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Conserved domains on  [gi|446280147|ref|WP_000358002|]
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MULTISPECIES: UDP-N-acetylglucosamine 1-carboxyvinyltransferase [Staphylococcus]

Protein Classification

UDP-N-acetylglucosamine 1-carboxyvinyltransferase( domain architecture ID 10793226)

UDP-N-acetylglucosamine 1-carboxyvinyltransferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan

Graphical summary

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List of domain hits

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 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFD-GNGTVTIDASN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:PRK09369  79 INNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELNHLDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDlrasaslvlaglvaEGTTIVDRIYHLDR 398
                        410
                 ....*....|....*....
gi 446280147 401 GYVDLHGKLKQLGADIERI 419
Cdd:PRK09369 399 GYERIEEKLRALGADIERV 417
 
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 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFD-GNGTVTIDASN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:PRK09369  79 INNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELNHLDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDlrasaslvlaglvaEGTTIVDRIYHLDR 398
                        410
                 ....*....|....*....
gi 446280147 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: 666.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLT-DGPVTLRNVPDLSDVRTMLELLESLGVKVERD-DGGTLTIDASN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAkDGLKGTSI 160
Cdd:COG0766   79 INSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARA-GRLKGARI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:COG0766  158 YLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:COG0766  238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELNHLDR 400
Cdd:COG0766  318 EGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDlragaalvlaglaaEGETVIDNIYHIDR 397
                        410
                 ....*....|....*....
gi 446280147 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 446280147  12 LTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTyKKDENAVVVDATKTLNEEAPYEYV 91
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVE-FEGENTLVIDASNINSTEAPYELV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  92 SKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSIHLDFPSVGATQ 171
Cdd:cd01555   79 RKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 172 NIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRG 251
Cdd:cd01555  159 NIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 252 DIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLTANGHKVVTETV 330
Cdd:cd01555  239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 331 FENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELNHLDRGYVDLHGKLK 410
Cdd:cd01555  319 FENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398

                 ..
gi 446280147 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: 584.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147    1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYkkDENAVVVDATK 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLT-DEPVTLTNVPDLSDVKTTLDLLRNLGARVER--DNNTLEINTPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:TIGR01072  78 INSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLT 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  320 ANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELNHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
                         410
                  ....*....|....*....
gi 446280147  400 RGYVDLHGKLKQLGADIER 418
Cdd:TIGR01072 398 RGYEDLEEKLRALGAKIER 416
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-409 2.15e-109

