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Conserved domains on  [gi|42571811|ref|NP_973996|]
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RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta [Arabidopsis thaliana]

Protein Classification

PLN02338 family protein( domain architecture ID 11476666)

PLN02338 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
22-489 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase


:

Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 877.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   22 ASEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVETHSENNRAVVEGCGG 101
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  102 VFPASIDSKSDIELYLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVN 181
Cdd:PLN02338  81 KFPVSGDSKEDVELFLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  182 ANGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESWDRFFVKGGQKY 261
Cdd:PLN02338 161 AAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDSWDRFFIKGGQKY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  262 KSPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRDAFGMRHLRA 341
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  342 IDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGAT 421
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRK-------------------------LGAT 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571811  422 VEEGSDYCVITPPKKVKPAEIDTYDDHRMAMAFSLAACADVPITINDPGCTRKTFPDYFQVLERITKH 489
Cdd:PLN02338 376 VEEGPDYCIITPPKKLKPAEIDTYDDHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAKH 443
 
Name Accession Description Interval E-value
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
22-489 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 877.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   22 ASEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVETHSENNRAVVEGCGG 101
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  102 VFPASIDSKSDIELYLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVN 181
Cdd:PLN02338  81 KFPVSGDSKEDVELFLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  182 ANGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESWDRFFVKGGQKY 261
Cdd:PLN02338 161 AAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDSWDRFFIKGGQKY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  262 KSPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRDAFGMRHLRA 341
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  342 IDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGAT 421
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRK-------------------------LGAT 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571811  422 VEEGSDYCVITPPKKVKPAEIDTYDDHRMAMAFSLAACADVPITINDPGCTRKTFPDYFQVLERITKH 489
Cdd:PLN02338 376 VEEGPDYCIITPPKKLKPAEIDTYDDHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAKH 443
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
23-486 2.08e-180

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: 511.94  E-value: 2.08e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  23 SEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEtHSENNRAVVEGCGGV 102
Cdd:COG0128   2 SSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIE-ELDGGTLRVTGVGGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 103 FPASidsksDIELYLGNAGTAMRPLTAAvtAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTlGTNCPPVRVNA 182
Cdd:COG0128  81 LKEP-----DAVLDCGNSGTTMRLLTGL--LALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESR-GGGYLPLTIRG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 183 nGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSEsWDRFFVKGGQKYK 262
Cdd:COG0128 153 -GPLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEG-YRRFTVPGGQRYR 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 263 sPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGpsrdafgmRHLRAI 342
Cdd:COG0128 231 -PGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRG--------SPLKGI 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 343 DVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATV 422
Cdd:COG0128 302 DIDLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRK-------------------------LGADV 356
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571811 423 EEGSDYCVITPPKKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERI 486
Cdd:COG0128 357 EETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAEGPVTIDDAECVAKSFPDFFELLESL 421
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
35-489 2.80e-178

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: 506.04  E-value: 2.80e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811    35 GLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEthSENNRAVVEGCGGVFPasidsksDIE 114
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIE--DGGEVAVIEGVGGKEP-------QAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   115 LYLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNanGGLPGGKVKLS 194
Cdd:TIGR01356  72 LDLGNSGTTARLLTGVLALADGE--VVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTIS--GPLPGGIVYIS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   195 GSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESwDRFFVKGGQKYKSPGnAYVEGDAS 274
Cdd:TIGR01356 148 GSASSQYKSALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDG-RKIVVPGGQKYGPQG-YDVPGDYS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   275 SASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRdafgmrhLRAIDVNMNKMPDVAM 354
Cdd:TIGR01356 226 SAAFFLAAAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASG-------LKGIKIDMDDMIDELP 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   355 TLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEEGSDYCVITPP 434
Cdd:TIGR01356 299 TLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRK-------------------------LGVDVEEFEDGLYIRGK 353
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571811   435 KKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERITKH 489
Cdd:TIGR01356 354 KELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
33-486 2.57e-164

