|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 679.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFD-GNGTVTIDASN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:PRK09369 79 INNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELTHLDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDlrasaslvlaglvaEGTTIVDRIYHLDR 398
|
410
....*....|....*....
gi 612660555 401 GYVDLHGKLKQLGADIERI 419
Cdd:PRK09369 399 GYERIEEKLRALGADIERV 417
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 667.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLT-DGPVTLRNVPDLSDVRTMLELLESLGVKVERD-DGGTLTIDASN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAkDGLKGTSI 160
Cdd:COG0766 79 INSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARA-GRLKGARI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:COG0766 158 YLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:COG0766 238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELTHLDR 400
Cdd:COG0766 318 EGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDlragaalvlaglaaEGETVIDNIYHIDR 397
|
410
....*....|....*....
gi 612660555 401 GYVDLHGKLKQLGADIERI 419
Cdd:COG0766 398 GYENLEEKLRALGADIERV 416
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
12-412 |
0e+00 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.
Pssm-ID: 238796 Cd Length: 400 Bit Score: 593.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 12 LTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTyKKDENAVVVDATKTLNEEAPYEYV 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVE-FEGENTLVIDASNINSTEAPYELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 92 SKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSIHLDFPSVGATQ 171
Cdd:cd01555 79 RKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 172 NIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRG 251
Cdd:cd01555 159 NIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 252 DIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLTANGHKVVTETV 330
Cdd:cd01555 239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 331 FENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELTHLDRGYVDLHGKLK 410
Cdd:cd01555 319 FENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398
|
..
gi 612660555 411 QL 412
Cdd:cd01555 399 AL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
1-418 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 162190 [Multi-domain] Cd Length: 416 Bit Score: 583.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYkkDENAVVVDATK 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLT-DEPVTLTNVPDLSDVKTTLDLLRNLGARVER--DNNTLEINTPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:TIGR01072 78 INSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLT 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 320 ANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELTHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
|
410
....*....|....*....
gi 612660555 400 RGYVDLHGKLKQLGADIER 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-409 |
2.82e-109 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 327.72 E-value: 2.82e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 7 KGGNKLTGEVKVEG-AKNAVLPILTASLLASdkPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEE 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAG--ESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 86 APYEYVSKMRASILVMGPLLARLGHAI--VALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAK---DGLKGTSI 160
Cdd:pfam00275 79 APEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDT-ITINGVESLHGVEHAIIPDRIEA 239
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 240 GTLLIAGAITRGDIFVRGAIKEHM---ASLVYKLEEMGVELEYQEDG-IRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMM 314
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDAdIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 315 ALLLTANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSA-KLEGKSQLQGAQVKAT-DLRAAAALILAGLVADGKTSV 392
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETII 398
|
410
....*....|....*..
gi 612660555 393 TELTHLDRGYVDLHGKL 409
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09369 |
PRK09369 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
Pssm-ID: 236486 Cd Length: 417 Bit Score: 679.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:PRK09369 1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFD-GNGTVTIDASN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:PRK09369 79 INNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELTHLDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDlrasaslvlaglvaEGTTIVDRIYHLDR 398
|
410
....*....|....*....
gi 612660555 401 GYVDLHGKLKQLGADIERI 419
Cdd:PRK09369 399 GYERIEEKLRALGADIERV 417
|
|
| MurA |
COG0766 |
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ... |
1-419 |
0e+00 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine enolpyruvyl transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440529 Cd Length: 416 Bit Score: 667.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:COG0766 1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLT-DGPVTLRNVPDLSDVRTMLELLESLGVKVERD-DGGTLTIDASN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAkDGLKGTSI 160
Cdd:COG0766 79 INSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARA-GRLKGARI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:COG0766 158 YLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:COG0766 238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELTHLDR 400
Cdd:COG0766 318 EGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDlragaalvlaglaaEGETVIDNIYHIDR 397
|
410
....*....|....*....
gi 612660555 401 GYVDLHGKLKQLGADIERI 419
Cdd:COG0766 398 GYENLEEKLRALGADIERV 416
|
|
| UdpNAET |
cd01555 |
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ... |
12-412 |
0e+00 |
|
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.