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 328.10  E-value: 2.15e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147    7 KGGNKLTGEVKVEG-AKNAVLPILTASLLASdkPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEE 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAG--ESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   86 APYEYVSKMRASILVMGPLLARLGHAI--VALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAK---DGLKGTSI 160
Cdd:pfam00275  79 APEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDT-ITINGVESLHGVEHAIIPDRIEA 239
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  240 GTLLIAGAITRGDIFVRGAIKEHM---ASLVYKLEEMGVELDYQEDG-IRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMM 314
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDAdIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  315 ALLLTANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSA-KLEGKSQLQGAQVKAT-DLRAAAALILAGLVADGKTSV 392
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETII 398
                         410
                  ....*....|....*..
gi 446280147  393 TELNHLDRGYVDLHGKL 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 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:PRK09369   1 MDKLVIEGGKPLSGEVTISGAKNAALPILAASLLA-EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFD-GNGTVTIDASN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:PRK09369  79 INNTEAPYELVKKMRASILVLGPLLARFGEAKVSLPGGCAIGARPVDLHLKGLEALGAEIEIEHGYVEAKADGRLKGAHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK09369 159 VLDFPSVGATENILMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKISGAGTDTITIEGVERLHGAEHTVIPDRIEAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK09369 239 TFLVAAAITGGDVTIRGARPEHLEAVLAKLREAGAEIEEGEDGIRVDMPGRLKAVDIKTAPYPGFPTDMQAQFMALLTQA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELNHLDR 400
Cdd:PRK09369 319 EGTSVITETIFENRFMHVPELIRMGADIEVDGHTAVVRGVEKLSGAPVMATDlrasaslvlaglvaEGTTIVDRIYHLDR 398
                        410
                 ....*....|....*....
gi 446280147 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: 666.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKkDENAVVVDATK 80
Cdd:COG0766    1 MDKLIIEGGKPLSGEVRISGAKNAALPILAAALLT-DGPVTLRNVPDLSDVRTMLELLESLGVKVERD-DGGTLTIDASN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAkDGLKGTSI 160
Cdd:COG0766   79 INSTEAPYELVRKMRASILVLGPLLARFGEARVSLPGGCAIGARPIDLHLKGLEALGAEIEIEHGYIEARA-GRLKGARI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:COG0766  158 YLDFPSVGATENIMMAAVLAEGTTVIENAAREPEIVDLANFLNAMGAKIEGAGTDTITIEGVEKLHGAEHTVIPDRIEAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:COG0766  238 TFLVAAAITGGDVTVKNVIPEHLEAVLAKLREAGVEIEEGDDGIRVRGPGRLKAVDIKTAPYPGFPTDLQAQFMALLTQA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDlraaaalilaglvaDGKTSVTELNHLDR 400
Cdd:COG0766  318 EGTSVITETVFENRFMHVDELNRMGADIKLDGHTAIVRGVTKLSGAPVMATDlragaalvlaglaaEGETVIDNIYHIDR 397
                        410
                 ....*....|....*....
gi 446280147 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 446280147  12 LTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTyKKDENAVVVDATKTLNEEAPYEYV 91
Cdd:cd01555    1 LSGEVRISGAKNAALPILAAALLT-DEPVTLRNVPDLLDVETMIELLRSLGAKVE-FEGENTLVIDASNINSTEAPYELV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  92 SKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSIHLDFPSVGATQ 171
Cdd:cd01555   79 RKMRASILVLGPLLARFGEARVSLPGGCAIGARPVDLHLKGLEALGAKIEIEDGYVEAKAAGRLKGARIYLDFPSVGATE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 172 NIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRG 251
Cdd:cd01555  159 NIMMAAVLAEGTTVIENAAREPEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLHGAEHTVIPDRIEAGTFLVAAAITGG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 252 DIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLTANGHKVVTETV 330
Cdd:cd01555  239 DITVENVIPEHLEAVLAKLREMGAKIEIGEDGIRVDGDGgRLKAVDIETAPYPGFPTDLQAQFMALLTQAEGTSVITETI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 331 FENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELNHLDRGYVDLHGKLK 410
Cdd:cd01555  319 FENRFMHVDELNRMGADIKVEGNTAIIRGVTKLSGAPVMATDLRAGAALVLAGLAAEGETIISNIYHIDRGYERIEEKLR 398