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: 470.50  E-value: 2.57e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  33 ISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEthSENNRAVVEGCGGVFPasidsKSD 112
Cdd:cd01556   1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIE--EEGGTVEIVGGGGLGL-----PPE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 113 IELYLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNanGGLPGGKVK 192
Cdd:cd01556  74 AVLDCGNSGTTMRLLTGLLALQGGD--SVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGG--GGLKGGEVE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 193 LSGSISSQYLTALLMAAPLALGDVEIEIVdKLISVPYVEMTLKLMERFGVSAEHSEsWDRFFVKGGQKYKSPgNAYVEGD 272
Cdd:cd01556 150 IPGAVSSQFKSALLLAAPLAEGPTTIIIG-ELESKPYIDHTERMLRAFGAEVEVDG-YRTITVKGGQKYKGP-EYTVEGD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 273 ASSASYFLAGAAITGETVTVEGCGTTSlqGDVKFAEVLEKMGCKVSWT-ENSVTVTGPsrdafgmRHLRAIDVNMNKMPD 351
Cdd:cd01556 227 ASSAAFFLAAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGnEDTVVVESG-------GKLKGIDIDGNDIPD 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 352 VAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEEGSDYCVI 431
Cdd:cd01556 298 EAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRK-------------------------LGADVEETEDGLII 352
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571811 432 TP-PKKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERI 486
Cdd:cd01556 353 EGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPECVAKSFPNFFEDLESL 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
28-483 1.03e-147

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 428.64  E-value: 1.03e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811    28 QPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILG-LNVETHSENNRAVVEGCGGVFPAS 106
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGaEIIKLDDEKSVVIVEGLGGSFEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   107 idskSDIELYLGNAGTAMRPLTAAvtAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNangGL 186
Cdd:pfam00275  81 ----EDLVLDMGNSGTALRPLTGR--LALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVR---GL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   187 PGGKVKLSGSISSQYLTALLMAAPLALGDvEIEIVDkLISVPYVEMTLKLMERFGVSAEHSESWDRFFVKGGQKYKSpGN 266
Cdd:pfam00275 152 RLGGIHIDGDVSSQFVTSLLMLAALLAEG-TTTIEN-LASEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPG-QE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   267 AYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSrdafgmrHLRAIDVNM 346
Cdd:pfam00275 229 YRVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPP-------GLRGKAVDI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   347 NKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEEGS 426
Cdd:pfam00275 302 RTAPDPAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRR-------------------------LGADVEELP 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571811   427 DYCVITPP-KKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVL 483
Cdd:pfam00275 357 DGLIIIPAvKELKGAEVDSYGDHRIAMALALAGLvAEGETIIDDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
22-489 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 877.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   22 ASEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVETHSENNRAVVEGCGG 101
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  102 VFPASIDSKSDIELYLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVN 181
Cdd:PLN02338  81 KFPVSGDSKEDVELFLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  182 ANGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESWDRFFVKGGQKY 261
Cdd:PLN02338 161 AAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDSWDRFFIKGGQKY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  262 KSPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRDAFGMRHLRA 341
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTGPPRDAFGGKHLKA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  342 IDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGAT 421
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRK-------------------------LGAT 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571811  422 VEEGSDYCVITPPKKVKPAEIDTYDDHRMAMAFSLAACADVPITINDPGCTRKTFPDYFQVLERITKH 489
Cdd:PLN02338 376 VEEGPDYCIITPPKKLKPAEIDTYDDHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAKH 443
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
27-488 0e+00

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 531.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   27 LQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVETHSENnrAVVEGCGGVFPAS 106
Cdd:PRK11860   9 LPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDT--YRITGLGGQFPVK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  107 idsksDIELYLGNAGTAMRPLTAAVTAAGGnaSYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNANGGL 186
Cdd:PRK11860  87 -----QADLFLGNAGTAMRPLTAALALLGG--EYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  187 PGGKVKLSGSISSQYLTALLMAAPLALG-DVEIEIVDKLISVPYVEMTLKLMERFGVSAEHsESWDRFFVKGGQKYKSPG 265
Cdd:PRK11860 160 LDAPIRVRGDVSSQFLTALLMALPLVARrDITIEVVGELISKPYIEITLNLLARFGIAVQR-EGWQRFTIPAGSRYRSPG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  266 NAYVEGDASSASYFLAGAAI-TGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRDafgmrhLRAIDV 344
Cdd:PRK11860 239 EIHVEGDASSASYFIAAGAIaGGAPVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAWP------LKAIDL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  345 NMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEE 424
Cdd:PRK11860 313 DCNHIPDAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRK-------------------------LGATVEE 367
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571811  425 GSDYCVITPPKKV---KPAEIDTYDDHRMAMAFSLAA--CADVPITINDPGCTRKTFPDYFQVLERITK 488
Cdd:PRK11860 368 GADYIRVTPPAQAadwKAAAIHTYDDHRMAMCFSLAAfnPAGLPVRINDPKCVAKTFPDYFEALFSVAQ 436
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
23-486 2.08e-180