Pssm-ID: 238796 Cd Length: 400 Bit Score: 593.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 12 LTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTyKKDENAVVVDATKTLNEEAPYEYV 91
Cdd:cd01555 1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVE-FEGENTLVIDASNINSTEAPYELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 92 SKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSIHLDFPSVGATQ 171
Cdd:cd01555 79 RKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 172 NIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRG 251
Cdd:cd01555 159 NIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 252 DIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLTANGHKVVTETV 330
Cdd:cd01555 239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 331 FENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELTHLDRGYVDLHGKLK 410
Cdd:cd01555 319 FENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398
|
..
gi 612660555 411 QL 412
Cdd:cd01555 399 AL 400
|
|
| murA |
TIGR01072 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and ... |
1-418 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 162190 [Multi-domain] Cd Length: 416 Bit Score: 583.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYkkDENAVVVDATK 80
Cdd:TIGR01072 1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLT-DEPVTLTNVPDLSDVKTTLDLLRNLGARVER--DNNTLEINTPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:TIGR01072 78 INSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLT 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 320 ANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELTHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
|
410
....*....|....*....
gi 612660555 400 RGYVDLHGKLKQLGADIER 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
|
|
| PRK12830 |
PRK12830 |
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed |
1-421 |
0e+00 |
|
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
Pssm-ID: 183779 Cd Length: 417 Bit Score: 518.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKKDEnaVVVDATK 80
Cdd:PRK12830 1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILA-DGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDT--LEIDPTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAkDGLKGTSI 160
Cdd:PRK12830 78 IQSMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKA-DELKGAHI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK12830 157 YLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELEYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK12830 237 TYMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELTHLDR 400
Cdd:PRK12830 317 NGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDR 396
|
410 420
....*....|....*....|.
gi 612660555 401 GYVDLHGKLKQLGADIERIND 421
Cdd:PRK12830 397 GYSNIIEKLKALGADIWREED 417
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
7-409 |
2.82e-109 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 327.72 E-value: 2.82e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 7 KGGNKLTGEVKVEG-AKNAVLPILTASLLASdkPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEE 85
Cdd:pfam00275 1 TGGSRLSGEVKIPGsKSNSHRALILAALAAG--ESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 86 APYEYVSKMRASILVMGPLLARLGHAI--VALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAK---DGLKGTSI 160
Cdd:pfam00275 79 APEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDT-ITINGVESLHGVEHAIIPDRIEA 239
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 240 GTLLIAGAITRGDIFVRGAIKEHM---ASLVYKLEEMGVELEYQEDG-IRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMM 314
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDAdIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 315 ALLLTANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSA-KLEGKSQLQGAQVKAT-DLRAAAALILAGLVADGKTSV 392
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETII 398
|
410
....*....|....*..
gi 612660555 393 TELTHLDRGYVDLHGKL 409
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
12-412 |
5.96e-77 |
|
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: 244.82 E-value: 5.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 12 LTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEEA-PYEY 90
Cdd:cd01554 1 LHGIIRVPGDKSISHRSLIFASLA-EGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQnALNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 91 VSKMRASILVMGPLLARLGHaiVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAK--DGLKGTSIHLD-FPSV 167
Cdd:cd01554 80 GNSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLkgGKNLGPIHYEDpIASA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 168 GATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGA 247
Cdd:cd01554 158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 248 ITRGDIFVRGA-IKEHMASLVYKLEEMGVELEYQEDGIRVRAeGDLQPVDIKTLPHPgFPTDMQSQMMALLLTANGHKVV 326
Cdd:cd01554 238 IAPGRLVLQNVgINETRTGIIDVLRAMGAKIEIGEDTISVES-SDLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 327 TETVF------ENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKAT-DLRAAAALILAGLVADGKTSVTELTHLD 399
Cdd:cd01554 316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
|
410
....*....|...
