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Conserved domains on  [gi|446175376|ref|WP_000253231|]
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MULTISPECIES: 3-phosphoshikimate 1-carboxyvinyltransferase [Staphylococcus]

Protein Classification

3-phosphoshikimate 1-carboxyvinyltransferase( domain architecture ID 11479797)

3-phosphoshikimate 1-carboxyvinyltransferase catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate

EC:  2.5.1.19
Gene Ontology:  GO:0009073|GO:0008652|GO:0003866|GO:0009423
PubMed:  17348837

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 10-431 1.45e-171

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


:

Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 487.73  E-value: 1.45e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  10 SGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIkeDEDKLVVNSPGYKAFKTPHQVL 89
Cdd:PRK02427  10 PSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI--EDDEVVVEGVGGGGLKEPEDVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  90 YTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVI-KGINYQMEVASA 168
Cdd:PRK02427  88 DCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKgGPIEYDGPVSSQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 169 QVKSAILFASLFSND--TTVIKELDVSRNHTET---MFRHFNIPIEAE--RLSITTTPDAIQHIKPADFHVPGDISSAAF 241
Cdd:PRK02427 168 FVKSLLLLAPLFAEGdtETTVIEPLPSRPHTEItlrMLRAFGVEVENVegWGYRRIVIKGGQRLRGQDITVPGDPSSAAF 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 242 FIVAALITPESDVTIHNVGINPTRSG--IIDIVEKMGGNIQLFNQTTGAEPTASIRIQyTPMLQPITIEgelVPKAIDEL 319
Cdd:PRK02427 248 FLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVR-SSELKGIDID---IPDIIDEA 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 320 PVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKtnATVDSLTDHRIGMMLAVAS 399
Cdd:PRK02427 324 PTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRIAMAFAIAG 401

                        410       420       430
                 ....*....|....*....|....*....|..
gi 446175376 400 LLSSEPVKIKQFDAVNVSFPGFLPKLKLLENE 431
Cdd:PRK02427 402 LAAEGPVTIDDPECVAKSFPDFFEDLASLGAN 433
 
Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 10-431 1.45e-171

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 487.73  E-value: 1.45e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  10 SGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIkeDEDKLVVNSPGYKAFKTPHQVL 89
Cdd:PRK02427  10 PSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI--EDDEVVVEGVGGGGLKEPEDVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  90 YTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVI-KGINYQMEVASA 168
Cdd:PRK02427  88 DCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKgGPIEYDGPVSSQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 169 QVKSAILFASLFSND--TTVIKELDVSRNHTET---MFRHFNIPIEAE--RLSITTTPDAIQHIKPADFHVPGDISSAAF 241
Cdd:PRK02427 168 FVKSLLLLAPLFAEGdtETTVIEPLPSRPHTEItlrMLRAFGVEVENVegWGYRRIVIKGGQRLRGQDITVPGDPSSAAF 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 242 FIVAALITPESDVTIHNVGINPTRSG--IIDIVEKMGGNIQLFNQTTGAEPTASIRIQyTPMLQPITIEgelVPKAIDEL 319
Cdd:PRK02427 248 FLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVR-SSELKGIDID---IPDIIDEA 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 320 PVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKtnATVDSLTDHRIGMMLAVAS 399
Cdd:PRK02427 324 PTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRIAMAFAIAG 401

                        410       420       430
                 ....*....|....*....|....*....|..
gi 446175376 400 LLSSEPVKIKQFDAVNVSFPGFLPKLKLLENE 431
Cdd:PRK02427 402 LAAEGPVTIDDPECVAKSFPDFFEDLASLGAN 433
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 3-428 7.07e-162

