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Conserved domains on  [gi|695731700|ref|WP_032658201|]
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MULTISPECIES: 3-phosphoshikimate 1-carboxyvinyltransferase [Enterobacter]

Protein Classification

3-phosphoshikimate 1-carboxyvinyltransferase( domain architecture ID 11414790)

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; 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
PubMed:  8973316|17348837
SCOP:  4001425

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-423 0e+00

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: 607.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDrTRCEVTGNGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALRsGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128   80 GLK-EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLV 239
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
                        410       420
                 ....*....|....*....|....*
gi 695731700 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128  397 GPVTIDDAECVAKSFPDFFELLESL 421
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-423 0e+00

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: 607.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDrTRCEVTGNGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALRsGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128   80 GLK-EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLV 239
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
                        410       420
                 ....*....|....*....|....*
gi 695731700 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128  397 GPVTIDDAECVAKSFPDFFELLESL 421
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
1-424 0e+00

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 606.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTRceVTGNGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALrSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860  82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 159 GGHVEVDGSVSSQFLTALLMTAPL-APQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGNY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGE--LNAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK---LQFAEIGTYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 695731700 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-423 0e+00

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: 551.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRtrCEVTGNGGALRSGEElELF 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPPEA-VLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  92 LGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQ 171
Cdd:cd01556   78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 172 FLTALLMTAPLAPQDTVITIkGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPgNYLVEGDASSASYFLA 251
Cdd:cd01556  158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 252 AGAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAIVTWGD-DFISCTH-GELNAIDMDMNHIPDAAMTIATAALFAKGTT 329
Cdd:cd01556  236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTP-PAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556  314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
                        410
                 ....*....|....*.
gi 695731700 408 CTAKTFPDYFEQLARI 423
Cdd:cd01556  394 CVAKSFPNFFEDLESL 409
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-423 2.99e-165

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: 470.22  E-value: 2.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   14 GTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrcEVTGNGGALRSGEeleLFLG 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGKEPQAE---LDLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   94 NAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQFL 173
Cdd:TIGR01356  76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  174 TALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGnYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  254 AIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHG-ELNAIDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  333 NIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
                         410
                  ....*....|..
gi 695731700  412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-420 6.46e-164

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 467.16  E-value: 6.46e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700    7 QPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGV-HYTLSDDRTRCEVTGNGGALRSG 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   86 EELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGfTGGHVEVD 165
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  166 GSVSSQFLTALLMTAPLAPQDTVITIkgELVSKPYIDITLHLMKTFGVEVENQ-SYQRFVVRGAQQYQSpGNYLVEGDAS 244
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIE--NLASEPYIDDTENMLKKFGAKIEGSgTELSITVKGGEKLPG-QEYRVEGDRS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  245 SASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDF-ISCTHGELNAIDMDMNHIPDAAMTIATAAL 323
Cdd:pfam00275 237 SAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLAA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  324 FAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK-LQFAEIGTYNDHRMAMCFSLVAL-SDTPV 401
Cdd:pfam00275 317 FAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGET 396
                         410
                  ....*....|....*....
gi 695731700  402 TILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 397 IIDDIECTDRSFPDFEEKL 415
 
Name Accession Description Interval E-value
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
1-423 0e+00

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: 607.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDrTRCEVTGNGG 80
Cdd:COG0128    1 MSSLTIAPPSPLKGTVRVPGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALGAEIEELDG-GTLRVTGVGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALRsGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEqENYPPLRLRGG-FTG 159
Cdd:COG0128   80 GLK-EPDAVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGpLKG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLV 239
Cdd:COG0128  158 GEYEIPGSASSQFKSALLLAGPLAEGGLEITVTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQRYR-PGDYTV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIPDAAMTIA 319
Cdd:COG0128  237 PGDISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGILDILKEMGADIEIENDGITVRGSPLKGIDIDLSDIPDEAPTLA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 320 TAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SD 398
Cdd:COG0128  317 VLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPKLKGAEVDSYGDHRIAMAFAVAGLrAE 396
                        410       420
                 ....*....|....*....|....*
gi 695731700 399 TPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:COG0128  397 GPVTIDDAECVAKSFPDFFELLESL 421
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
1-424 0e+00