gi 612660555 400 RGYVDLHGKLKQL 412
Cdd:cd01554 396 TSYPSFFDDLESL 408
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
1-369 |
9.35e-15 |
|
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: 75.51 E-value: 9.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAK---NAVLpiLTASLlaSDKPSKLVNvPALS-DVETINNVLTTLNADVTYKKDENAVVV 76
Cdd:COG0128 1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEGESTIRN-LLESdDTLATLEALRALGAEIEELDGGTLRVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 77 DATKTLNEEAPYEYV----SKMRasiLVMGpLLArLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGN-----I 147
Cdd:COG0128 76 GVGGGLKEPDAVLDCgnsgTTMR---LLTG-LLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGylpltI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 148 YANakdGLKGTSIHLdfPSVGATQ---NIIMAASLAKGKTLIENAAKEPEIVdlanYIN-------EMGGRITGAGTDTI 217
Cdd:COG0128 151 RGG---PLKGGEYEI--PGSASSQfksALLLAGPLAEGGLEITVTGELESKP----YRDhtermlrAFGVEVEVEGYRRF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 218 TINGVESLHGVEHAIIPDRIEAGTLLIAGAITRGDIFVRGAIKEHM---ASLVYKLEEMGVELEYQEDGIRVRAeGDLQP 294
Cdd:COG0128 222 TVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITVRG-SPLKG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 295 VDIktlphPG------FPTdmqsqMMALLLTANGhkvvtETVFEN----RF--------MhVAEFKRMNANINVEGRSAK 356
Cdd:COG0128 301 IDI-----DLsdipdeAPT-----LAVLAAFAEG-----TTRIRGaaelRVkesdriaaM-ATELRKLGADVEETEDGLI 364
|
410
....*....|...
gi 612660555 357 LEGKSQLQGAQVK 369
Cdd:COG0128 365 IEGGPKLKGAEVD 377
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
12-297 |
3.64e-14 |
|
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: 73.75 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 12 LTGEVKVEGAKN----AvlpILTASLlaSDKPSKLVNvPALSDvetinNVLTTLNA----DVTYKKDENAVVVDATKTLN 83
Cdd:cd01556 1 LSGEITVPGSKSishrA---LLLAAL--AEGESRIEN-LLDSD-----DTLATLEAlralGAKIEEEGGTVEIVGGGGLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 84 EEAPYE-YV----SKMRasiLVMGpLLARLGHAIVaLPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDG--LK 156
Cdd:cd01556 70 LPPEAVlDCgnsgTTMR---LLTG-LLALQGGDSV-LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGggLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 157 GTSIHLDFPS----VGAtqnIIMAASLAKGKTLIENAAKEPEI-VDL-ANYINEMGGRITGAGTDTITINGVESLHGVEH 230
Cdd:cd01556 145 GGEVEIPGAVssqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEY 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612660555 231 AIIPDRIEAGTLLIAGAITRGDIFVRGAIKEHMASLVYK-LEEMGVELEY-QEDGIRVRAEGDLQPVDI 297
Cdd:cd01556 222 TVEGDASSAAFFLAAAAITGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIgNEDTVVVESGGKLKGIDI 290