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: 511.94  E-value: 2.08e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  23 SEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEtHSENNRAVVEGCGGV 102
Cdd:COG0128   2 SSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIE-ELDGGTLRVTGVGGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 103 FPASidsksDIELYLGNAGTAMRPLTAAvtAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTlGTNCPPVRVNA 182
Cdd:COG0128  81 LKEP-----DAVLDCGNSGTTMRLLTGL--LALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESR-GGGYLPLTIRG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 183 nGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSEsWDRFFVKGGQKYK 262
Cdd:COG0128 153 -GPLKGGEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEG-YRRFTVPGGQRYR 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 263 sPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGpsrdafgmRHLRAI 342
Cdd:COG0128 231 -PGDYTVPGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRG--------SPLKGI 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 343 DVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATV 422
Cdd:COG0128 302 DIDLSDIPDEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRK-------------------------LGADV 356
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571811 423 EEGSDYCVITPPKKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERI 486
Cdd:COG0128 357 EETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAEGPVTIDDAECVAKSFPDFFELLESL 421
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
35-489 2.80e-178

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: 506.04  E-value: 2.80e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811    35 GLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEthSENNRAVVEGCGGVFPasidsksDIE 114
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIE--DGGEVAVIEGVGGKEP-------QAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   115 LYLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNanGGLPGGKVKLS 194
Cdd:TIGR01356  72 LDLGNSGTTARLLTGVLALADGE--VVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTIS--GPLPGGIVYIS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   195 GSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESwDRFFVKGGQKYKSPGnAYVEGDAS 274
Cdd:TIGR01356 148 GSASSQYKSALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDG-RKIVVPGGQKYGPQG-YDVPGDYS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   275 SASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSRdafgmrhLRAIDVNMNKMPDVAM 354
Cdd:TIGR01356 226 SAAFFLAAAAITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGASG-------LKGIKIDMDDMIDELP 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   355 TLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEEGSDYCVITPP 434
Cdd:TIGR01356 299 TLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRK-------------------------LGVDVEEFEDGLYIRGK 353
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571811   435 KKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERITKH 489
Cdd:TIGR01356 354 KELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAKSFPSFFDVLERLGAN 409
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
33-486 2.57e-164

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: 470.50  E-value: 2.57e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  33 ISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEthSENNRAVVEGCGGVFPasidsKSD 112
Cdd:cd01556   1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIE--EEGGTVEIVGGGGLGL-----PPE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 113 IELYLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNanGGLPGGKVK 192
Cdd:cd01556  74 AVLDCGNSGTTMRLLTGLLALQGGD--SVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGG--GGLKGGEVE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 193 LSGSISSQYLTALLMAAPLALGDVEIEIVdKLISVPYVEMTLKLMERFGVSAEHSEsWDRFFVKGGQKYKSPgNAYVEGD 272
Cdd:cd01556 150 IPGAVSSQFKSALLLAAPLAEGPTTIIIG-ELESKPYIDHTERMLRAFGAEVEVDG-YRTITVKGGQKYKGP-EYTVEGD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 273 ASSASYFLAGAAITGETVTVEGCGTTSlqGDVKFAEVLEKMGCKVSWT-ENSVTVTGPsrdafgmRHLRAIDVNMNKMPD 351
Cdd:cd01556 227 ASSAAFFLAAAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGnEDTVVVESG-------GKLKGIDIDGNDIPD 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 352 VAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEEGSDYCVI 431
Cdd:cd01556 298 EAPTLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRK-------------------------LGADVEETEDGLII 352
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571811 432 TP-PKKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERI 486
Cdd:cd01556 353 EGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPECVAKSFPNFFEDLESL 409
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
24-488 3.82e-163