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 606.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTRceVTGNGG 80
Cdd:PRK11860   4 TEFLDLPPLLSAGGTVRLPGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGCGVEQLGDTYR--ITGLGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALrSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGG--FT 158
Cdd:PRK11860  82 QF-PVKQADLFLGNAGTAMRPLTAALALLGGEYELSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAplRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 159 GGHVEVDGSVSSQFLTALLMTAPL-APQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGNY 237
Cdd:PRK11860 161 DAPIRVRGDVSSQFLTALLMALPLvARRDITIEVVGELISKPYIEITLNLLARFGIAVQREGWQRFTIPAGSRYRSPGEI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 238 LVEGDASSASYFLAAGAIKGGT-VKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHGE--LNAIDMDMNHIPDA 314
Cdd:PRK11860 241 HVEGDASSASYFIAAGAIAGGApVRIEGVGRDSIQGDIRFAEAARAMGAQVTSGPNWLEVRRGAwpLKAIDLDCNHIPDA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 315 AMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK---LQFAEIGTYNDHRMAMCF 391
Cdd:PRK11860 321 AMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQaadWKAAAIHTYDDHRMAMCF 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 695731700 392 SLVAL--SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK11860 401 SLAAFnpAGLPVRINDPKCVAKTFPDYFEALFSVA 435
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-424 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 590.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYtlsdDRTRCEVTGNGG 80
Cdd:PRK02427   2 MMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGVEI----EDDEVVVEGVGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALRSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYlEQENYPPLRLRGGFTGG 160
Cdd:PRK02427  78 GGLKEPEDVLDCGNSGTTMRLLTGLLALQPGEVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRGGKKGG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 161 HVEVDGSVSSQFLTALLMTAPL-APQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQ---SYQRFVVRGAQQYQsPGN 236
Cdd:PRK02427 157 PIEYDGPVSSQFVKSLLLLAPLfAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVegwGYRRIVIKGGQRLR-GQD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 237 YLVEGDASSASYFLAAGAIKGG-TVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDF--------ISCTHGELNAIDMD 307
Cdd:PRK02427 236 ITVPGDPSSAAFFLAAAAITGGsEVTITNVGLNSTQGGKAIIDVLEKMGADIEIENEReggepvgdIRVRSSELKGIDID 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 308 MNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLqfAEIGTYNDHRM 387
Cdd:PRK02427 316 IPDIIDEAPTLAVLAAFAEGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGPLA--GVVDSYGDHRI 393
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 695731700 388 AMCFSLVAL-SDTPVTILDPKCTAKTFPDYFEQLARIS 424
Cdd:PRK02427 394 AMAFAIAGLaAEGPVTIDDPECVAKSFPDFFEDLASLG 431
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
1-425 0e+00

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 570.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTRCEVTGNGG 80
Cdd:PLN02338   1 AEEITLQPIKEISGTVKLPGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGLNVEEDSENNRAVVEGCGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALRSG----EELELFLGNAGTAMRPLAAALCLGSNN--IVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRL- 153
Cdd:PLN02338  81 KFPVSgdskEDVELFLGNAGTAMRPLTAAVTAAGGNasYVLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVn 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 154 -RGGFTGGHVEVDGSVSSQFLTALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQ-SYQRFVVRGAQQY 231
Cdd:PLN02338 161 aAGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSdSWDRFFIKGGQKY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 232 QSPGNYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCT--------HGELNA 303
Cdd:PLN02338 241 KSPGNAYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFAEVLEKMGAKVEWTENSVTVTgpprdafgGKHLKA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 304 IDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYN 383
Cdd:PLN02338 321 IDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIITPPKKLKPAEIDTYD 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 695731700 384 DHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARIST 425
Cdd:PLN02338 401 DHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLESIAK 442
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
12-423 0e+00

