
4-417 |
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: 620.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 4 EVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIK-TQLNDTVLEVDTTEIKN 82
Cdd:COG0766 2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNINS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:COG0766 82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHG-YIEARAGRLKGARIYLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:COG0766 161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:COG0766 241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:COG0766 321 SVITETVFENRFMHVDELNRMGADIKLDG--HTAIVRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
|
410
....*....|....*.
gi 488391868 402 YTDIVEHLEQLGADIW 417
Cdd:COG0766 399 YENLEEKLRALGADIE 414
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
14-412 |
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: 578.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 14 LKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDT-VLEVDTTEIKNAPLPNNKVES 92
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 93 LRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDTSMKIEAKELIGTTIFLDMVSVGATINI 172
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 173 MLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMAAACGQEV 252
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 253 KINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAK-YKNVDIKTLVYPGFATDLQQPITPLLFKASGPSFVTETIYP 331
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 332 ARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLE 410
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEG--NTAIIRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398
|
..
gi 488391868 411 QL 412
Cdd:cd01555 399 AL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
3-417 |
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: 517.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIdESSDTSMKIEAKE-LIGTTIFL 161
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEI-VIEDGYVYASAKGrLVGAHIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 162 DMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTY 241
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 242 MCMAAACGQEVKINNIVPKHVEALMVKLQELGVDITV-EDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKAS 320
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVdENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 321 GPSFVTETIYPARFKHVEELQHMGANIEADevTGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIY 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLE--GNTAVIHgVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
|
410
....*....|....*...
gi 488391868 400 RGYTDIVEHLEQLGADIW 417
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIE 415
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
9-409 |
3.38e-91 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 281.49 E-value: 3.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 9 RGGQTLKGEVNISG-AKNSAVAIIPATLLAqGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTE--IKNAPL 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEglGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 86 PNNKVESLRASYYMMGAMLGRF--KKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSD---TSMKIEAKELIGTTIF 160
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLalQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGynyAPLKVRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 161 LDMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTST-LKIKGVDALHGSEYQVIPDRIEAG 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 240 TYMCMAAACGQEVKINNIVPKHV---EALMVKLQELGVDITVEDEYAIIKGKAKY--KNVDIKTLVYPGFATDLQQPITP 314
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 315 LLFKASGPSFVTETIYPARFKHVEELQHMGANIEADEVTGTATIKPSTLHGTEVYAS-DLRAGACLIIAGLIAEGVTTIY 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 488391868 394 NVKHIYRGYTDIVEHL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
3-421 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 742.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILADGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDTLEIDPTGIQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:PRK12830 81 MPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGG-AIYLKADELKGAHIYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:PRK12830 160 VVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAGTYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:PRK12830 240 ILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKANGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:PRK12830 320 SVVTDTIYEKRFKHVDELKRMGANIKVEG--RSAIITgPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDRG 397
|
410 420
....*....|....*....|
gi 488391868 402 YTDIVEHLEQLGADIWTEKV 421
Cdd:PRK12830 398 YSNIIEKLKALGADIWREED 417
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
4-417 |
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: 620.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 4 EVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIK-TQLNDTVLEVDTTEIKN 82
Cdd:COG0766 2 DKLIIEGGKPLSGEVRISGAKNAALPILAAALLTDGPVTLRNVPDLSDVRTMLELLESLGVKvERDDGGTLTIDASNINS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDtSMKIEAKELIGTTIFLD 162
Cdd:COG0766 82 TEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHG-YIEARAGRLKGARIYLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 163 MVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYM 242
Cdd:COG0766 161 FPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAGTFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 243 CMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKASGP 322
Cdd:COG0766 241 VAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQAEGT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 323 SFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRG 401
Cdd:COG0766 321 SVITETVFENRFMHVDELNRMGADIKLDG--HTAIVRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETVIDNIYHIDRG 398
|
410
....*....|....*.