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: 462.25  E-value: 7.07e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   3 SEQIIDISGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKE-DEDKLVVNSPGYKa 81
Cdd:COG0128    2 SSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEElDGGTLRVTGVGGG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  82 FKTPHQVLYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVIKGINY 161
Cdd:COG0128   81 LKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGPLKGGEY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 162 QME-VASAQVKSAILFASLFSND---TTVIKEL--DVSRNHTETMFRHFNIPIEAERLSITTTPdAIQHIKPADFHVPGD 235
Cdd:COG0128  161 EIPgSASSQFKSALLLAGPLAEGgleITVTGELesKPYRDHTERMLRAFGVEVEVEGYRRFTVP-GGQRYRPGDYTVPGD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 236 ISSAAFFIVAALITpESDVTIHNVGINPT--RSGIIDIVEKMGGNIQLFNQTtgaeptasIRIQYTPmLQPITIEGELVP 313
Cdd:COG0128  240 ISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG--------ITVRGSP-LKGIDIDLSDIP 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 314 kaiDELPVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTNATVDSLTDHRIGM 393
Cdd:COG0128  310 ---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAM 386

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 446175376 394 MLAVASLLSSEPVKIKQFDAVNVSFPGFLPKLKLL 428
Cdd:COG0128  387 AFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 13-428 4.25e-154

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: 442.38  E-value: 4.25e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  13 LKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSPGyKAFKTPHQVLYTG 92
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  93 NSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVIKGINYQMEVA-SAQVK 171
Cdd:cd01556   80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAvSSQFK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 172 SAILFA-SLFSNDTTVIKELDVS---RNHTETMFRHFNIPIEAE-RLSITTTPdaIQHIKPADFHVPGDISSAAFFIVAA 246
Cdd:cd01556  160 SALLLAaPLAEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDgYRTITVKG--GQKYKGPEYTVEGDASSAAFFLAAA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 247 LITPeSDVTIHNVGINPTRSGIIDIVEKMGGNIQLFNQTTgaeptasIRIQYTPMLQPITIEGELVPkaiDELPVIALLC 326
Cdd:cd01556  238 AITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDT-------VVVESGGKLKGIDIDGNDIP---DEAPTLAVLA 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 327 TQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFK-TNATVDSLTDHRIGMMLAVASLLSSEP 405
Cdd:cd01556  307 AFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPLKgAGVEVYTYGDHRIAMSFAIAGLVAEGG 386

                        410       420
                 ....*....|....*....|...
gi 446175376 406 VKIKQFDAVNVSFPGFLPKLKLL 428
Cdd:cd01556  387 VTIEDPECVAKSFPNFFEDLESL 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-425 2.67e-147

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 425.17  E-value: 2.67e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376    8 DISGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDI-KEDEDKLVVNSPGY-KAFKTP 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIiKLDDEKSVVIVEGLgGSFEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   86 -HQVLYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIE-DNYTPLIIKPSVIKGINYQM 163
Cdd:pfam00275  81 eDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREgYNYAPLKVRGLRLGGIHIDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  164 EVASAQVKSAILFASLFSNDTTVIKEL--DVSRNHTETMFRHFNIPIEAER--LSITTTPdaIQHIKPADFHVPGDISSA 239
Cdd:pfam00275 161 DVSSQFVTSLLMLAALLAEGTTTIENLasEPYIDDTENMLKKFGAKIEGSGteLSITVKG--GEKLPGQEYRVEGDRSSA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  240 AFFIVAALITPeSDVTIHNVGINPTRSG--IIDIVEKMGGNIQlfnqttgAEPTASIRIQYTpmlqPITIEGELVPKAID 317
Cdd:pfam00275 239 AYFLVAAAITG-GTVTVENVGINSLQGDeaLLEILEKMGAEIT-------QEEDADIVVGPP----GLRGKAVDIRTAPD 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  318 ELPVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTN-ATVDSLTDHRIGMMLA 396
Cdd:pfam00275 307 PAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKELKgAEVDSYGDHRIAMALA 386

                         410       420
                  ....*....|....*....|....*....
gi 446175376  397 VASLLSSEPVKIKQFDAVNVSFPGFLPKL 425
Cdd:pfam00275 387 LAGLVAEGETIIDDIECTDRSFPDFEEKL 415
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 15-421 6.47e-118