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: 551.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRtrCEVTGNGGALRSGEElELF 91
Cdd:cd01556    1 LSGEITVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGAKIEEEGGT--VEIVGGGGLGLPPEA-VLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  92 LGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQ 171
Cdd:cd01556   78 CGNSGTTMRLLTGLLALQGGDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIGGGGLKGGEVEIPGAVSSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 172 FLTALLMTAPLAPQDTVITIkGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPgNYLVEGDASSASYFLA 251
Cdd:cd01556  158 FKSALLLAAPLAEGPTTIII-GELESKPYIDHTERMLRAFGAEVEVDGYRTITVKGGQKYKGP-EYTVEGDASSAAFFLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 252 AGAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAIVTWGD-DFISCTH-GELNAIDMDMNHIPDAAMTIATAALFAKGTT 329
Cdd:cd01556  236 AAAITGSEIVIKNVGLNS--GDTGIIDVLKEMGADIEIGNeDTVVVESgGKLKGIDIDGNDIPDEAPTLAVLAAFAEGPT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 330 TLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTP-PAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01556  314 RIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGgPLKGAGVEVYTYGDHRIAMSFAIAGLvAEGGVTIEDPE 393
                        410
                 ....*....|....*.
gi 695731700 408 CTAKTFPDYFEQLARI 423
Cdd:cd01556  394 CVAKSFPNFFEDLESL 409
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
12-423 0e+00

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: 544.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  12 VDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDdrTRCEVTGNGGALRSGEELELF 91
Cdd:cd01554    1 LHGIIRVPGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGVEIEDKD--GVITIQGVGMAGLKAPQNALN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  92 LGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQ 171
Cdd:cd01554   79 LGNSGTAIRLISGVLAGADFEVELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKGGKNLGPIHYEDPIASAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 172 FLTALLMTAPLAPQDTVITIKgelVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPgNYLVEGDASSASYFLA 251
Cdd:cd01554  159 VKSALMFAALLAKGETVIIEA---AKEPTINHTENMLQTFGGHISVQGTKKIVVQGPQKLTGQ-KYVVPGDISSAAFFLV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 252 AGAIKGGTVKVTGIGRNSvqGDIRFADVLEKMGAIVTWGDDFISCTHGELNAIDMDMNHIP---DAAMTIATAALFAKGT 328
Cdd:cd01554  235 AAAIAPGRLVLQNVGINE--TRTGIIDVLRAMGAKIEIGEDTISVESSDLKATEICGALIPrliDELPIIALLALQAQGT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 329 TTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPK 407
Cdd:cd01554  313 TVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLHGARVNTFGDHRIGMMTALAALvADGEVELDRAE 392
                        410
                 ....*....|....*.
gi 695731700 408 CTAKTFPDYFEQLARI 423
Cdd:cd01554  393 AINTSYPSFFDDLESL 408
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
14-423 2.99e-165

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: 470.22  E-value: 2.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   14 GTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrcEVTGNGGALRSGEeleLFLG 93
Cdd:TIGR01356   1 GEIRAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKIEDGGEVA--VIEGVGGKEPQAE---LDLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   94 NAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTGGHVEVDGSVSSQFL 173
Cdd:TIGR01356  76 NSGTTARLLTGVLALADGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTISGPLPGGIVYISGSASSQYK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  174 TALLMTAPLAPQDTVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPGnYLVEGDASSASYFLAAG 253
Cdd:TIGR01356 156 SALLLAAPALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGRKIVVPGGQKYGPQG-YDVPGDYSSAAFFLAAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  254 AIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISCTHG-ELNAIDMDMNHIPDAAMTIATAALFAKGTTTLR 332
Cdd:TIGR01356 235 AITGGRVTLENLGINPTQGDKAIIIVLEEMGADIEVEEDDLIVEGAsGLKGIKIDMDDMIDELPTLAVLAAFAEGVTRIT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  333 NIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQFAEIGTYNDHRMAMCFSLVAL-SDTPVTILDPKCTAK 411
Cdd:TIGR01356 315 GAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKKELKGAVVDTFGDHRIAMAFAVAGLvAEGEVLIDDPECVAK 394
                         410
                  ....*....|..
gi 695731700  412 TFPDYFEQLARI 423
Cdd:TIGR01356 395 SFPSFFDVLERL 406
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
7-420 6.46e-164