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
2-299 |
5.28e-14 |
|
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: 73.08 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 2 DKIVIKGGNKLTGEVKVEgAKNA--VLPILTASLLASDKPSKLVNVPALSD--VETINNVLTTLNADVTYKKDENA--VV 75
Cdd:TIGR01356 56 EVAVIEGVGGKEPQAELD-LGNSgtTARLLTGVLALADGEVVLTGDESLRKrpMGRLVDALRQLGAEISSLEGGGSlpLT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 76 VDATKTLNeeapYEYVSKMRAS-----ILVMGPLLARLGHAIVALPggcaIGSRP-IEQHIKGFEALGAEIHLENGN--- 146
Cdd:TIGR01356 135 ISGPLPGG----IVYISGSASSqyksaLLLAAPALQAVGITIVGEP----LKSRPyIEITLDLLGSFGVEVERSDGRkiv 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 147 IYANAKDGLKGTSIHLDFPSvgATQnIIMAASLAKGKTLIENAAKEPEIVD--LANYINEMGGRITgAGTDTITINGVES 224
Cdd:TIGR01356 207 VPGGQKYGPQGYDVPGDYSS--AAF-FLAAAAITGGRVTLENLGINPTQGDkaIIIVLEEMGADIE-VEEDDLIVEGASG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 225 LHGVEHAI--IPDriEAGTLLIAGAITRGDIFVRGA----IKE--HMASLVYKLEEMGVELEYQEDGIRVRAEGDLQPVD 296
Cdd:TIGR01356 283 LKGIKIDMddMID--ELPTLAVLAAFAEGVTRITGAeelrVKEsdRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAV 360
|
...
gi 612660555 297 IKT 299
Cdd:TIGR01356 361 VDT 363
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
234-346 |
2.52e-11 |
|
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: 62.68 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 234 PDRIEAGTLLIAGAITRGDIFVRGA--------IKEHMASLVYKLEEMG----VELEYQEDGIRVRAeGDLQPVDIKTLP 301
Cdd:cd01553 8 GGGQILRSFLVLAAISGGPITVTGIrpdrakpgLLRQHLTFLKALEKICgatvEGGELGSDRISFRP-GTVRGGDVRFAI 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 612660555 302 HP-GFPTDMQSQMMALLLTANGHKVVTETVF----------ENRFMHVAEFKRMNA 346
Cdd:cd01553 87 GSaGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGA 142
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
58-299 |
1.52e-10 |
|
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: 62.57 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 58 LTTLNADVTYKKDENAVVVDATKTLnEEAPYE--------YVSkmraSILVMGPLLArlGHAIVALPggcAIGSRP-IEQ 128
Cdd:cd01556 119 LRQLGAEIEGREGGGYPPLIGGGGL-KGGEVEipgavssqFKS----ALLLAAPLAE--GPTTIIIG---ELESKPyIDH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 129 HIKGFEALGAEIHLENGN-IYANAKDGLKGTSIHL--DFPSVGAtqnIIMAASLAKGKTLIENAAKEPEIVDLANYINEM 205
Cdd:cd01556 189 TERMLRAFGAEVEVDGYRtITVKGGQKYKGPEYTVegDASSAAF---FLAAAAITGSEIVIKNVGLNSGDTGIIDVLKEM 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 206 GGRITGAGTDTITINGVESLHGVE--HAIIPDriEAGTLLIAGAITRGDIFVRGA----IKE--HMASLVYKLEEMGVEL 277
Cdd:cd01556 266 GADIEIGNEDTVVVESGGKLKGIDidGNDIPD--EAPTLAVLAAFAEGPTRIRNAaelrVKEsdRIAAMATELRKLGADV 343
|
250 260
....*....|....*....|...