                 ..
gi 446280147 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: 584.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147    1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYkkDENAVVVDATK 80
Cdd:TIGR01072   1 MDKLVVEGGKPLSGEVTISGAKNAALPIIAATLLT-DEPVTLTNVPDLSDVKTTLDLLRNLGARVER--DNNTLEINTPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSI 160
Cdd:TIGR01072  78 INSTEAPYELVRKMRASILVLGPLLARFGKAVVSLPGGCAIGARPVDLHLKGLKALGAEIVIEDGYVYASAKGRLVGAHI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:TIGR01072 158 VLDKVSVGATENIIMAAVLAEGTTVIENAAREPEIVDLCEFLNKMGAKITGAGSNTITIEGVEKLHGTEHSVIPDRIEAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMMALLLT 319
Cdd:TIGR01072 238 TFLVAAAITGGEITIKNVRPDHLRAVLAKLREIGAEVEVDENGIRVDMRQkRLKAVDIETLPYPGFPTDLQAQFMALLSQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  320 ANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELNHLD 399
Cdd:TIGR01072 318 AEGTSVITETVFENRFMHVDELIRMGANIKLEGNTAVIHGVEQLSGAEVMATDLRAGAALVLAGLVAEGETIVHNVYHLD 397
                         410
                  ....*....|....*....
gi 446280147  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: 517.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKKDEnaVVVDATK 80
Cdd:PRK12830   1 MEKIVINGGKPLSGEVTISGAKNSAVALIPAAILA-DGPVTLDGVPDISDVHSLVDILEELGGKVKRDGDT--LEIDPTG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 TLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAkDGLKGTSI 160
Cdd:PRK12830  78 IQSMPLPNGKVKSLRASYYFMGALLGRFKKAVVGLPGGCDLGPRPIDQHIKGFEALGAEVTNEGGAIYLKA-DELKGAHI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAG 240
Cdd:PRK12830 157 YLDVVSVGATINIMLAAVKAKGRTVIENAAKEPEIIDVATLLNNMGANIKGAGTDVIRIEGVDELHGCRHTVIPDRIEAG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 241 TLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVDIKTLPHPGFPTDMQSQMMALLLTA 320
Cdd:PRK12830 237 TYMILAAACGGGVTINNVIPEHLESFIAKLEEMGVRVEVNEDSIFVEKQGNLKAVDIKTLPYPGFATDLQQPLTPLLLKA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 321 NGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELNHLDR 400
Cdd:PRK12830 317 NGRSVVTDTIYEKRFKHVDELKRMGANIKVEGRSAIITGPSKLTGAKVKATDLRAGAALVIAGLMAEGVTEITNIEHIDR 396
                        410       420
                 ....*....|....*....|.
gi 446280147 401 GYVDLHGKLKQLGADIERIND 421
Cdd:PRK12830 397 GYSNIIEKLKALGADIWREED 417
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-409 2.15e-109

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 328.10  E-value: 2.15e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147    7 KGGNKLTGEVKVEG-AKNAVLPILTASLLASdkPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEE 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGsKSNSHRALILAALAAG--ESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   86 APYEYVSKMRASILVMGPLLARLGHAI--VALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAK---DGLKGTSI 160
Cdd:pfam00275  79 APEDLVLDMGNSGTALRPLTGRLALQSgeVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKvrgLRLGGIHI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  161 HLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDT-ITINGVESLHGVEHAIIPDRIEA 239
Cdd:pfam00275 159 DGDVSSQFVTSLLMLAALLAEGTTTIENLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLPGQEYRVEGDRSSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  240 GTLLIAGAITRGDIFVRGAIKEHM---ASLVYKLEEMGVELDYQEDG-IRVRAEG-DLQPVDIKTLPHPGFPTDMQSQMM 314
Cdd:pfam00275 239 AYFLVAAAITGGTVTVENVGINSLqgdEALLEILEKMGAEITQEEDAdIVVGPPGlRGKAVDIRTAPDPAPTTAVLAAFA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  315 ALLLTANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSA-KLEGKSQLQGAQVKAT-DLRAAAALILAGLVADGKTSV 392
Cdd:pfam00275 319 EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLiIIPAVKELKGAEVDSYgDHRIAMALALAGLVAEGETII 398
                         410
                  ....*....|....*..
gi 446280147  393 TELNHLDRGYVDLHGKL 409
Cdd:pfam00275 399 DDIECTDRSFPDFEEKL 415
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-412 1.80e-76