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 467.16  E-value: 6.46e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700    7 QPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGV-HYTLSDDRTRCEVTGNGGALRSG 85
Cdd:pfam00275   1 TGGSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAeIIKLDDEKSVVIVEGLGGSFEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   86 EELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGfTGGHVEVD 165
Cdd:pfam00275  81 EDLVLDMGNSGTALRPLTGRLALQSGEVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGL-RLGGIHID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  166 GSVSSQFLTALLMTAPLAPQDTVITIkgELVSKPYIDITLHLMKTFGVEVENQ-SYQRFVVRGAQQYQSpGNYLVEGDAS 244
Cdd:pfam00275 160 GDVSSQFVTSLLMLAALLAEGTTTIE--NLASEPYIDDTENMLKKFGAKIEGSgTELSITVKGGEKLPG-QEYRVEGDRS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  245 SASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDF-ISCTHGELNAIDMDMNHIPDAAMTIATAAL 323
Cdd:pfam00275 237 SAAYFLVAAAITGGTVTVENVGINSLQGDEALLEILEKMGAEITQEEDAdIVVGPPGLRGKAVDIRTAPDPAPTTAVLAA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  324 FAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAK-LQFAEIGTYNDHRMAMCFSLVAL-SDTPV 401
Cdd:pfam00275 317 FAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVKeLKGAEVDSYGDHRIAMALALAGLvAEGET 396
                         410
                  ....*....|....*....
gi 695731700  402 TILDPKCTAKTFPDYFEQL 420
Cdd:pfam00275 397 IIDDIECTDRSFPDFEEKL 415
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
1-420 4.62e-159

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 464.18  E-value: 4.62e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   1 MESLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVhyTLSDDRTRCEVTGNGG 80
Cdd:PRK11861 240 MEHLDLGPFSHAQGTVRLPGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGV--KLSRDGGTCVVGGTRG 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  81 ALrSGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEYLEQENYPPLRLRGGFTG- 159
Cdd:PRK11861 318 AF-TAKTADLFLGNAGTAVRPLTAALAVNGGEYRIHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISv 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 -GHVEVDGSVSSQFLTALLMTAPLAPQD---TVITIKGELVSKPYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQSPG 235
Cdd:PRK11861 397 dAPIRVRGDVSSQFLTALLMTLPLVKAKdgaSVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFTVPAGVRYRSPG 476
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 236 NYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGAIVTWGDDFISC-----THGELNAIDMDMNH 310
Cdd:PRK11861 477 TIMVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQMGANVTMGDDWIEVrgighDHGRLAPIDMDFNL 556
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 311 IPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTPPAKLQ-FAEIGTYNDHRMAM 389
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLTpNASIDTYDDHRMAM 636
                        410       420       430
                 ....*....|....*....|....*....|.
gi 695731700 390 CFSLVALSDTPVTILDPKCTAKTFPDYFEQL 420
Cdd:PRK11861 637 CFSLVSLGGVPVRINDPKCVGKTFPDYFDRF 667
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
240-423 1.80e-57