gi 488391868 402 YTDIVEHLEQLGADIW 417
Cdd:COG0766 399 YENLEEKLRALGADIE 414
|
|
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
4-417 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 580.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 4 EVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDT-VLEVDTTEIKN 82
Cdd:PRK09369 2 DKLVIEGGKPLSGEVTISGAKNAALPILAASLLAEEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNgTVTIDASNINN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDTsmkIEAK---ELIGTTI 159
Cdd:PRK09369 82 TEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGY---VEAKadgRLKGAHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 160 FLDMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAG 239
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 240 TYMCMAAACGQEVKINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKA 319
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 320 SGPSFVTETIYPARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHI 398
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDG--HTAVVRgVEKLSGAPVMATDLRASASLVLAGLVAEGTTIVDRIYHL 396
|
410
....*....|....*....
gi 488391868 399 YRGYTDIVEHLEQLGADIW 417
Cdd:PRK09369 397 DRGYERIEEKLRALGADIE 415
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
14-412 |
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: 578.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 14 LKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDT-VLEVDTTEIKNAPLPNNKVES 92
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLGAKVEFEGEnTLVIDASNINSTEAPYELVRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 93 LRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSDTSMKIEAKELIGTTIFLDMVSVGATINI 172
Cdd:cd01555 81 MRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATENI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 173 MLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMAAACGQEV 252
Cdd:cd01555 161 MMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGGDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 253 KINNIVPKHVEALMVKLQELGVDITVEDEYAIIKGKAK-YKNVDIKTLVYPGFATDLQQPITPLLFKASGPSFVTETIYP 331
Cdd:cd01555 241 TVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGGrLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETIFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 332 ARFKHVEELQHMGANIEADEvtGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLE 410
Cdd:cd01555 321 NRFMHVDELNRMGADIKVEG--NTAIIRgVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398
|
..
gi 488391868 411 QL 412
Cdd:cd01555 399 AL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
3-417 |
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: 517.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 3 QEVIKIRGGQTLKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEIKN 82
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLTDEPVTLTNVPDLSDVKTTLDLLRNLGARVERDNNTLEINTPNINS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 83 APLPNNKVESLRASYYMMGAMLGRFKKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIdESSDTSMKIEAKE-LIGTTIFL 161
Cdd:TIGR01072 81 TEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEI-VIEDGYVYASAKGrLVGAHIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 162 DMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTY 241
Cdd:TIGR01072 160 DKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAGTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 242 MCMAAACGQEVKINNIVPKHVEALMVKLQELGVDITV-EDEYAIIKGKAKYKNVDIKTLVYPGFATDLQQPITPLLFKAS 320
Cdd:TIGR01072 240 LVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVdENGIRVDMRQKRLKAVDIETLPYPGFPTDLQAQFMALLSQAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 321 GPSFVTETIYPARFKHVEELQHMGANIEADevTGTATIK-PSTLHGTEVYASDLRAGACLIIAGLIAEGVTTIYNVKHIY 399
Cdd:TIGR01072 320 GTSVITETVFENRFMHVDELIRMGANIKLE--GNTAVIHgVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
|
410
....*....|....*...
gi 488391868 400 RGYTDIVEHLEQLGADIW 417
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIE 415
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
9-409 |
3.38e-91 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 281.49 E-value: 3.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 9 RGGQTLKGEVNISG-AKNSAVAIIPATLLAqGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTE--IKNAPL 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAA-GESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEglGGSFEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 86 PNNKVESLRASYYMMGAMLGRF--KKCVIGLPGGCPLGPRPIDQHIKGFKALGAEIDESSD---TSMKIEAKELIGTTIF 160
Cdd:pfam00275 80 PEDLVLDMGNSGTALRPLTGRLalQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGynyAPLKVRGLRLGGIHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 161 LDMVSVGATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTST-LKIKGVDALHGSEYQVIPDRIEAG 239
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 240 TYMCMAAACGQEVKINNIVPKHV---EALMVKLQELGVDITVEDEYAIIKGKAKY--KNVDIKTLVYPGFATDLQQPITP 314
Cdd:pfam00275 240 YFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDADIVVGPPGLrgKAVDIRTAPDPAPTTAVLAAFAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 315 LLFKASGPSFVTETIYPARFKHVEELQHMGANIEADEVTGTATIKPSTLHGTEVYAS-DLRAGACLIIAGLIAEGVTTIY 393
Cdd:pfam00275 320 GTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETIID 399
|
410
....*....|....*.