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: 243.28  E-value: 1.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  12 LTGEVKVEGAKNAVLPILTASLLAsDKPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEEA-PYEY 90
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLA-EGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQnALNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  91 VSKMRASILVMGPLLARLGHaiVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAK--DGLKGTSIHLD-FPSV 167
Cdd:cd01554   80 GNSGTAIRLISGVLAGADFE--VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLkgGKNLGPIHYEDpIASA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 168 GATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGA 247
Cdd:cd01554  158 QVKSALMFAALLAKGETVIIEAAKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQKYVVPGDISSAAFFLVAAA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 248 ITRGDIFVRGA-IKEHMASLVYKLEEMGVELDYQEDGIRVRAeGDLQPVDIKTLPHPgFPTDMQSQMMALLLTANGHKVV 326
Cdd:cd01554  238 IAPGRLVLQNVgINETRTGIIDVLRAMGAKIEIGEDTISVES-SDLKATEICGALIP-RLIDELPIIALLALQAQGTTVI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 327 TETVF------ENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKAT-DLRAAAALILAGLVADGKTSVTELNHLD 399
Cdd:cd01554  316 KDAEElkvketDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFgDHRIGMMTALAALVADGEVELDRAEAIN 395
                        410
                 ....*....|...
gi 446280147 400 RGYVDLHGKLKQL 412
Cdd:cd01554  396 TSYPSFFDDLESL 408
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-369 2.51e-14

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: 74.35  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   1 MDKIVIKGGNKLTGEVKVEGAK---NAVLpiLTASLlaSDKPSKLVNvPALS-DVETINNVLTTLNADVTYKKDENAVVV 76
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKsisHRAL--LLAAL--AEGESTIRN-LLESdDTLATLEALRALGAEIEELDGGTLRVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  77 DATKTLNEEAPYEYV----SKMRasiLVMGpLLArLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGN-----I 147
Cdd:COG0128   76 GVGGGLKEPDAVLDCgnsgTTMR---LLTG-LLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGylpltI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 148 YANakdGLKGTSIHLdfPSVGATQ---NIIMAASLAKGKTLIENAAKEPEIVdlanYIN-------EMGGRITGAGTDTI 217
Cdd:COG0128  151 RGG---PLKGGEYEI--PGSASSQfksALLLAGPLAEGGLEITVTGELESKP----YRDhtermlrAFGVEVEVEGYRRF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 218 TINGVESLHGVEHAIIPDRIEAGTLLIAGAITRGDIFVRGAIKEHM---ASLVYKLEEMGVELDYQEDGIRVRAeGDLQP 294
Cdd:COG0128  222 TVPGGQRYRPGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTqgdTGILDILKEMGADIEIENDGITVRG-SPLKG 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 295 VDIktlphPG------FPTdmqsqMMALLLTANGhkvvtETVFEN----RF--------MhVAEFKRMNANINVEGRSAK 356
Cdd:COG0128  301 IDI-----DLsdipdeAPT-----LAVLAAFAEG-----TTRIRGaaelRVkesdriaaM-ATELRKLGADVEETEDGLI 364
                        410
                 ....*....|...
gi 446280147 357 LEGKSQLQGAQVK 369
Cdd:COG0128  365 IEGGPKLKGAEVD 377
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
2-299 9.59e-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: 72.31  E-value: 9.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147    2 DKIVIKGGNKLTGEVKVEgAKNA--VLPILTASLLASDKPSKLVNVPALSD--VETINNVLTTLNADVTYKKDENA--VV 75
Cdd:TIGR01356  56 EVAVIEGVGGKEPQAELD-LGNSgtTARLLTGVLALADGEVVLTGDESLRKrpMGRLVDALRQLGAEISSLEGGGSlpLT 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   76 VDATKTLNeeapYEYVSKMRAS-----ILVMGPLLARLGHAIVALPggcaIGSRP-IEQHIKGFEALGAEIHLENGN--- 146
Cdd:TIGR01356 135 ISGPLPGG----IVYISGSASSqyksaLLLAAPALQAVGITIVGEP----LKSRPyIEITLDLLGSFGVEVERSDGRkiv 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  147 IYANAKDGLKGTSIHLDFPSvgATQnIIMAASLAKGKTLIENAAKEPEIVD--LANYINEMGGRITgAGTDTITINGVES 224
Cdd:TIGR01356 207 VPGGQKYGPQGYDVPGDYSS--AAF-FLAAAAITGGRVTLENLGINPTQGDkaIIIVLEEMGADIE-VEEDDLIVEGASG 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  225 LHGVEHAI--IPDriEAGTLLIAGAITRGDIFVRGA----IKE--HMASLVYKLEEMGVELDYQEDGIRVRAEGDLQPVD 296
Cdd:TIGR01356 283 LKGIKIDMddMID--ELPTLAVLAAFAEGVTRITGAeelrVKEsdRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAV 360