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: 187.87  E-value: 1.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGTVKVTGIGRNSV-----QGDIRFADVLEKM-GAIVTWG---DDFISCTHGELNAIDMDMNH 310
Cdd:cd01553    7 KGGGQILRSFLVLAAISGGPITVTGIRPDRAkpgllRQHLTFLKALEKIcGATVEGGelgSDRISFRPGTVRGGDVRFAI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 311 -----IPDAAMTIATAALFAKGTTTLRNIYNWRV----KETDRLFAMATELRKVGAEVEEGED------------YIRVT 369
Cdd:cd01553   87 gsagsCTDVLQTILPLLLFAKGPTRLTVTGGTDNpsapPADFIRFVLEPELAKIGAHQEETLLrhgfypagggvvATEVS 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 695731700 370 PPAKLQFAEIgtyndhRMAMCFSLVAlsdTPVTILDPKCTAKTFPDYFEQLARI 423
Cdd:cd01553  167 PVEKLNTAQL------RQLVLPMLLA---SGAVEFTVAHPSCHLLTNFAVLEAL 211
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
3-422 1.82e-39

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 150.53  E-value: 1.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700   3 SLTLQPIARVDGTINLPGSKSVSNRALLLAALANGTTVLTNLLDSDDVRHMLNALKALGVhytLSDDRTRCEVTGNGGAL 82
Cdd:PRK14806 303 SYSVLPGGAVKGTIRVPGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMGV---VIEGPHNGRVTIHGVGL 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  83 R--SGEELELFLGNAGTAMRPLAAALCLGSNNIVLTGEPRMKERPIGHLVDALRQGGAQIEyLEQENYPPLRLRGGFTGG 160
Cdd:PRK14806 380 HglKAPPGPLYMGNSGTSMRLLSGLLAAQSFDSVLTGDASLSKRPMERVAKPLREMGAVIE-TGEEGRPPLSIRGGQRLK 458
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 161 HVEVDGSV-SSQFLTALLMTAPLAPQDTVITikgELvsKPYIDITLHLMKTFGVEVENQSyQRFVVRGAQQYQSpGNYLV 239
Cdd:PRK14806 459 GIHYDLPMaSAQVKSCLLLAGLYAEGETSVT---EP--APTRDHTERMLRGFGYPVKVEG-NTISVEGGGKLTA-TDIEV 531
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 240 EGDASSASYFLAAGAIKGGT-VKVTGIGRNSVQgdIRFADVLEKMGAIVTW-----------GDdfISCTHGELNAIDMD 307
Cdd:PRK14806 532 PADISSAAFFLVAASIAEGSeLTLEHVGINPTR--TGVIDILKLMGADITLenerevggepvAD--IRVRGARLKGIDIP 607
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 308 MNHIPDA-----AMTIATAalFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRVTppAKLQFA-EIGT 381
Cdd:PRK14806 608 EDQVPLAidefpVLFVAAA--CAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIE--GGIFGGgEVES 683
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 695731700 382 YNDHRMAMCFSLVAL-SDTPVTILDPKCTAKTFPDyFEQLAR 422
Cdd:PRK14806 684 HGDHRIAMSFSVASLrASGPITIHDCANVATSFPN-FLELAN 724
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
36-379 3.25e-11

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: 64.62  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  36 NGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrceVTGNGGALRSGE---ELelflgnaGTAMRplAAALCLGSnn 112
Cdd:COG0766   36 DGPVTLRNVPDLSDVRTMLELLESLGVKVERDDGGT---LTIDASNINSTEapyEL-------VRKMR--ASILVLGP-- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 113 ivLTGepRMKE-------------RPIG-HLvDALRQGGAQIEYlEQENYpplRLR-GGFTGGHVEVDG-SVssqflTA- 175
Cdd:COG0766  102 --LLA--RFGEarvslpggcaigaRPIDlHL-KGLEALGAEIEI-EHGYI---EARaGRLKGARIYLDFpSV-----GAt 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 176 --LLMTAPLAPQDTVItikgELVSK-PYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYqSPGNYLVEGD---ASSasyF 249
Cdd:COG0766  168 enIMMAAVLAEGTTVI----ENAARePEIVDLANFLNAMGAKIEGAGTDTITIEGVEKL-HGAEHTVIPDrieAGT---F 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 250 LAAGAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAIVTWGDDFISCT-HGELNAIDM----------DMNHIpdaAMT 317
Cdd:COG0766  240 LVAAAITGGDVTVKNV----IPEHLEaVLAKLREAGVEIEEGDDGIRVRgPGRLKAVDIktapypgfptDLQAQ---FMA 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695731700 318 IATaalFAKGTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGeDYIRVTPPAKLQFAEI 379
Cdd:COG0766  313 LLT---QAEGTSVITeTVFENR-------FMHVDELNRMGADIKlDG-HTAIVRGVTKLSGAPV 365
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
36-379 8.78e-08