gi 488391868 394 NVKHIYRGYTDIVEHL 409
Cdd:pfam00275 400 DIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
14-412 |
5.82e-74 |
|
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: 237.12 E-value: 5.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 14 LKGEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVDTTEI---KNAPLPNNKV 90
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMaglKAPQNALNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 91 ESLRASYYMMGAMLGRFKKcvIGLPGGCPLGPRPIDQHIKGFKALGAEI---DESSDTSMKIEAKELIGTTIFLDMVSVG 167
Cdd:cd01554 81 NSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASIsgqEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 168 ATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMAAA 247
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 248 CGQEVKINNIVPKHVE-ALMVKLQELGVDITVEDEYaIIKGKAKYKNVDIKTLVYPgFATDLQQPITPLLFKASGPSFVT 326
Cdd:cd01554 239 APGRLVLQNVGINETRtGIIDVLRAMGAKIEIGEDT-ISVESSDLKATEICGALIP-RLIDELPIIALLALQAQGTTVIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 327 ETIYPA------RFKHVEELQHMGANIEadEVTGTATIK-PSTLHGTEVYA-SDLRAGACLIIAGLIAEGVTTIYNVKHI 398
Cdd:cd01554 317 DAEELKvketdrIFVVADELNSMGADIE--PTADGMIIKgKEKLHGARVNTfGDHRIGMMTALAALVADGEVELDRAEAI 394
|
410
....*....|....
gi 488391868 399 YRGYTDIVEHLEQL 412
Cdd:cd01554 395 NTSYPSFFDDLESL 408
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
14-412 |
1.67e-25 |
|
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: 107.26 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 14 LKGEVNISGAKN-SAVAIIPAtLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVdtTEIKNAPLPNNKV-- 90
Cdd:cd01556 1 LSGEITVPGSKSiSHRALLLA-ALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEI--VGGGGLGLPPEAVld 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 91 --ESLRASYYMMGAMLGRFKKCVIGlpGGCPLGPRPIDQHIKGFKALGAEID--ESSDTSMKIEAKELIGTTIFLDM-VS 165
Cdd:cd01556 78 cgNSGTTMRLLTGLLALQGGDSVLT--GDESLRKRPMGRLVDALRQLGAEIEgrEGGGYPPLIGGGGLKGGEVEIPGaVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 166 ---VGAtinIMLAAVHAKGQTIIENAAKEPEV-VDV-ANFLMSMGANIKGAGTSTLKIKGVDALHGSEYQVIPDrIEAGT 240
Cdd:cd01556 156 sqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEYTVEGD-ASSAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 241 YMcMAAAC--GQEVKINNIVPKHVEALMVK-LQELGVDITVEDE-YAIIKGKAKYKNVDIKtlvyPGFATDLQQPITPLL 316
Cdd:cd01556 232 FF-LAAAAitGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIGNEdTVVVESGGKLKGIDID----GNDIPDEAPTLAVLA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 317 FKASGPSFVTeTIYPARFKH-------VEELQHMGANIEadEVTGTATIKPSTLH--GTEVYAS-DLRAGACLIIAGLIA 386
Cdd:cd01556 307 AFAEGPTRIR-NAAELRVKEsdriaamATELRKLGADVE--ETEDGLIIEGGPLKgaGVEVYTYgDHRIAMSFAIAGLVA 383
|
410 420
....*....|....*....|....*.