                  ...
gi 446280147  297 IKT 299
Cdd:TIGR01356 361 VDT 363
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-297 9.93e-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: 72.20  E-value: 9.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  12 LTGEVKVEGAKN----AvlpILTASLlaSDKPSKLVNvPALSDvetinNVLTTLNA----DVTYKKDENAVVVDATKTLN 83
Cdd:cd01556    1 LSGEITVPGSKSishrA---LLLAAL--AEGESRIEN-LLDSD-----DTLATLEAlralGAKIEEEGGTVEIVGGGGLG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  84 EEAPYE-YV----SKMRasiLVMGpLLARLGHAIVaLPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDG--LK 156
Cdd:cd01556   70 LPPEAVlDCgnsgTTMR---LLTG-LLALQGGDSV-LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGggLK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 157 GTSIHLDFPS----VGAtqnIIMAASLAKGKTLIENAAKEPEI-VDL-ANYINEMGGRITGAGTDTITINGVESLHGVEH 230
Cdd:cd01556  145 GGEVEIPGAVssqfKSA---LLLAAPLAEGPTTIIIGELESKPyIDHtERMLRAFGAEVEVDGYRTITVKGGQKYKGPEY 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446280147 231 AIIPDRIEAGTLLIAGAITRGDIFVRGAIKEHMASLVYK-LEEMGVELDY-QEDGIRVRAEGDLQPVDI 297
Cdd:cd01556  222 TVEGDASSAAFFLAAAAITGSEIVIKNVGLNSGDTGIIDvLKEMGADIEIgNEDTVVVESGGKLKGIDI 290
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
234-346 5.27e-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: 61.91  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 234 PDRIEAGTLLIAGAITRGDIFVRGA--------IKEHMASLVYKLEEMG----VELDYQEDGIRVRAeGDLQPVDIKTLP 301
Cdd:cd01553    8 GGGQILRSFLVLAAISGGPITVTGIrpdrakpgLLRQHLTFLKALEKICgatvEGGELGSDRISFRP-GTVRGGDVRFAI 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446280147 302 HP-GFPTDMQSQMMALLLTANGHKVVTETVF----------ENRFMHVAEFKRMNA 346
Cdd:cd01553   87 GSaGSCTDVLQTILPLLLFAKGPTRLTVTGGtdnpsappadFIRFVLEPELAKIGA 142
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
58-299 4.35e-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: 61.03  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  58 LTTLNADVTYKKDENAVVVDATKTLnEEAPYE--------YVSkmraSILVMGPLLArlGHAIVALPggcAIGSRP-IEQ 128
Cdd:cd01556  119 LRQLGAEIEGREGGGYPPLIGGGGL-KGGEVEipgavssqFKS----ALLLAAPLAE--GPTTIIIG---ELESKPyIDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 129 HIKGFEALGAEIHLENGN-IYANAKDGLKGTSIHL--DFPSVGAtqnIIMAASLAKGKTLIENAAKEPEIVDLANYINEM 205
Cdd:cd01556  189 TERMLRAFGAEVEVDGYRtITVKGGQKYKGPEYTVegDASSAAF---FLAAAAITGSEIVIKNVGLNSGDTGIIDVLKEM 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 206 GGRITGAGTDTITINGVESLHGVE--HAIIPDriEAGTLLIAGAITRGDIFVRGA----IKE--HMASLVYKLEEMGVEL 277
Cdd:cd01556  266 GADIEIGNEDTVVVESGGKLKGIDidGNDIPD--EAPTLAVLAAFAEGPTRIRNAaelrVKEsdRIAAMATELRKLGADV 343
                        250       260
                 ....*....|....*....|...
gi 446280147 278 DYQEDGIRVRA-EGDLQPVDIKT 299
Cdd:cd01556  344 EETEDGLIIEGgPLKGAGVEVYT 366
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
174-421 1.89e-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: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 174 IMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGV-ESLHGVEHAIipDRIEAGTL--LIAGAITR 250
Cdd:COG0128   29 LLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDGGTLRVTGVgGGLKEPDAVL--DCGNSGTTmrLLTGLLAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 251 GDIFVR----GAIKEH-MASLVYKLEEMGVELDYQEDG---IRVRAeGDLQPVDIKTlphpgfPTDMQSQ-----MMALL 317
Cdd:COG0128  107 QPGEVVltgdESLRKRpMGRLLDPLRQLGARIESRGGGylpLTIRG-GPLKGGEYEI------PGSASSQfksalLLAGP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 318 LTANGHKVVTETVFENRF---MHVAEFKRMNANINVEG-RSAKLEGKSQLQGAQVK--------------ATdlraaaal 379
Cdd:COG0128  180 LAEGGLEITVTGELESKPyrdHTERMLRAFGVEVEVEGyRRFTVPGGQRYRPGDYTvpgdissaafflaaAA-------- 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446280147 380 ilaglVADGKTSVTELN----HLDRGYVDLhgkLKQLGADIERIND 421
Cdd:COG0128  252 -----ITGSEVTVEGVGlnstQGDTGILDI---LKEMGADIEIEND 289
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-297 2.00e-06