gi 612660555 278 EYQEDGIRVRA-EGDLQPVDIKT 299
Cdd:cd01556 344 EETEDGLIIEGgPLKGAGVEVYT 366
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
174-421 |
6.30e-08 |
|
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: 54.32 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 174 IMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGV-ESLHGVEHAIipDRIEAGTL--LIAGAITR 250
Cdd:COG0128 29 LLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGVgGGLKEPDAVL--DCGNSGTTmrLLTGLLAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 251 GDIFVR----GAIKEH-MASLVYKLEEMGVELEYQEDG---IRVRAeGDLQPVDIKTlphpgfPTDMQSQ-----MMALL 317
Cdd:COG0128 107 QPGEVVltgdESLRKRpMGRLLDPLRQLGARIESRGGGylpLTIRG-GPLKGGEYEI------PGSASSQfksalLLAGP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 318 LTANGHKVVTETVFENRF---MHVAEFKRMNANINVEG-RSAKLEGKSQLQGAQVK--------------ATdlraaaal 379
Cdd:COG0128 180 LAEGGLEITVTGELESKPyrdHTERMLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTvpgdissaafflaaAA-------- 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 612660555 380 ilaglVADGKTSVTEL----THLDRGYVDLhgkLKQLGADIERIND 421
Cdd:COG0128 252 -----ITGSEVTVEGVglnsTQGDTGILDI---LKEMGADIEIEND 289
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
1-297 |
6.47e-07 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 51.30 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKN----AvlpILTASLlaSDKPSKLVNvPALS-DVE-TINnVLTTLNADVtykkDENAV 74
Cdd:PRK02427 2 MMMLLIIPPSPLSGTVRVPGSKSishrA---LLLAAL--AEGETTITN-LLRSeDTLaTLN-ALRALGVEI----EDDEV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 75 VVDATKTLNEEAPYEYV------SKMRasiLVMGpLLArLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGN-- 146
Cdd:PRK02427 71 VVEGVGGGGLKEPEDVLdcgnsgTTMR---LLTG-LLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGyl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 147 ---IYANAKdgLKGTSIHLDFPSvgatQNI---IMAASL-AKGKTLIEnaAKEPEI----VDL-ANYINEMGGRIT---G 211
Cdd:PRK02427 146 pltIRGGKK--GGPIEYDGPVSS----QFVkslLLLAPLfAEGDTETT--VIEPLPsrphTEItLRMLRAFGVEVEnveG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 212 AGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRG-DIFVRGAIKEHM---ASLVYKLEEMGVELEYQE------ 281
Cdd:PRK02427 218 WGYRRIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTqggKAIIDVLEKMGADIEIENeregge 297
|
330
....*....|....*...
gi 612660555 282 --DGIRVRAeGDLQPVDI 297
Cdd:PRK02427 298 pvGDIRVRS-SELKGIDI 314
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
58-287 |
3.30e-06 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 48.99 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 58 LTTLNADVTYKKDENA-VVVDATKTLNeeaPYEYVSKMrAS-----ILVMGPLLARLGHAIV---ALPggcaigSRP-IE 127
Cdd:PRK02427 130 LRQMGAKIEGRDEGYLpLTIRGGKKGG---PIEYDGPV-SSqfvksLLLLAPLFAEGDTETTviePLP------SRPhTE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 128 QHIKGFEALGAEIHLENGN----IYANAKDGLKGTSIHL--DFPSVGAtqnIIMAASLAKGKTL-IENAAKEP-----EI 195
Cdd:PRK02427 200 ITLRMLRAFGVEVENVEGWgyrrIVIKGGQRLRGQDITVpgDPSSAAF---FLAAAAITGGSEVtITNVGLNStqggkAI 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 196 VDLanyINEMGGRIT-------GAGTDTITINGvESLHGVEHAI--IPDriEAGTLLIAGAITRGDIFVRGA----IKE- 261
Cdd:PRK02427 277 IDV---LEKMGADIEieneregGEPVGDIRVRS-SELKGIDIDIpdIID--EAPTLAVLAAFAEGTTVIRNAeelrVKEt 350
|
250 260
....*....|....*....|....*..