gi 488391868 387 EGVTTIYNVKHIYRGYTDIVEHLEQL 412
Cdd:cd01556 384 EGGVTIEDPECVAKSFPNFFEDLESL 409
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
16-415 |
8.85e-19 |
|
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: 87.72 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 16 GEVNISGAKNSAVAIIPATLLAQGKVQLDGLPQISDVETLVSLLEDLNIKTQLNDTVLEVD--TTEIKNAPL-PNNKVES 92
Cdd:TIGR01356 1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEgvGGKEPQAELdLGNSGTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 93 LRasyYMMGAM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSDTS---MKIEAKELIGTTIFLDMVSVGA 168
Cdd:TIGR01356 81 AR---LLTGVLaLADGEVVLTGDES---LRKRPMGRLVDALRQLGAEISSLEGGGslpLTISGPLPGGIVYISGSASSQY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 169 TINIMLAAVHAKGQTIIENAAKEPEV--VDVANFLMSM-GANIKGAGTSTLKIKGVDALHGSEYQVIPDRIEAGTYMCMA 245
Cdd:TIGR01356 155 KSALLLAAPALQAVGITIVGEPLKSRpyIEITLDLLGSfGVEVERSDGRKIVVPGGQKYGPQGYDVPGDYSSAAFFLAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 246 AACGQEVKINNIVPKHVE---ALMVKLQELGVDITVEDEYAIIKGKAKYK--NVDIKTLvypgfaTDLQQPITPLLFKAS 320
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQgdkAIIIVLEEMGADIEVEEDDLIVEGASGLKgiKIDMDDM------IDELPTLAVLAAFAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 321 GPSFVTEtIYPARFKH-------VEELQHMGANIE--AD--EVTGTATIKPSTLHGtevYAsDLRAGACLIIAGLIAEGV 389
Cdd:TIGR01356 309 GVTRITG-AEELRVKEsdriaaiAEELRKLGVDVEefEDglYIRGKKELKGAVVDT---FG-DHRIAMAFAVAGLVAEGE 383
|
410 420
....*....|....*....|....*.
gi 488391868 390 TTIYNVKHIYRGYTDIVEHLEQLGAD 415
Cdd:TIGR01356 384 VLIDDPECVAKSFPSFFDVLERLGAN 409
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
4-412 |
1.94e-17 |
|
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: 83.60 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 4 EVIKIRGGQTLKGEVNISGAKN-SAVAIIPAtLLAQGKVQLDGLPQISDVETLVSLLEDLNIK-TQLNDTVLEVdttEIK 81
Cdd:COG0128 2 SSLTIAPPSPLKGTVRVPGSKSiSHRALLLA-ALAEGESTIRNLLESDDTLATLEALRALGAEiEELDGGTLRV---TGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 82 NAPLPNNKVE--------SLRasyYMMGAM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSDTS--MKIE 150
Cdd:COG0128 78 GGGLKEPDAVldcgnsgtTMR---LLTGLLaLQPGEVVLTGDES---LRKRPMGRLLDPLRQLGARIESRGGGYlpLTIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 151 AKELIGTTIFLD-MVS---VGAtinIMLAAVHAKGQTIIENAAKEPEV--VDVA-NFLMSMGANIKGAGTSTLKIKGVDA 223
Cdd:COG0128 152 GGPLKGGEYEIPgSASsqfKSA---LLLAGPLAEGGLEITVTGELESKpyRDHTeRMLRAFGVEVEVEGYRRFTVPGGQR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 224 LHGSEYQVIPDRIEAGTYMCMAAACGQEVKINN--IVPKHVEALMVK-LQELGVDITVEDEYAIIKGkAKYKNVDIKtlv 300
Cdd:COG0128 229 YRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGvgLNSTQGDTGILDiLKEMGADIEIENDGITVRG-SPLKGIDID--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 301 yPGFATDLQQPITPLLFKASGPSFVTeTIYPARFKH-------VEELQHMGANIEADE----VTGTATIKPSTLHGtevY 369
