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Conserved domains on  [gi|1049100|gb|AAA97400|]
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encodes EPSP synthase domain, partial [Pneumocystis carinii f. sp. mustelae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EPT_RTPC-like super family cl00288
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
 1-108 5.06e-32

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.


The actual alignment was detected with superfamily member cd01556:

Pssm-ID: 444811  Cd Length: 409  Bit Score: 115.73  E-value: 5.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    1 FLTTAILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlniSDLLSPTNGIDCHNDH 80
Cdd:cd01556 299 APTLAVLAAFA--EGP---TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDH 370

                        90       100
                ....*....|....*....|....*...
gi 1049100   81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:cd01556 371 RIAMSFAIAGLVAEGGVTIEDPECVAKS 398
 
Name Accession Description Interval E-value
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 1-108 5.06e-32

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: 115.73  E-value: 5.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    1 FLTTAILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlniSDLLSPTNGIDCHNDH 80
Cdd:cd01556 299 APTLAVLAAFA--EGP---TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDH 370

                        90       100
                ....*....|....*....|....*...
gi 1049100   81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:cd01556 371 RIAMSFAIAGLVAEGGVTIEDPECVAKS 398
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 1-108 2.43e-31

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: 113.91  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100      1 FLTTAILASVAYKEsesciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRALniSDLLSPTngIDCHNDH 80
Cdd:TIGR01356 297 LPTLAVLAAFAEGV-----TRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGK--KELKGAV--VDTFGDH 367

                          90       100
                  ....*....|....*....|....*...
gi 1049100     81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:TIGR01356 368 RIAMAFAVAGLVAEGEVLIDDPECVAKS 395
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 5-108 9.30e-31

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 112.54  E-value: 9.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100     5 AILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRALnisdllSPTNGIDCHNDHRIAM 84
Cdd:PRK02427 327 AVLAAFA--EGT---TVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGG------PLAGVVDSYGDHRIAM 395

                         90       100
                 ....*....|....*....|....
gi 1049100    85 SFSVLACVSPNPTIILNKTCVNKT 108
Cdd:PRK02427 396 AFAIAGLAAEGPVTIDDPECVAKS 419
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 5-108 1.04e-30

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: 112.10  E-value: 1.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    5 AILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlniSDLLSPTNgIDCHNDHRIAM 84
Cdd:COG0128 316 AVLAAFA--EGT---TRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPKLKGAE-VDSYGDHRIAM 386

                        90       100
                ....*....|....*....|....
gi 1049100   85 SFSVLACVSPNPTIILNKTCVNKT 108
Cdd:COG0128 387 AFAVAGLRAEGPVTIDDAECVAKS 410
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
1-108 3.50e-22

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 88.89  E-value: 3.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100      1 FLTTAILASVAykeseSCITEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlnISDLLSPTnGIDCHNDH 80
Cdd:pfam00275 308 APTTAVLAAFA-----EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIP--AVKELKGA-EVDSYGDH 379

                          90       100
                  ....*....|....*....|....*...
gi 1049100     81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:pfam00275 380 RIAMALALAGLVAEGETIIDDIECTDRS 407
 
Name Accession Description Interval E-value
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 1-108 5.06e-32

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: 115.73  E-value: 5.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    1 FLTTAILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlniSDLLSPTNGIDCHNDH 80
Cdd:cd01556 299 APTLAVLAAFA--EGP---TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDH 370

                        90       100
                ....*....|....*....|....*...
gi 1049100   81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:cd01556 371 RIAMSFAIAGLVAEGGVTIEDPECVAKS 398
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 1-108 2.43e-31

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: 113.91  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100      1 FLTTAILASVAYKEsesciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRALniSDLLSPTngIDCHNDH 80
Cdd:TIGR01356 297 LPTLAVLAAFAEGV-----TRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGK--KELKGAV--VDTFGDH 367

                          90       100
                  ....*....|....*....|....*...
gi 1049100     81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:TIGR01356 368 RIAMAFAVAGLVAEGEVLIDDPECVAKS 395
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 5-108 9.30e-31