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: 54.02  E-value: 8.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  36 NGTTVLTNLLDSDDVRHMLNALKALGVHYtlsddrtrcEVTGNGGAL---RSGEELELFLGNAGTaMRplAAALCLGsnn 112
Cdd:cd01555   25 DEPVTLRNVPDLLDVETMIELLRSLGAKV---------EFEGENTLVidaSNINSTEAPYELVRK-MR--ASILVLG--- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 113 iVLTGepRMKE-------------RPIG-HLVdALRQGGAQIEylEQENYPPLRLRGGFTGGHVEVD-GSVssqflTA-- 175
Cdd:cd01555   90 -PLLA--RFGEarvslpggcaigaRPVDlHLK-GLEALGAKIE--IEDGYVEAKAAGRLKGARIYLDfPSV-----GAte 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 176 -LLMTAPLAPQDTVItikgELVSK-PYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYQsPGNYLVEGDASSASYFLAAG 253
Cdd:cd01555  159 nIMMAAVLAEGTTVI----ENAARePEIVDLANFLNKMGAKIEGAGTDTIRIEGVERLH-GAEHTVIPDRIEAGTFLVAA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 254 AIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAIVTWGDDFISCTH--GELNAIDMDMNHIP----DAAMTIATAALFAK 326
Cdd:cd01555  234 AITGGDITVENV----IPEHLEaVLAKLREMGAKIEIGEDGIRVDGdgGRLKAVDIETAPYPgfptDLQAQFMALLTQAE 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 695731700 327 GTTTLR-NIYNWRvketdrlFAMATELRKVGAEVE-EGEDYIrVTPPAKLQFAEI 379
Cdd:cd01555  310 GTSVITeTIFENR-------FMHVDELNRMGADIKvEGNTAI-IRGVTKLSGAPV 356
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
36-360 1.29e-05

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 46.95  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700  36 NGTTVLTNLLDSDDVRHMLNALKALGVHYTLSDDRTrceVTGNGGALRSGE---ELelflgnAGTaMRplAAALCLGsnn 112
Cdd:PRK09369  36 EEPVTLTNVPDLSDVRTMIELLRSLGAKVEFDGNGT---VTIDASNINNTEapyEL------VKK-MR--ASILVLG--- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 113 ivltgeP---RMKE-------------RPIG-HLvDALRQGGAQIEylEQENYPPLRLRGGFTGGHVEVDG-SVssqflT 174
Cdd:PRK09369 101 ------PllaRFGEakvslpggcaigaRPVDlHL-KGLEALGAEIE--IEHGYVEAKADGRLKGAHIVLDFpSV-----G 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 175 A---LLMTAPLAPQDTVItikgELVSK-PYIDITLHLMKTFGVEVENQSYQRFVVRGAQQYqSPGNYLVEGDASSASYFL 250
Cdd:PRK09369 167 AtenILMAAVLAEGTTVI----ENAARePEIVDLANFLNKMGAKISGAGTDTITIEGVERL-HGAEHTVIPDRIEAGTFL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 251 AAGAIKGGTVKVTGIgrnsVQGDIR-FADVLEKMGAIVTWGDDFISCT-HGELNAIDM----------DMNhipdaAMTI 318
Cdd:PRK09369 242 VAAAITGGDVTIRGA----RPEHLEaVLAKLREAGAEIEEGEDGIRVDmPGRLKAVDIktapypgfptDMQ-----AQFM 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 695731700 319 ATAALfAKGTTTlrniynwrVKET---DRLFaMATELRKVGAEVE 360
Cdd:PRK09369 313 ALLTQ-AEGTSV--------ITETifeNRFM-HVPELIRMGADIE 347
PRK12830 PRK12830
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed
246-379 3.47e-05