Cdd:COG0128 305 -LSDIPDEAPTLAVLAAFAEGTTRIR-GAAELRVKEsdriaamATELRKLGADVEETEdgliIEGGPKLKGAEVDS---Y 379
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488391868 370 AsDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLEQL 412
Cdd:COG0128 380 G-DHRIAMAFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
6-416 |
3.73e-13 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 70.56 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 6 IKIRGGQTLKGEVNISGAKN-SAVAIIPAtLLAQGKVQLDGLPQISDVETLVSLLEDLNIKtqLNDTVLEVDTTEIKNAP 84
Cdd:PRK02427 5 LLIIPPSPLSGTVRVPGSKSiSHRALLLA-ALAEGETTITNLLRSEDTLATLNALRALGVE--IEDDEVVVEGVGGGGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 85 LPNNKVE------SLRasyYMMGAM-LGRFKKCVIGLPGgcpLGPRPIDQHIKGFKALGAEIDESSDTS--MKIE-AKEL 154
Cdd:PRK02427 82 EPEDVLDcgnsgtTMR---LLTGLLaLQPGEVVLTGDES---LRKRPMGRLLDPLRQMGAKIEGRDEGYlpLTIRgGKKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 155 IGTTIFLDM----VSvGAtinIMLAAVHAKGQTIIEnaAKEPEV----VDV-ANFLMSMGANIK---GAGTSTLKIKGVD 222
Cdd:PRK02427 156 GPIEYDGPVssqfVK-SL---LLLAPLFAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveGWGYRRIVIKGGQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 223 ALHGSEYQVIPDrIEAGTYMcMAAAC---GQEVKINNI--VPKHVEALMVK-LQELGVDITVEDEYAIIKGKAkykNVDI 296
Cdd:PRK02427 230 RLRGQDITVPGD-PSSAAFF-LAAAAitgGSEVTITNVglNSTQGGKAIIDvLEKMGADIEIENEREGGEPVG---DIRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 297 KTLVYPGF------ATDLQQPITPL-LFkASGPSfvteTIYPA---RFKH-------VEELQHMGANIEADEvtGTATIK 359
Cdd:PRK02427 305 RSSELKGIdidipdIIDEAPTLAVLaAF-AEGTT----VIRNAeelRVKEtdriaamATELRKLGAEVEETE--DGLIIT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488391868 360 PSTLHGT-EVYAsDLRAGACLIIAGLIAEGVTTIYNVKHIYRGYTDIVEHLEQLGADI 416
Cdd:PRK02427 378 GGPLAGVvDSYG-DHRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLASLGANI 434
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
129-416 |
6.05e-13 |
|
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: 70.12 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 129 IKGFKALGAEIDESSDTSMKIE--AKELIGTTIFLDMVSVGATINIMLAAV-HAKGQTII---ENAAKEP--EVVDVanf 200
Cdd:COG0128 54 LEALRALGAEIEELDGGTLRVTgvGGGLKEPDAVLDCGNSGTTMRLLTGLLaLQPGEVVLtgdESLRKRPmgRLLDP--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 201 LMSMGANIKGAGTST--LKIKGvDALHGSEY--------QVIpdrieagTYMCMAAAC---GQEVKI-NNIVPK----HV 262
Cdd:COG0128 131 LRQLGARIESRGGGYlpLTIRG-GPLKGGEYeipgsassQFK-------SALLLAGPLaegGLEITVtGELESKpyrdHT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 263 EALMvklQELGVDITVEDEYAI-IKGKAKYKNVDIKtlVyPGfatDLQQPITPLLFKASGPSFVT------ETIYP-ARF 334
Cdd:COG0128 203 ERML---RAFGVEVEVEGYRRFtVPGGQRYRPGDYT--V-PG---DISSAAFFLAAAAITGSEVTvegvglNSTQGdTGI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 335 khVEELQHMGANIEADEvtGTATIKPSTLHGTEVyasDLRAGACLI----IAGLIAEGVTTIYNVKHIyRGY-TD----I 405
Cdd:COG0128 274 --LDILKEMGADIEIEN--DGITVRGSPLKGIDI---DLSDIPDEAptlaVLAAFAEGTTRIRGAAEL-RVKeSDriaaM 345
|
330
....*....|.