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 468.47  E-value: 3.82e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   24 EIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEthseNNRAVVEGCGGvf 103
Cdd:PRK02427   4 MLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEIE----DDEVVVEGVGG-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  104 pASIDSKSDIeLYLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVVGLKQLGADVECTlGTNCPPVRVNan 183
Cdd:PRK02427  78 -GGLKEPEDV-LDCGNSGTTMRLLTGLLALQPGE--VVLTGDESLRKRPMGRLLDPLRQMGAKIEGR-DEGYLPLTIR-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  184 GGLPGGKVKLSGSISSQY----------LTAllmaaplalGDVEIEIVDKLISVPYVEMTLKLMERFGVSAEHSESWD-- 251
Cdd:PRK02427 151 GGKKGGPIEYDGPVSSQFvksllllaplFAE---------GDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGyr 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  252 RFFVKGGQKYKsPGNAYVEGDASSASYFLAGAAIT-GETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTvtGPS 330
Cdd:PRK02427 222 RIVIKGGQRLR-GQDITVPGDPSSAAFFLAAAAITgGSEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEREG--GEP 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  331 RDAFGMRH--LRAIDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahs 408
Cdd:PRK02427 299 VGDIRVRSseLKGIDIDIPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRK---------------- 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  409 kkfcgicvqLGATVEEGSDYCVITPPKKVkpAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERIT 487
Cdd:PRK02427 363 ---------LGAEVEETEDGLIITGGPLA--GVVDSYGDHRIAMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLG 431

                 .
gi 42571811  488 K 488
Cdd:PRK02427 432 A 432
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
28-483 1.03e-147

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 428.64  E-value: 1.03e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811    28 QPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILG-LNVETHSENNRAVVEGCGGVFPAS 106
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGaEIIKLDDEKSVVIVEGLGGSFEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   107 idskSDIELYLGNAGTAMRPLTAAvtAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNangGL 186
Cdd:pfam00275  81 ----EDLVLDMGNSGTALRPLTGR--LALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVR---GL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   187 PGGKVKLSGSISSQYLTALLMAAPLALGDvEIEIVDkLISVPYVEMTLKLMERFGVSAEHSESWDRFFVKGGQKYKSpGN 266
Cdd:pfam00275 152 RLGGIHIDGDVSSQFVTSLLMLAALLAEG-TTTIEN-LASEPYIDDTENMLKKFGAKIEGSGTELSITVKGGEKLPG-QE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   267 AYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPSrdafgmrHLRAIDVNM 346
Cdd:pfam00275 229 YRVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDADIVVGPP-------GLRGKAVDI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   347 NKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKvkfffslslsvysahskkfcgicvqLGATVEEGS 426
Cdd:pfam00275 302 RTAPDPAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRR-------------------------LGADVEELP 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571811   427 DYCVITPP-KKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVL 483
Cdd:pfam00275 357 DGLIIIPAvKELKGAEVDSYGDHRIAMALALAGLvAEGETIIDDIECTDRSFPDFEEKL 415
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
4-480 3.12e-129

bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 390.22  E-value: 3.12e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811    4 GSEIRPVKVRASVSTAEKASEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGl 83
Cdd:PRK11861 222 GAKPAPAVRSDTSGTGSHMEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLG- 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   84 nVETHSENNRAVVEGCGGVFPASIdsksdIELYLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVVGLKQL 163
Cdd:PRK11861 301 -VKLSRDGGTCVVGGTRGAFTAKT-----ADLFLGNAGTAVRPLTAALAVNGGE--YRIHGVPRMHERPIGDLVDGLRQI 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  164 GADVECTLGTNCPPVRVNANGGLPGGKVKLSGSISSQYLTALLMA---APLALGDVEIEIVDKLISVPYVEMTLKLMERF 240
Cdd:PRK11861 373 GARIDYEGNEGFPPLRIRPATISVDAPIRVRGDVSSQFLTALLMTlplVKAKDGASVVEIDGELISKPYIEITIKLMARF 452
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  241 GVSAEHsESWDRFFVKGGQKYKSPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWT 320
Cdd:PRK11861 453 GVTVER-DGWQRFTVPAGVRYRSPGTIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMG 531
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  321 ENSVTVTGPSRDafgMRHLRAIDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKVkfffsls 400
Cdd:PRK11861 532 DDWIEVRGIGHD---HGRLAPIDMDFNLIPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKV------- 601
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  401 lsvysahskkfcgicvqlGATVEEGSDYCVITPPKKVKP-AEIDTYDDHRMAMAFSLAACADVPITINDPGCTRKTFPDY 479
Cdd:PRK11861 602 ------------------GATVEEGADYLVVTPPAQLTPnASIDTYDDHRMAMCFSLVSLGGVPVRINDPKCVGKTFPDY 663

                 .
gi 42571811  480 F 480
Cdd:PRK11861 664 F 664
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
33-486 2.03e-100