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: 350.04  E-value: 6.47e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   15 GEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSPGYKafkTPHQVLYTGNS 94
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGK---EPQAELDLGNS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   95 GTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIE-DNYTPLIIKPSVIKGINYQMEVASAQVKSA 173
Cdd:TIGR01356  78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEgGGSLPLTISGPLPGGIVYISGSASSQYKSA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  174 ILFASLFSND--TTVIKELDVSRNHTETM---FRHFNIPIEAER-LSITTTPDaiQHIKPADFHVPGDISSAAFFIVAAL 247
Cdd:TIGR01356 158 LLLAAPALQAvgITIVGEPLKSRPYIEITldlLGSFGVEVERSDgRKIVVPGG--QKYGPQGYDVPGDYSSAAFFLAAAA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  248 ITPeSDVTIHNVGINPTRSG--IIDIVEKMGGNIQLFNQttgaeptaSIRIQYTPMLQPITIEgelVPKAIDELPVIALL 325
Cdd:TIGR01356 236 ITG-GRVTLENLGINPTQGDkaIIIVLEEMGADIEVEED--------DLIVEGASGLKGIKID---MDDMIDELPTLAVL 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  326 CTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTNATVDSLTDHRIGMMLAVASLLSSEP 405
Cdd:TIGR01356 304 AAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLVAEGE 383

                         410
                  ....*....|....*.
gi 446175376  406 VKIKQFDAVNVSFPGF 421
Cdd:TIGR01356 384 VLIDDPECVAKSFPSF 399
 
Name Accession Description Interval E-value
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 10-431 1.45e-171

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 487.73  E-value: 1.45e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  10 SGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIkeDEDKLVVNSPGYKAFKTPHQVL 89
Cdd:PRK02427  10 PSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI--EDDEVVVEGVGGGGLKEPEDVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  90 YTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVI-KGINYQMEVASA 168
Cdd:PRK02427  88 DCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEGRDEGYLPLTIRGGKKgGPIEYDGPVSSQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 169 QVKSAILFASLFSND--TTVIKELDVSRNHTET---MFRHFNIPIEAE--RLSITTTPDAIQHIKPADFHVPGDISSAAF 241
Cdd:PRK02427 168 FVKSLLLLAPLFAEGdtETTVIEPLPSRPHTEItlrMLRAFGVEVENVegWGYRRIVIKGGQRLRGQDITVPGDPSSAAF 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 242 FIVAALITPESDVTIHNVGINPTRSG--IIDIVEKMGGNIQLFNQTTGAEPTASIRIQyTPMLQPITIEgelVPKAIDEL 319
Cdd:PRK02427 248 FLAAAAITGGSEVTITNVGLNSTQGGkaIIDVLEKMGADIEIENEREGGEPVGDIRVR-SSELKGIDID---IPDIIDEA 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 320 PVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKtnATVDSLTDHRIGMMLAVAS 399
Cdd:PRK02427 324 PTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRIAMAFAIAG 401

                        410       420       430
                 ....*....|....*....|....*....|..
gi 446175376 400 LLSSEPVKIKQFDAVNVSFPGFLPKLKLLENE 431
Cdd:PRK02427 402 LAAEGPVTIDDPECVAKSFPDFFEDLASLGAN 433
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 3-428 7.07e-162

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: 462.25  E-value: 7.07e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   3 SEQIIDISGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKE-DEDKLVVNSPGYKa 81
Cdd:COG0128    2 SSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEElDGGTLRVTGVGGG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  82 FKTPHQVLYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVIKGINY 161
Cdd:COG0128   81 LKEPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRGGGYLPLTIRGGPLKGGEY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 162 QME-VASAQVKSAILFASLFSND---TTVIKEL--DVSRNHTETMFRHFNIPIEAERLSITTTPdAIQHIKPADFHVPGD 235
Cdd:COG0128  161 EIPgSASSQFKSALLLAGPLAEGgleITVTGELesKPYRDHTERMLRAFGVEVEVEGYRRFTVP-GGQRYRPGDYTVPGD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 236 ISSAAFFIVAALITpESDVTIHNVGINPT--RSGIIDIVEKMGGNIQLFNQTtgaeptasIRIQYTPmLQPITIEGELVP 313
Cdd:COG0128  240 ISSAAFFLAAAAIT-GSEVTVEGVGLNSTqgDTGILDILKEMGADIEIENDG--------ITVRGSP-LKGIDIDLSDIP 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 314 kaiDELPVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTNATVDSLTDHRIGM 393
Cdd:COG0128  310 ---DEAPTLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAM 386