gi 488391868 406 VEHLEQLGADI 416
Cdd:COG0128 346 ATELRKLGADV 356
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
233-412 |
3.29e-12 |
|
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: 65.38 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 233 PDRIEAGTYMCMAAACGQEVKINNIVP---------KHVEALMVKLQELGVDITV--EDEYAIIKGKAKYKNVDIKTLVY 301
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTGIRPdrakpgllrQHLTFLKALEKICGATVEGgeLGSDRISFRPGTVRGGDVRFAIG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 302 P-GFATDLQQPITPLLFKASGPSFVTETIYPA----------RFKHVEELQHMGANIEADEVTGTATIKPSTLHGTEVY- 369
Cdd:cd01553 88 SaGSCTDVLQTILPLLLFAKGPTRLTVTGGTDnpsappadfiRFVLEPELAKIGAHQEETLLRHGFYPAGGGVVATEVSp 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488391868 370 -----ASDLRAGACLIIAGliaeGVTTIYNVKHIYRGYTDIVEHLEQL 412
Cdd:cd01553 168 veklnTAQLRQLVLPMLLA----SGAVEFTVAHPSCHLLTNFAVLEAL 211
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
129-422 |
2.71e-09 |
|
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: 58.44 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 129 IKGFKALGAEIDESSDTsMKIEAKELIGTTIFLDMVSVGATINIMLAAVHAKGQTII----ENAAKEPeVVDVANFLMSM 204
Cdd:TIGR01356 41 LDALRALGAKIEDGGEV-AVIEGVGGKEPQAELDLGNSGTTARLLTGVLALADGEVVltgdESLRKRP-MGRLVDALRQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 205 GANI---KGAGTSTLKIKGvdALHGSEYQVIPDR-IEAGTYMCMAAACGQ----EVKINNIVPK-HVEaLMVKLQE-LGV 274
Cdd:TIGR01356 119 GAEIsslEGGGSLPLTISG--PLPGGIVYISGSAsSQYKSALLLAAPALQavgiTIVGEPLKSRpYIE-ITLDLLGsFGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 275 DITVEDEYAI-IKGKAKYKNVDIKTlvyPGfatDLQQPITPLLFKASGPSFVTET---IYPARF--KHVEELQHMGANIE 348
Cdd:TIGR01356 196 EVERSDGRKIvVPGGQKYGPQGYDV---PG---DYSSAAFFLAAAAITGGRVTLEnlgINPTQGdkAIIIVLEEMGADIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 349 AD----EVTGtatikPSTLHGTEVYASDLrAGACLIIAGL--IAEGVTTIYNVKHIYRGYTD----IVEHLEQLGADIwT 418
Cdd:TIGR01356 270 VEeddlIVEG-----ASGLKGIKIDMDDM-IDELPTLAVLaaFAEGVTRITGAEELRVKESDriaaIAEELRKLGVDV-E 342
|
....
