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Conserved domains on  [gi|1049098|gb|AAA97399|]
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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
aroA super family cl29621
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 1-108 4.37e-30

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]


The actual alignment was detected with superfamily member TIGR01356:

Pssm-ID: 273574  Cd Length: 409  Bit Score: 110.44  E-value: 4.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098      1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKisDLLSPTngVNCYNDH 80
Cdd:TIGR01356 297 LPTLAVLAAFA-----EGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKK--ELKGAV--VDTFGDH 367

                          90       100
                  ....*....|....*....|....*...
gi 1049098     81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:TIGR01356 368 RIAMAFAVAGLVAEGEVLIDDPECVAKS 395
 
Name Accession Description Interval E-value
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 1-108 4.37e-30

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: 110.44  E-value: 4.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098      1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKisDLLSPTngVNCYNDH 80
Cdd:TIGR01356 297 LPTLAVLAAFA-----EGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKK--ELKGAV--VDTFGDH 367

                          90       100
                  ....*....|....*....|....*...
gi 1049098     81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:TIGR01356 368 RIAMAFAVAGLVAEGEVLIDDPECVAKS 395
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 1-108 1.80e-29

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: 108.80  E-value: 1.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSlkiSDLLSPTNGVNCYNDH 80
Cdd:cd01556 299 APTLAVLAAFA-----EGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDH 370

                        90       100
                ....*....|....*....|....*...
gi 1049098   81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:cd01556 371 RIAMSFAIAGLVAEGGVTIEDPECVAKS 398
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 3-108 2.51e-28

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 106.00  E-value: 2.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098     3 TAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKisdllsPTNGVNCYNDHRI 82
Cdd:PRK02427 325 TLAVLAAFA-----EGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP------LAGVVDSYGDHRI 393

                         90       100
                 ....*....|....*....|....*.
gi 1049098    83 AMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:PRK02427 394 AMAFAIAGLAAEGPVTIDDPECVAKS 419
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 1-108 7.06e-28

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: 104.40  E-value: 7.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSlkiSDLLSPTNgVNCYNDH 80
Cdd:COG0128 312 APTLAVLAAFA-----EGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPKLKGAE-VDSYGDH 382

                        90       100
                ....*....|....*....|....*...
gi 1049098   81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:COG0128 383 RIAMAFAVAGLRAEGPVTIDDAECVAKS 410
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
20-108 8.74e-23

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 90.82  E-value: 8.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098     20 TEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKIsdLLSPTnGVNCYNDHRIAMSFSVLACVSPKPTII 99
Cdd:pfam00275 322 TRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVK--ELKGA-EVDSYGDHRIAMALALAGLVAEGETII 398


                  ....*....
gi 1049098    100 LDKTCINKT 108
Cdd:pfam00275 399 DDIECTDRS 407
 
Name Accession Description Interval E-value
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
 1-108 4.37e-30

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: 110.44  E-value: 4.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098      1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKisDLLSPTngVNCYNDH 80
Cdd:TIGR01356 297 LPTLAVLAAFA-----EGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGKK--ELKGAV--VDTFGDH 367

                          90       100
                  ....*....|....*....|....*...
gi 1049098     81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:TIGR01356 368 RIAMAFAVAGLVAEGEVLIDDPECVAKS 395
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
 1-108 1.80e-29

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: 108.80  E-value: 1.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSlkiSDLLSPTNGVNCYNDH 80
Cdd:cd01556 299 APTLAVLAAFA-----EGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDH 370

                        90       100
                ....*....|....*....|....*...
gi 1049098   81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:cd01556 371 RIAMSFAIAGLVAEGGVTIEDPECVAKS 398
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 3-108 2.51e-28

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 106.00  E-value: 2.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098     3 TAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKisdllsPTNGVNCYNDHRI 82
Cdd:PRK02427 325 TLAVLAAFA-----EGTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP------LAGVVDSYGDHRI 393

                         90       100
                 ....*....|....*....|....*.
gi 1049098    83 AMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:PRK02427 394 AMAFAIAGLAAEGPVTIDDPECVAKS 419
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
 1-108 7.06e-28

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: 104.40  E-value: 7.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    1 FLTAAILSSVAyeeskSSITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSlkiSDLLSPTNgVNCYNDH 80
Cdd:COG0128 312 APTLAVLAAFA-----EGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPKLKGAE-VDSYGDH 382

                        90       100
                ....*....|....*....|....*...
gi 1049098   81 RIAMSFSVLACVSPKPTIILDKTCINKT 108
Cdd:COG0128 383 RIAMAFAVAGLRAEGPVTIDDAECVAKS 410
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
20-108 8.74e-23

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 90.82  E-value: 8.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098     20 TEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKIsdLLSPTnGVNCYNDHRIAMSFSVLACVSPKPTII 99
Cdd:pfam00275 322 TRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAVK--ELKGA-EVDSYGDHRIAMALALAGLVAEGETII 398


                  ....*....
gi 1049098    100 LDKTCINKT 108
Cdd:pfam00275 399 DDIECTDRS 407
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
 19-108 7.79e-14

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: 65.70  E-value: 7.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098   19 ITEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLkisdllSPTNG--VNCYNDHRIAMSFSVLACVSPKP 96
Cdd:cd01554 312 TTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGK------EKLHGarVNTFGDHRIGMMTALAALVADGE 385

                        90
                ....*....|..
gi 1049098   97 TIILDKTCINKT 108
Cdd:cd01554 386 VELDRAEAINTS 397
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
20-108 1.03e-12

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 62.37  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    20 TEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSLKISDLLSPTnGVNCYNDHRIAMSFSvLACVSPK--PT 97
Cdd:PRK11860 335 TTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADWKAA-AIHTYDDHRMAMCFS-LAAFNPAglPV 412

                         90
                 ....*....|.
gi 1049098    98 IILDKTCINKT 108
Cdd:PRK11860 413 RINDPKCVAKT 423
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
 20-108 7.71e-11

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 57.07  E-value: 7.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    20 TEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYV---KSLKIsdllsptNGVNCYNDHRIAMSFSVLACvSPKP 96
Cdd:PLN02338 346 TAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCIItppKKLKP-------AEIDTYDDHRMAMAFSLAAC-GDVP 417

                         90
                 ....*....|..
gi 1049098    97 TIILDKTCINKT 108
Cdd:PLN02338 418 VTINDPGCTRKT 429
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 20-101 6.45e-10

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 54.62  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    20 TEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSlKIsdllsPTNG-VNCYNDHRIAMSFSVLACVSPKPTI 98
Cdd:PRK14806 632 TVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEG-GI-----FGGGeVESHGDHRIAMSFSVASLRASGPIT 705


                 ...
gi 1049098    99 ILD 101
Cdd:PRK14806 706 IHD 708
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 20-108 2.77e-08

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 50.09  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049098    20 TEITGISNQKIKECNRINAMIYELKKFGIEAGELPNGIYVKSlkiSDLLSPTNGVNCYNDHRIAMSFSvLACVSPKPTII 99
Cdd:PRK11861 575 STLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTP---PAQLTPNASIDTYDDHRMAMCFS-LVSLGGVPVRI 650


                 ....*....
gi 1049098   100 LDKTCINKT 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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