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 446175376 394 MLAVASLLSSEPVKIKQFDAVNVSFPGFLPKLKLL 428
Cdd:COG0128  387 AFAVAGLRAEGPVTIDDAECVAKSFPDFFELLESL 421
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 13-428 4.25e-154

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: 442.38  E-value: 4.25e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  13 LKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSPGyKAFKTPHQVLYTG 92
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGTVEIVGGG-GLGLPPEAVLDCG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  93 NSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIKPSVIKGINYQMEVA-SAQVK 171
Cdd:cd01556   80 NSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAvSSQFK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 172 SAILFA-SLFSNDTTVIKELDVS---RNHTETMFRHFNIPIEAE-RLSITTTPdaIQHIKPADFHVPGDISSAAFFIVAA 246
Cdd:cd01556  160 SALLLAaPLAEGPTTIIIGELESkpyIDHTERMLRAFGAEVEVDgYRTITVKG--GQKYKGPEYTVEGDASSAAFFLAAA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 247 LITPeSDVTIHNVGINPTRSGIIDIVEKMGGNIQLFNQTTgaeptasIRIQYTPMLQPITIEGELVPkaiDELPVIALLC 326
Cdd:cd01556  238 AITG-SEIVIKNVGLNSGDTGIIDVLKEMGADIEIGNEDT-------VVVESGGKLKGIDIDGNDIP---DEAPTLAVLA 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 327 TQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFK-TNATVDSLTDHRIGMMLAVASLLSSEP 405
Cdd:cd01556  307 AFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPLKgAGVEVYTYGDHRIAMSFAIAGLVAEGG 386

                        410       420
                 ....*....|....*....|...
gi 446175376 406 VKIKQFDAVNVSFPGFLPKLKLL 428
Cdd:cd01556  387 VTIEDPECVAKSFPNFFEDLESL 409
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
8-425 2.67e-147

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 425.17  E-value: 2.67e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376    8 DISGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDI-KEDEDKLVVNSPGY-KAFKTP 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIiKLDDEKSVVIVEGLgGSFEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   86 -HQVLYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIE-DNYTPLIIKPSVIKGINYQM 163
Cdd:pfam00275  81 eDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREgYNYAPLKVRGLRLGGIHIDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  164 EVASAQVKSAILFASLFSNDTTVIKEL--DVSRNHTETMFRHFNIPIEAER--LSITTTPdaIQHIKPADFHVPGDISSA 239
Cdd:pfam00275 161 DVSSQFVTSLLMLAALLAEGTTTIENLasEPYIDDTENMLKKFGAKIEGSGteLSITVKG--GEKLPGQEYRVEGDRSSA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  240 AFFIVAALITPeSDVTIHNVGINPTRSG--IIDIVEKMGGNIQlfnqttgAEPTASIRIQYTpmlqPITIEGELVPKAID 317
Cdd:pfam00275 239 AYFLVAAAITG-GTVTVENVGINSLQGDeaLLEILEKMGAEIT-------QEEDADIVVGPP----GLRGKAVDIRTAPD 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  318 ELPVIALLCTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTN-ATVDSLTDHRIGMMLA 396
Cdd:pfam00275 307 PAPTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKELKgAEVDSYGDHRIAMALA 386

                         410       420
                  ....*....|....*....|....*....
gi 446175376  397 VASLLSSEPVKIKQFDAVNVSFPGFLPKL 425
Cdd:pfam00275 387 LAGLVAEGETIIDDIECTDRSFPDFEEKL 415
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 10-422 1.24e-132