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 49.76  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   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 446280147  75 VVDATKTLNEEAPYEYV------SKMRasiLVMGpLLArLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGN-- 146
Cdd:PRK02427  71 VVEGVGGGGLKEPEDVLdcgnsgTTMR---LLTG-LLA-LQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGyl 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 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 446280147 212 AGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRG-DIFVRGAIKEHM---ASLVYKLEEMGVELDYQE------ 281
Cdd:PRK02427 218 WGYRRIVIKGGQRLRGQDITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTqggKAIIDVLEKMGADIEIENeregge 297
                        330
                 ....*....|....*...
gi 446280147 282 --DGIRVRAeGDLQPVDI 297
Cdd:PRK02427 298 pvGDIRVRS-SELKGIDI 314
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
174-369 3.03e-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: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 174 IMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGtDTITINGVESLHGVEHAIIpDRIEAGT----LLIAGAIT 249
Cdd:cd01556   18 LLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEG-GTVEIVGGGGLGLPPEAVL-DCGNSGTtmrlLTGLLALQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 250 RGDIFVRG---AIKEHMASLVYKLEEMGVELDYQEDGIR--VRAEGDLQPVDIKtlphpgFPTDMQSQ-----MMALLLt 319
Cdd:cd01556   96 GGDSVLTGdesLRKRPMGRLVDALRQLGAEIEGREGGGYppLIGGGGLKGGEVE------IPGAVSSQfksalLLAAPL- 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446280147 320 ANGHKVVTETVFEN---RFMHVAEFKRMNANINVEG-RSAKLEGKSQLQGAQVK 369
Cdd:cd01556  169 AEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDGyRTITVKGGQKYKGPEYT 222
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
58-287 1.43e-05