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 112.54  E-value: 9.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100     5 AILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRALnisdllSPTNGIDCHNDHRIAM 84
Cdd:PRK02427 327 AVLAAFA--EGT---TVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGG------PLAGVVDSYGDHRIAM 395

                         90       100
                 ....*....|....*....|....
gi 1049100    85 SFSVLACVSPNPTIILNKTCVNKT 108
Cdd:PRK02427 396 AFAIAGLAAEGPVTIDDPECVAKS 419
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 5-108 1.04e-30

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: 112.10  E-value: 1.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    5 AILASVAykESEsciTEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlniSDLLSPTNgIDCHNDHRIAM 84
Cdd:COG0128 316 AVLAAFA--EGT---TRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPKLKGAE-VDSYGDHRIAM 386

                        90       100
                ....*....|....*....|....
gi 1049100   85 SFSVLACVSPNPTIILNKTCVNKT 108
Cdd:COG0128 387 AFAVAGLRAEGPVTIDDAECVAKS 410
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
1-108 3.50e-22

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 88.89  E-value: 3.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100      1 FLTTAILASVAykeseSCITEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlnISDLLSPTnGIDCHNDH 80
Cdd:pfam00275 308 APTTAVLAAFA-----EGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIP--AVKELKGA-EVDSYGDH 379

                          90       100
                  ....*....|....*....|....*...
gi 1049100     81 RIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:pfam00275 380 RIAMALALAGLVAEGETIIDDIECTDRS 407
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
20-108 2.29e-15

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 70.08  E-value: 2.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    20 TEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRALNISDLLSPTnGIDCHNDHRIAMSFSvLACVSP--NPT 97
Cdd:PRK11860 335 TTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADWKAA-AIHTYDDHRMAMCFS-LAAFNPagLPV 412

                         90
                 ....*....|.
gi 1049100    98 IILNKTCVNKT 108
Cdd:PRK11860 413 RINDPKCVAKT 423
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 5-99 7.35e-13

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 63.09  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100     5 AILASVAYKESESCITeitGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRALnisdllSPTNG-IDCHNDHRIA 83
Cdd:PRK14806 620 VLFVAAACAEGRTVLT---GAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGG------IFGGGeVESHGDHRIA 690

                         90
                 ....*....|....*.
gi 1049100    84 MSFSVLACVSPNPTII 99
Cdd:PRK14806 691 MSFSVASLRASGPITI 706
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 3-108 3.11e-11

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: 58.38  E-value: 3.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    3 TTAILASVAykeseSCITEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIY---VRALNISDllsptngIDCHND 79
Cdd:cd01554 301 IIALLALQA-----QGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIikgKEKLHGAR-------VNTFGD 368

                        90       100
                ....*....|....*....|....*....
gi 1049100   80 HRIAMSFSVLACVSPNPTIILNKTCVNKT 108
Cdd:cd01554 369 HRIGMMTALAALVADGEVELDRAEAINTS 397
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
 20-108 3.75e-11

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 57.84  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    20 TEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYV---RALNIsdllsptNGIDCHNDHRIAMSFSVLACvSPNP 96
Cdd:PLN02338 346 TAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIItppKKLKP-------AEIDTYDDHRMAMAFSLAAC-GDVP 417

                         90
                 ....*....|..
gi 1049100    97 TIILNKTCVNKT 108
Cdd:PLN02338 418 VTINDPGCTRKT 429
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 20-108 1.02e-08

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 51.25  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049100    20 TEITGISNQRIKECNRINAMVCEFKKFGIEAGELPDGIYVRAlniSDLLSPTNGIDCHNDHRIAMSFSvLACVSPNPTII 99
Cdd:PRK11861 575 STLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTP---PAQLTPNASIDTYDDHRMAMCFS-LVSLGGVPVRI 650


                 ....*....
gi 1049100   100 LNKTCVNKT 108
Cdd:PRK11861 651 NDPKCVGKT 659
 
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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