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 398.60  E-value: 1.24e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  10 SGPLKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKE-DEDKLVVNSPGYKAFKTPHQV 88
Cdd:PRK14806 309 GGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGVVIEGpHNGRVTIHGVGLHGLKAPPGP 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  89 LYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPLIIK-PSVIKGINYQMEVAS 167
Cdd:PRK14806 389 LYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIETGEEGRPPLSIRgGQRLKGIHYDLPMAS 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 168 AQVKSAILFASLFSNDTTVIKELDVSRNHTETMFRHFNIPIEAERLSITTTPDAiqHIKPADFHVPGDISSAAFFIVAAL 247
Cdd:PRK14806 469 AQVKSCLLLAGLYAEGETSVTEPAPTRDHTERMLRGFGYPVKVEGNTISVEGGG--KLTATDIEVPADISSAAFFLVAAS 546

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 248 ITPESDVTIHNVGINPTRSGIIDIVEKMGGNIQLFNQT-TGAEPTASIRIQYTPmLQPITIEGELVPKAIDELPV--IAL 324
Cdd:PRK14806 547 IAEGSELTLEHVGINPTRTGVIDILKLMGADITLENEReVGGEPVADIRVRGAR-LKGIDIPEDQVPLAIDEFPVlfVAA 625

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 325 LCTQavGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFkTNATVDSLTDHRIGMMLAVASLLSSE 404
Cdd:PRK14806 626 ACAE--GRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGIF-GGGEVESHGDHRIAMSFSVASLRASG 702

                        410
                 ....*....|....*...
gi 446175376 405 PVKIKQFDAVNVSFPGFL 422
Cdd:PRK14806 703 PITIHDCANVATSFPNFL 720
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 15-421 6.47e-118

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: 350.04  E-value: 6.47e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   15 GEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSPGYKafkTPHQVLYTGNS 94
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVAVIEGVGGK---EPQAELDLGNS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   95 GTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIE-DNYTPLIIKPSVIKGINYQMEVASAQVKSA 173
Cdd:TIGR01356  78 GTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEgGGSLPLTISGPLPGGIVYISGSASSQYKSA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  174 ILFASLFSND--TTVIKELDVSRNHTETM---FRHFNIPIEAER-LSITTTPDaiQHIKPADFHVPGDISSAAFFIVAAL 247
Cdd:TIGR01356 158 LLLAAPALQAvgITIVGEPLKSRPYIEITldlLGSFGVEVERSDgRKIVVPGG--QKYGPQGYDVPGDYSSAAFFLAAAA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  248 ITPeSDVTIHNVGINPTRSG--IIDIVEKMGGNIQLFNQttgaeptaSIRIQYTPMLQPITIEgelVPKAIDELPVIALL 325
Cdd:TIGR01356 236 ITG-GRVTLENLGINPTQGDkaIIIVLEEMGADIEVEED--------DLIVEGASGLKGIKID---MDDMIDELPTLAVL 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  326 CTQAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTNATVDSLTDHRIGMMLAVASLLSSEP 405
Cdd:TIGR01356 304 AAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLVAEGE 383

                         410
                  ....*....|....*.
gi 446175376  406 VKIKQFDAVNVSFPGF 421
Cdd:TIGR01356 384 VLIDDPECVAKSFPSF 399
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 13-428 1.22e-89

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: 277.56  E-value: 1.22e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  13 LKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSPGYKAFKTPHQVLYTG 92
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  93 NSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGIED-NYTPLIIKPSVIKGINYQMEVASAQVK 171
Cdd:cd01554   81 NSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEErDLPPLLKGGKNLGPIHYEDPIASAQVK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 172 SAILFASLFSNDTTVIKEL--DVSRNHTETMFRHFNIPIEAERLSITTTpDAIQHIKPADFHVPGDISSAAFFIVAALIT 249
Cdd:cd01554  161 SALMFAALLAKGETVIIEAakEPTINHTENMLQTFGGHISVQGTKKIVV-QGPQKLTGQKYVVPGDISSAAFFLVAAAIA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 250 PeSDVTIHNVGINPTRSGIIDIVEKMGGNIQLFNQTTGAEPTAsiriqytpmLQPITIEGELVPKAIDELPVIALLCTQA 329
Cdd:cd01554  240 P-GRLVLQNVGINETRTGIIDVLRAMGAKIEIGEDTISVESSD---------LKATEICGALIPRLIDELPIIALLALQA 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 330 VGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTNATVDSLTDHRIGMMLAVASLLSSEPVKIK 409
Cdd:cd01554  310 QGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALVADGEVELD 389