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: 307.61  E-value: 2.03e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  33 ISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEthSENNRAVVEGCGG-VFPAsidskS 111
Cdd:cd01554   1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIE--DKDGVITIQGVGMaGLKA-----P 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 112 DIELYLGNAGTAMRPLTAAVtaAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVnaNGGLPGGKV 191
Cdd:cd01554  74 QNALNLGNSGTAIRLISGVL--AGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLK--GGKNLGPIH 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 192 KLSGSISSQYLTALLMAAPLALGDVEIEIVdklISVPYVEMTLKLMERFGVSAEhSESWDRFFVKGGQKYKSPgNAYVEG 271
Cdd:cd01554 150 YEDPIASAQVKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHIS-VQGTKKIVVQGPQKLTGQ-KYVVPG 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 272 DASSASYFLAGAAITGETVTVEGCGTTSlqGDVKFAEVLEKMGCKVSWTENSVTVTgpsrdafgMRHLRAIDVNMN---K 348
Cdd:cd01554 225 DISSAAFFLVAAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVE--------SSDLKATEICGAlipR 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 349 MPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKVkfffslslsvysahskkfcgicvqlGATVEEGSDY 428
Cdd:cd01554 295 LIDELPIIALLALQAQGTTVIKDAEELKVKETDRIFVVADELNSM-------------------------GADIEPTADG 349
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571811 429 CVITPPKKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLERI 486
Cdd:cd01554 350 MIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAEAINTSYPSFFDDLESL 408
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
26-486 1.87e-28

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 119.33  E-value: 1.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811   26 VLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGLNVEThSENNRAVVEGCG--GVF 103
Cdd:PRK14806 305 SVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEG-PHNGRVTIHGVGlhGLK 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  104 PASidsksdIELYLGNAGTAMRpLTAAVTAAGGNASyVLDGVPRMRERPIGDLVVGLKQLGADVECtlGTNC-PPVRVna 182
Cdd:PRK14806 384 APP------GPLYMGNSGTSMR-LLSGLLAAQSFDS-VLTGDASLSKRPMERVAKPLREMGAVIET--GEEGrPPLSI-- 451
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  183 ngglPGGKVkLSG------SISSQYLTALLMAAPLALGDVeieivdkliSVPYVEMTLKLMER----FGVSAEhsESWDR 252
Cdd:PRK14806 452 ----RGGQR-LKGihydlpMASAQVKSCLLLAGLYAEGET---------SVTEPAPTRDHTERmlrgFGYPVK--VEGNT 515
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  253 FFVKGGQKYKSpGNAYVEGDASSASYFLAGAAIT-GETVTVEGCGTTSLQgdVKFAEVLEKMGCKVSwTENSVTVTG-PS 330
Cdd:PRK14806 516 ISVEGGGKLTA-TDIEVPADISSAAFFLVAASIAeGSELTLEHVGINPTR--TGVIDILKLMGADIT-LENEREVGGePV 591
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  331 RD-AFGMRHLRAIDVNMNKMP---DVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKVkfffslslsvysa 406
Cdd:PRK14806 592 ADiRVRGARLKGIDIPEDQVPlaiDEFPVLFVAAACAEGRTVLTGAEELRVKESDRIQVMADGLKTL------------- 658
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  407 hskkfcGICvqlgATVEEGSdycVITPPKKVKPAEIDTYDDHRMAMAFSLAAC-ADVPITINDPGCTRKTFPDYFQVLER 485
Cdd:PRK14806 659 ------GID----CEPTPDG---IIIEGGIFGGGEVESHGDHRIAMSFSVASLrASGPITIHDCANVATSFPNFLELANQ 725

                 .
gi 42571811  486 I 486
Cdd:PRK14806 726 V 726
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
270-486 1.67e-26

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: 106.59  E-value: 1.67e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 270 EGDASSASYFLAGAAITGETVTVEGCGTTS-----LQGDVKFAEVLEKM-GCKVSWTEnsvtvTGPSRDAFGMRHLRAID 343
Cdd:cd01553   7 KGGGQILRSFLVLAAISGGPITVTGIRPDRakpglLRQHLTFLKALEKIcGATVEGGE-----LGSDRISFRPGTVRGGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 344 VNMN-----KMPDVAMTLAVVALFADGPTTIRDVASWRV----KETERMIAICTELRKVkfffslslsvysahskkfcgi 414
Cdd:cd01553  82 VRFAigsagSCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKI--------------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 415 cvqlGATVEEGSD------------YCVITPPKKVKPAEIdtyddhRMAMAFSLAACADVpitINDPGCTRKTFPDYFQV 482
Cdd:cd01553 141 ----GAHQEETLLrhgfypagggvvATEVSPVEKLNTAQL------RQLVLPMLLASGAV---EFTVAHPSCHLLTNFAV 207