gi 612660555 262 -HMASLVYKLEEMGVELEYQEDGIRVR 287
Cdd:PRK02427 351 dRIAAMATELRKLGAEVEETEDGLIIT 377
|
|
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
174-369 |
3.40e-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: 49.09 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 174 IMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGtDTITINGVESLHGVEHAIIpDRIEAGT----LLIAGAIT 249
Cdd:cd01556 18 LLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG-GTVEIVGGGGLGLPPEAVL-DCGNSGTtmrlLTGLLALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 250 RGDIFVRG---AIKEHMASLVYKLEEMGVELEYQEDGIR--VRAEGDLQPVDIKtlphpgFPTDMQSQ-----MMALLLt 319
Cdd:cd01556 96 GGDSVLTGdesLRKRPMGRLVDALRQLGAEIEGREGGGYppLIGGGGLKGGEVE------IPGAVSSQfksalLLAAPL- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612660555 320 ANGHKVVTETVFEN---RFMHVAEFKRMNANINVEG-RSAKLEGKSQLQGAQVK 369
Cdd:cd01556 169 AEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDGyRTITVKGGQKYKGPEYT 222
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
174-368 |
5.59e-05 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 45.13 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 174 IMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITgagTDTITINGVeslhGVEHAIIPDRI----EAGT---LLIA- 245
Cdd:PRK02427 30 LLLAALAEGETTITNLLRSEDTLATLNALRALGVEIE---DDEVVVEGV----GGGGLKEPEDVldcgNSGTtmrLLTGl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 246 GAITRGDIFVRG---AIKEHMASLVYKLEEMGVELEYQEDG---IRVRAEGDLQPVDIKtlphpgfpTDMQSQ-----MM 314
Cdd:PRK02427 103 LALQPGEVVLTGdesLRKRPMGRLLDPLRQMGAKIEGRDEGylpLTIRGGKKGGPIEYD--------GPVSSQfvkslLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612660555 315 ALLLTANGhkvVTETVFENRF-------MHVAEFKRMNANINVEG----RSAKLEGKSQLQGAQV 368
Cdd:PRK02427 175 LAPLFAEG---DTETTVIEPLpsrphteITLRMLRAFGVEVENVEgwgyRRIVIKGGQRLRGQDI 236
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
134-258 |
9.13e-05 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 44.36 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 134 EALGAEIHLENGNIYANAKDG-------LKGTSIhlDFPSVG-ATQNIIMAASLAKGKTLIENAA----KEPE-IVDLAN 200
Cdd:PRK02427 281 EKMGADIEIENEREGGEPVGDirvrsseLKGIDI--DIPDIIdEAPTLAVLAAFAEGTTVIRNAEelrvKETDrIAAMAT 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612660555 201 YINEMGGRITgAGTDTITINGVESLHGVE----HaiipdRIeAGTLLIAGAITRGDIFVRGA 258
Cdd:PRK02427 359 ELRKLGAEVE-ETEDGLIITGGPLAGVVDsygdH-----RI-AMAFAIAGLAAEGPVTIDDP 413
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
1-286 |
1.85e-04 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 43.58 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLASDKpSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATk 80
Cdd:PLN02338 1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGT-TVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGC- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 81 tlNEEAPYEYVSKMRASILV------MGPLLARL----GHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGN---- 146
Cdd:PLN02338 79 --GGKFPVSGDSKEDVELFLgnagtaMRPLTAAVtaagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTncpp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 147 IYANAKDGLKGTSIHLDfPSVGAT--QNIIMAASLAKGKTLIENAAKEPEI--VDLANYINEMGGRITG--AGTDTITIN 220
Cdd:PLN02338 157 VRVNAAGGLPGGKVKLS-GSISSQylTALLMAAPLALGDVEIEIVDKLISVpyVEMTLKLMERFGVSVEhsDSWDRFFIK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660555 221 GVESLHGVEHAIIPDRIEAGTLLIAGA-ITRGDIFVRGAIKEHMASLV---YKLEEMGVELEYQEDGIRV 286
Cdd:PLN02338 236 GGQKYKSPGNAYVEGDASSASYFLAGAaITGGTVTVEGCGTTSLQGDVkfaEVLEKMGAKVEWTENSVTV 305
|
|
| |