                        410
                 ....*....|....*....
gi 446175376 410 QFDAVNVSFPGFLPKLKLL 428
Cdd:cd01554  390 RAEAINTSYPSFFDDLESL 408
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
1-421 5.93e-38

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 145.58  E-value: 5.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   1 MVSEQIIDISgPL---KGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSP 77
Cdd:PRK11860   1 MFSTEFLDLP-PLlsaGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYRITGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  78 GYKaFKTPHQVLYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANIEGI-EDNYTPLIIKPSVI 156
Cdd:PRK11860  80 GGQ-FPVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLgNEGFPPLRIGPAPL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 157 KG---INYQMEVASaQVKSAILFA-SLFSNDTTVIK---ELdVSRNHTE---TMFRHFNIPIEAERLSITTTPDAIQHIK 226
Cdd:PRK11860 159 RLdapIRVRGDVSS-QFLTALLMAlPLVARRDITIEvvgEL-ISKPYIEitlNLLARFGIAVQREGWQRFTIPAGSRYRS 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 227 PADFHVPGDISSAAFFIVAALITPESDVTIHNVGINPTRSGI--IDIVEKMGGNIqlfnqtTGAEPTASIRIQYTPmLQP 304
Cdd:PRK11860 237 PGEIHVEGDASSASYFIAAGAIAGGAPVRIEGVGRDSIQGDIrfAEAARAMGAQV------TSGPNWLEVRRGAWP-LKA 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 305 ITIEGELVPKAIDELPVIALLctqAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTN---A 381
Cdd:PRK11860 310 IDLDCNHIPDAAMTLAVMALY---ADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADwkaA 386

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 446175376 382 TVDSLTDHRIGMMLAVASLLSSE-PVKIKQFDAVNVSFPGF 421
Cdd:PRK11860 387 AIHTYDDHRMAMCFSLAAFNPAGlPVRINDPKCVAKTFPDY 427
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 11-430 5.42e-35

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 137.53  E-value: 5.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  11 GPL---KGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKEDEDKLVVNSPgYKAFKTPHQ 87
Cdd:PRK11861 246 GPFshaQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKLSRDGGTCVVGGT-RGAFTAKTA 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  88 VLYTGNSGTTTRLLAGLLSGLGIESVLSGDVSIGKRPMDRVLRPLKLMDANI--EGIEdNYTPLIIKPSVIK---GINYQ 162
Cdd:PRK11861 325 DLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIdyEGNE-GFPPLRIRPATISvdaPIRVR 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 163 MEVASAQVKSAILFASLF-SNDTTVIKELD---VSRNHTETMFR---HFNIPIEAERLSITTTPDAIQHIKPADFHVPGD 235
Cdd:PRK11861 404 GDVSSQFLTALLMTLPLVkAKDGASVVEIDgelISKPYIEITIKlmaRFGVTVERDGWQRFTVPAGVRYRSPGTIMVEGD 483

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 236 ISSAAFFIVAALITpESDVTIHNVGINPTRS--GIIDIVEKMGGNIqlfnqTTGAEPTASIRIQYT-PMLQPITIEGELV 312
Cdd:PRK11861 484 ASSASYFLAAGALG-GGPLRVEGVGRASIQGdvGFANALMQMGANV-----TMGDDWIEVRGIGHDhGRLAPIDMDFNLI 557

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 313 PKAIDELPVIALLctqAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIH-PSEFKTNATVDSLTDHRI 391
Cdd:PRK11861 558 PDAAMTIAVAALF---ADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTpPAQLTPNASIDTYDDHRM 634

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 446175376 392 GMMLAVASlLSSEPVKIKQFDAVNVSFPGFLPKLKLLEN 430
Cdd:PRK11861 635 AMCFSLVS-LGGVPVRINDPKCVGKTFPDYFDRFLALAN 672
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
 13-426 2.64e-25