                ....
gi 42571811 483 LERI 486
Cdd:cd01553 208 LEAL 211
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
34-344 2.72e-06

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: 49.60  E-value: 2.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  34 SGLIKLPGSKslsNRIL-LLAA--LSEGTTVVDNLLNSDDINYMLDALKILGLNVEtHSENNRAVVEgcggvfPASIDSK 110
Cdd:COG0766  13 SGEVRISGAK---NAALpILAAalLTDGPVTLRNVPDLSDVRTMLELLESLGVKVE-RDDGGTLTID------ASNINST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 111 S-DIELylgnaGTAMR-------PL-----TAAVTAAGGNASyvldGVprmreRPIgDL-VVGLKQLGADVECTLGTncp 176
Cdd:COG0766  83 EaPYEL-----VRKMRasilvlgPLlarfgEARVSLPGGCAI----GA-----RPI-DLhLKGLEALGAEIEIEHGY--- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 177 pVRVNANGgLPGGKVKLsgsissqyltallmaaplalgDV---------------------------EIEIVDkLISVpy 229
Cdd:COG0766 145 -IEARAGR-LKGARIYL---------------------DFpsvgatenimmaavlaegttvienaarEPEIVD-LANF-- 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 230 vemtLKLM-----------------ERFGvSAEHSESWDRffvkggqkykspgnayVEgdassASYFLAGAAITGETVTV 292
Cdd:COG0766 199 ----LNAMgakiegagtdtitiegvEKLH-GAEHTVIPDR----------------IE-----AGTFLVAAAITGGDVTV 252
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571811 293 EGCGTTSLQGdvkFAEVLEKMGCKVSWTENSVTVTGPSRdafgmrhLRAIDV 344
Cdd:COG0766 253 KNVIPEHLEA---VLAKLREAGVEIEEGDDGIRVRGPGR-------LKAVDI 294
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
33-371 2.51e-05

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: 46.31  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811  33 ISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKILGlnVETHSENNRAVVegcggvfpasIDSkSD 112
Cdd:cd01555   1 LSGEVRISGAKNAALPILAAALLTDEPVTLRNVPDLLDVETMIELLRSLG--AKVEFEGENTLV----------IDA-SN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 113 IELYLGNAGTA--MR-------PL-----TAAVTAAGGNAsyvldgvprMRERPIgDL-VVGLKQLGADVECTLGTncpp 177
Cdd:cd01555  68 INSTEAPYELVrkMRasilvlgPLlarfgEARVSLPGGCA---------IGARPV-DLhLKGLEALGAKIEIEDGY---- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 178 VRVNANGGLPGGKVKLS-----GSISSqyltalLMAAPLALGDVEI-------EIVDkLISVpyvemtLKLMerfGVSAE 245
Cdd:cd01555 134 VEAKAAGRLKGARIYLDfpsvgATENI------MMAAVLAEGTTVIenaarepEIVD-LANF------LNKM---GAKIE 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571811 246 HSESwDRFFVKG-----GQKYKspgnayVEGDASSASYFLAGAAITGETVTVEGCGTTSLQgdvKFAEVLEKMGCKVSWT 320
Cdd:cd01555 198 GAGT-DTIRIEGverlhGAEHT------VIPDRIEAGTFLVAAAITGGDITVENVIPEHLE---AVLAKLREMGAKIEIG 267
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571811 321 ENSVTVTGPSRDafgmrhLRAIDVNMNKMP----DVAMTLAVVALFADGPTTIRD 371
Cdd:cd01555 268 EDGIRVDGDGGR------LKAVDIETAPYPgfptDLQAQFMALLTQAEGTSVITE 316
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
279-344 5.54e-04

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 42.33  E-value: 5.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571811  279 FLAGAAITGETVTVEGCGTTSLQGdvkFAEVLEKMGCKVSWTENSVTVTGPsrdafgmRHLRAIDV 344
Cdd:PRK09369 240 FLVAAAITGGDVTIRGARPEHLEA---VLAKLREAGAEIEEGEDGIRVDMP-------GRLKAVDI 295
 
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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