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed


Pssm-ID: 183779  Cd Length: 417  Bit Score: 45.62  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 246 ASYFLAAGAIKGGTVKVTGIGRNSVQGdirFADVLEKMGAIVTWGDDFIS-CTHGELNAIDMDMNHIP----DAAMTIAT 320
Cdd:PRK12830 235 AGTYMILAAACGGGVTINNVIPEHLES---FIAKLEEMGVRVEVNEDSIFvEKQGNLKAVDIKTLPYPgfatDLQQPLTP 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 321 AALFAKGTTTLR-NIYNWRVKETDrlfamatELRKVGAEVEEGEDYIRVTPPAKLQFAEI 379
Cdd:PRK12830 312 LLLKANGRSVVTdTIYEKRFKHVD-------ELKRMGANIKVEGRSAIITGPSKLTGAKV 364
PRK09369 PRK09369
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated
277-375 2.67e-04

UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated


Pssm-ID: 236486  Cd Length: 417  Bit Score: 43.10  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 277 ADVLEKMGAIVT-WGDDFI---------SCTHgelnAIdmdmnhIPD---AAmTIATAALFAKGTTTLRNIynwrvkETD 343
Cdd:PRK09369 197 ANFLNKMGAKISgAGTDTItiegverlhGAEH----TV------IPDrieAG-TFLVAAAITGGDVTIRGA------RPE 259
                         90       100       110
                 ....*....|....*....|....*....|..
gi 695731700 344 RLFAMATELRKVGAEVEEGEDYIRVTPPAKLQ 375
Cdd:PRK09369 260 HLEAVLAKLREAGAEIEEGEDGIRVDMPGRLK 291
MurA COG0766
UDP-N-acetylglucosamine enolpyruvyl transferase [Cell wall/membrane/envelope biogenesis]; ...
278-382 1.16e-03

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: 41.12  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 278 DVLEKMGAIVTWGDDFISCTHGEL--NAIDMDMnhiPD--AAMTIATAALFAKGTTTLRNIYnwrvKE---TDrlfaMAT 350
Cdd:COG0766  129 KGLEALGAEIEIEHGYIEARAGRLkgARIYLDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD----LAN 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 695731700 351 ELRKVGAEVE-EGEDYIRVTPPAKLQFA---------EIGTY 382
Cdd:COG0766  198 FLNAMGAKIEgAGTDTITIEGVEKLHGAehtvipdriEAGTF 239
UdpNAET cd01555
UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the ...
160-378 2.69e-03

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: 39.76  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 160 GHVEVDGSVSSqfLTALLMTAPLAPQDTVIT----IKGelvskpyIDITLHLMKTFGVEVENQSYQRFVV--RGAQQYQS 233
Cdd:cd01555    3 GEVRISGAKNA--ALPILAAALLTDEPVTLRnvpdLLD-------VETMIELLRSLGAKVEFEGENTLVIdaSNINSTEA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 234 PGNYlvegdASS--ASyFLAAGAI--KGGTVKVTG-----IGRNSVQGDIRfadVLEKMGAIVTWGDDFISCTH-GEL-- 301
Cdd:cd01555   74 PYEL-----VRKmrAS-ILVLGPLlaRFGEARVSLpggcaIGARPVDLHLK---GLEALGAKIEIEDGYVEAKAaGRLkg 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695731700 302 NAIDMDMnhiPD--AAMTIATAALFAKGTTTLRNIYnwrvKE---TDrlfaMATELRKVGAEVE-EGEDYIRVTPPAKLQ 375
Cdd:cd01555  145 ARIYLDF---PSvgATENIMMAAVLAEGTTVIENAA----REpeiVD----LANFLNKMGAKIEgAGTDTIRIEGVERLH 213

                 ...
gi 695731700 376 FAE 378
Cdd:cd01555  214 GAE 216
 
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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