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 107.14  E-value: 2.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  13 LKGEIEVPGDKSMTHRAIMLASLAEGTSNIYKPLLGEDCRRTMDIFRLLGVDIKED-EDK--LVVNSPGYKAFKTPHQV- 88
Cdd:PLN02338  12 ISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDsENNraVVEGCGGKFPVSGDSKEd 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  89 --LYTGNSGTTTRLLAGLLSGLGIES--VLSGDVSIGKRPMDRVLRPLKLMDANIEGIEDNYTPliikPSVIKGIN---- 160
Cdd:PLN02338  92 veLFLGNAGTAMRPLTAAVTAAGGNAsyVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCP----PVRVNAAGglpg 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 161 ---YQMEVASAQVKSAILFASLFSND--TTVIKELDVSRNHTE---TMFRHFNIPIEA----ERLSItttPDAIQHIKPA 228
Cdd:PLN02338 168 gkvKLSGSISSQYLTALLMAAPLALGdvEIEIVDKLISVPYVEmtlKLMERFGVSVEHsdswDRFFI---KGGQKYKSPG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 229 DFHVPGDISSAAFFIVAALITPESdVTIHNVGINPTRSGI--IDIVEKMGGNIQLFNQT---TGAEPTASIRIQytpmLQ 303
Cdd:PLN02338 245 NAYVEGDASSASYFLAGAAITGGT-VTVEGCGTTSLQGDVkfAEVLEKMGAKVEWTENSvtvTGPPRDAFGGKH----LK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 304 PITIEGELVPKAIDELPVIALLctqAVGTSTIKDAEELKVKETNRIDTTADMLNLLGFELQPTNDGLIIHPSEFKTNATV 383
Cdd:PLN02338 320 AIDVNMNKMPDVAMTLAVVALF---ADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEI 396

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 446175376 384 DSLTDHRIGMMLAVASlLSSEPVKIKQFDAVNVSFPGFLPKLK 426
Cdd:PLN02338 397 DTYDDHRMAMAFSLAA-CGDVPVTINDPGCTRKTFPTYFDVLE 438
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
 13-400 1.21e-11

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: 65.96  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  13 LKGEIEVPGDK-SMThrAIMLAS-LAEGTS---NIykPLLgEDCRRTMDIFRLLGVDIK-EDEDKLVVNSPGYKAFKTPh 86
Cdd:cd01555    1 LSGEVRISGAKnAAL--PILAAAlLTDEPVtlrNV--PDL-LDVETMIELLRSLGAKVEfEGENTLVIDASNINSTEAP- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  87 qvlYTGNSgtTTRLlagllsglgieSVL----------SGDVS------IGKRPMDRVLRPLKLMDANIEgIEDNYTpLI 150
Cdd:cd01555   75 ---YELVR--KMRA-----------SILvlgpllarfgEARVSlpggcaIGARPVDLHLKGLEALGAKIE-IEDGYV-EA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 151 IKPSVIKGINYQMEVASAQVKSAILFASLFSNDTTVIKeldvsrnhtetmfrhfNIPIEAE------------------- 211
Cdd:cd01555  137 KAAGRLKGARIYLDFPSVGATENIMMAAVLAEGTTVIE----------------NAAREPEivdlanflnkmgakiegag 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 212 --RLSITTTPDaiqhIKPADFHVPGDISSAAFFIVAALITpESDVTIHNVGINPTRSgIIDIVEKMGGNIQlfnqttgaE 289
Cdd:cd01555  201 tdTIRIEGVER----LHGAEHTVIPDRIEAGTFLVAAAIT-GGDITVENVIPEHLEA-VLAKLREMGAKIE--------I 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 290 PTASIRIQYTP-MLQPITIEGELVPK-AIDELPVIALLCTQAVGTSTIKDaeelKVKEtNRIdTTADMLNLLGFELQPTN 367
Cdd:cd01555  267 GEDGIRVDGDGgRLKAVDIETAPYPGfPTDLQAQFMALLTQAEGTSVITE----TIFE-NRF-MHVDELNRMGADIKVEG 340