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 47.06  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  58 LTTLNADVTYKKDENA-VVVDATKTLNeeaPYEYVSKMrAS-----ILVMGPLLARLGHAIV---ALPggcaigSRP-IE 127
Cdd:PRK02427 130 LRQMGAKIEGRDEGYLpLTIRGGKKGG---PIEYDGPV-SSqfvksLLLLAPLFAEGDTETTviePLP------SRPhTE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 128 QHIKGFEALGAEIHLENGN----IYANAKDGLKGTSIHL--DFPSVGAtqnIIMAASLAKGKTL-IENAAKEP-----EI 195
Cdd:PRK02427 200 ITLRMLRAFGVEVENVEGWgyrrIVIKGGQRLRGQDITVpgDPSSAAF---FLAAAAITGGSEVtITNVGLNStqggkAI 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 196 VDLanyINEMGGRIT-------GAGTDTITINGvESLHGVEHAI--IPDriEAGTLLIAGAITRGDIFVRGA----IKE- 261
Cdd:PRK02427 277 IDV---LEKMGADIEieneregGEPVGDIRVRS-SELKGIDIDIpdIID--EAPTLAVLAAFAEGTTVIRNAeelrVKEt 350
                        250       260
                 ....*....|....*....|....*..
gi 446280147 262 -HMASLVYKLEEMGVELDYQEDGIRVR 287
Cdd:PRK02427 351 dRIAAMATELRKLGAEVEETEDGLIIT 377
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
174-368 4.94e-05

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 45.13  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 174 IMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITgagTDTITINGVeslhGVEHAIIPDRI----EAGT---LLIA- 245
Cdd:PRK02427  30 LLLAALAEGETTITNLLRSEDTLATLNALRALGVEIE---DDEVVVEGV----GGGGLKEPEDVldcgNSGTtmrLLTGl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 246 GAITRGDIFVRG---AIKEHMASLVYKLEEMGVELDYQEDG---IRVRAEGDLQPVDIKtlphpgfpTDMQSQ-----MM 314
Cdd:PRK02427 103 LALQPGEVVLTGdesLRKRPMGRLLDPLRQMGAKIEGRDEGylpLTIRGGKKGGPIEYD--------GPVSSQfvkslLL 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446280147 315 ALLLTANG--HKVVTETV-----FEnrfMHVAEFKRMNANINVEG----RSAKLEGKSQLQGAQV 368
Cdd:PRK02427 175 LAPLFAEGdtETTVIEPLpsrphTE---ITLRMLRAFGVEVENVEgwgyRRIVIKGGQRLRGQDI 236
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
134-258 8.51e-05

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 44.36  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 134 EALGAEIHLENGNIYANAKDG-------LKGTSIhlDFPSVG-ATQNIIMAASLAKGKTLIENAA----KEPE-IVDLAN 200
Cdd:PRK02427 281 EKMGADIEIENEREGGEPVGDirvrsseLKGIDI--DIPDIIdEAPTLAVLAAFAEGTTVIRNAEelrvKETDrIAAMAT 358
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446280147 201 YINEMGGRITgAGTDTITINGVESLHGVE----HaiipdRIeAGTLLIAGAITRGDIFVRGA 258
Cdd:PRK02427 359 ELRKLGAEVE-ETEDGLIITGGPLAGVVDsygdH-----RI-AMAFAIAGLAAEGPVTIDDP 413
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
1-286 5.56e-04

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 42.04  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147   1 MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLASDKpSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATk 80
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGT-TVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGC- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147  81 tlNEEAPYEYVSKMRASILV------MGPLLARL----GHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGN---- 146
Cdd:PLN02338  79 --GGKFPVSGDSKEDVELFLgnagtaMRPLTAAVtaagGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTncpp 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 147 IYANAKDGLKGTSIHLDfPSVGAT--QNIIMAASLAKGKTLIENAAKEPEI--VDLANYINEMGGRITG--AGTDTITIN 220
Cdd:PLN02338 157 VRVNAAGGLPGGKVKLS-GSISSQylTALLMAAPLALGDVEIEIVDKLISVpyVEMTLKLMERFGVSVEhsDSWDRFFIK 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446280147 221 GVESLHGVEHAIIPDRIEAGTLLIAGA-ITRGDIFVRGAIKEHMASLV---YKLEEMGVELDYQEDGIRV 286
Cdd:PLN02338 236 GGQKYKSPGNAYVEGDASSASYFLAGAaITGGTVTVEGCGTTSLQGDVkfaEVLEKMGAKVEWTENSVTV 305
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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