gi 488391868 419 EKVD 422
Cdd:TIGR01356 343 EFED 346
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
269-416 |
3.24e-08 |
|
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: 55.26 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 269 LQELGVDITVEDEYAIIKGKAKYKNVDIKTLvYPGFATDLQQPITPLLFKASGPSFVTETIYPAR--FKH-VEELQHMGA 345
Cdd:cd01556 46 LRALGAKIEEEGGTVEIVGGGGLGLPPEAVL-DCGNSGTTMRLLTGLLALQGGDSVLTGDESLRKrpMGRlVDALRQLGA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488391868 346 NIEADEVTGTA-TIKPSTLHGTEVyasDLRAGA------CLIIAGLIAEGVTTIYNVKHIYRGYTDIVEH-LEQLGADI 416
Cdd:cd01556 125 EIEGREGGGYPpLIGGGGLKGGEV---EIPGAVssqfksALLLAAPLAEGPTTIIIGELESKPYIDHTERmLRAFGAEV 200
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
172-416 |
2.26e-07 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 52.78 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 172 IMLAAVhAKGQTIIENAAKEPEVVDVANFLMSMGANIKGAGTSTLKIKGVdalhGSEYQVIPDRI---EAGT--YMCMAA 246
Cdd:COG0128 29 LLLAAL-AEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGV----GGGLKEPDAVLdcgNSGTtmRLLTGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 247 ACGQevkinnivPKHVE----ALMVK---------LQELGVDIT-VEDEYA--IIKGkAKYKNVDIKTlvyPGFATDlqQ 310
Cdd:COG0128 104 LALQ--------PGEVVltgdESLRKrpmgrlldpLRQLGARIEsRGGGYLplTIRG-GPLKGGEYEI---PGSASS--Q 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 311 PITPLLFkaSGPSF-------VTETIYPARF-KHVEE-LQHMGANIEADEvTGTATIK-PSTLHGTEVY-ASDLRAGACL 379
Cdd:COG0128 170 FKSALLL--AGPLAeggleitVTGELESKPYrDHTERmLRAFGVEVEVEG-YRRFTVPgGQRYRPGDYTvPGDISSAAFF 246
|
250 260 270
....*....|....*....|....*....|....*...
gi 488391868 380 IIAGLIAEGVTTIYNV-KHIYRGYTDIVEHLEQLGADI 416
Cdd:COG0128 247 LAAAAITGSEVTVEGVgLNSTQGDTGILDILKEMGADI 284
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
133-288 |
4.35e-04 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 42.67 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 133 KALGAEIDESSDTSMKIEAKELIGTTIFL--DMVSvgATINIMLAAVHAKGQTIIENAAKEPEVVDVANFLMSMGANIK- 209
Cdd:PRK14806 503 RGFGYPVKVEGNTISVEGGGKLTATDIEVpaDISS--AAFFLVAASIAEGSELTLEHVGINPTRTGVIDILKLMGADITl 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 210 -------GAGTSTLKIKGVDaLHG---SEYQViPDRIEAGTYMCMAAACGQEVKinniVPKHVEALMVK----------- 268
Cdd:PRK14806 581 enerevgGEPVADIRVRGAR-LKGidiPEDQV-PLAIDEFPVLFVAAACAEGRT----VLTGAEELRVKesdriqvmadg 654
|
170 180
....*....|....*....|
gi 488391868 269 LQELGVDITVEDEYAIIKGK 288
Cdd:PRK14806 655 LKTLGIDCEPTPDGIIIEGG 674
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
262-416 |
1.61e-03 |
|
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: 40.34 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 262 VEALMVKLQELGVDITVEDEYAIIKGKA-KYKNVDIktlvYPGFATDLQQPITPLLFKASGPsfvTETIYPARFKH---- 336
Cdd:TIGR01356 37 TLATLDALRALGAKIEDGGEVAVIEGVGgKEPQAEL----DLGNSGTTARLLTGVLALADGE---VVLTGDESLRKrpmg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391868 337 --VEELQHMGANIEADEVTGTA--TIKpSTLHGTEVYASDLRA---GACLIIAGLIAEGVT-TIYNVKHIYRGYTDIVeh 408
Cdd:TIGR01356 110 rlVDALRQLGAEISSLEGGGSLplTIS-GPLPGGIVYISGSASsqyKSALLLAAPALQAVGiTIVGEPLKSRPYIEIT-- 186
|
....*...
gi 488391868 409 LEQLGADI 416
Cdd:TIGR01356 187 LDLLGSFG 194
|
|
|