                        410       420       430
                 ....*....|....*....|....*....|...
gi 446175376 368 DGLIIHPSEFKTNATVDSlTDHRIGMMLAVASL 400
Cdd:cd01555  341 NTAIIRGVTKLSGAPVMA-TDLRAGAALVLAGL 372
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
 12-337 1.80e-08

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: 56.15  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  12 PLKGEIEVPGDK-SMThrAIMLAS-LAEGTSNIYK-PLLgEDCRRTMDIFRLLGVDIK-EDEDKLVVNSPGYKAFKTPHQ 87
Cdd:COG0766   11 PLSGEVRISGAKnAAL--PILAAAlLTDGPVTLRNvPDL-SDVRTMLELLESLGVKVErDDGGTLTIDASNINSTEAPYE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  88 VlytgnsGTTTRLlagllsglgieSVL----------SGDVS------IGKRPMDRVLRPLKLMDANIEgIEDNYtpLII 151
Cdd:COG0766   88 L------VRKMRA-----------SILvlgpllarfgEARVSlpggcaIGARPIDLHLKGLEALGAEIE-IEHGY--IEA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 152 KPSVIKGINYQMEVASAQVKSAILFASLFSNDTTVIK---------EL---------DVSRNHTETmfrhfnIPIE-AER 212
Cdd:COG0766  148 RAGRLKGARIYLDFPSVGATENIMMAAVLAEGTTVIEnaarepeivDLanflnamgaKIEGAGTDT------ITIEgVEK 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 213 LsitttpdaiqhiKPADFHVPGDISSAAFFIVAALITpESDVTIHNVGINPTRSgIIDIVEKMGGNIqlfnqTTGAEpta 292
Cdd:COG0766  222 L------------HGAEHTVIPDRIEAGTFLVAAAIT-GGDVTVKNVIPEHLEA-VLAKLREAGVEI-----EEGDD--- 279

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446175376 293 SIRIQYTPMLQPITIEGELVPK-AIDELPVIALLCTQAVGTSTIKD 337
Cdd:COG0766  280 GIRVRGPGRLKAVDIKTAPYPGfPTDLQAQFMALLTQAEGTSVITE 325
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
 6-335 1.45e-06

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 50.03  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376   6 IIDISGPLKGEIEVPGDK-SMThrAIMLAS-LAEGTSNIYK-PLLGeDCRRTMDIFRLLGVDI-KEDEDKLVVNSPGYKA 81
Cdd:PRK09369   5 VIEGGKPLSGEVTISGAKnAAL--PILAASlLAEEPVTLTNvPDLS-DVRTMIELLRSLGAKVeFDGNGTVTIDASNINN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376  82 FKTPHQVlytgnsGTTTRLlagllsglgieSVL----------SGDVS------IGKRPMDRVLRPLKLMDANIEgIEDN 145
Cdd:PRK09369  82 TEAPYEL------VKKMRA-----------SILvlgpllarfgEAKVSlpggcaIGARPVDLHLKGLEALGAEIE-IEHG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 146 YtpliIKPSV---IKGINYQMEVASaqV---KSAILFASLfSNDTTVIK------EL------------DVSRNHTETmf 201
Cdd:PRK09369 144 Y----VEAKAdgrLKGAHIVLDFPS--VgatENILMAAVL-AEGTTVIEnaarepEIvdlanflnkmgaKISGAGTDT-- 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446175376 202 rhfnIPIE-AERLSITTT---PDAIQhikpadfhvpgdissAAFFIVAALITpESDVTIHNVGINPTRSgIIDIVEKMGG 277
Cdd:PRK09369 215 ----ITIEgVERLHGAEHtviPDRIE---------------AGTFLVAAAIT-GGDVTIRGARPEHLEA-VLAKLREAGA 273

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446175376 278 NIqlfnqTTGAEptaSIRIQYTPMLQPITIEGELVPK-AIDELPVIALLCTQAVGTSTI 335
Cdd:PRK09369 274 EI-----EEGED---GIRVDMPGRLKAVDIKTAPYPGfPTDMQAQFMALLTQAEGTSVI 324
 
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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