pheA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

PheA

Synonyms

fused chorismate mutase P[1], prephenate dehydratase[1], B2599[2][1], PheA[2][1] , ECK2596, JW2580, b2599

Product description

PheA[2][3];

Component of CHORISMUTPREPHENDEHYDRAT-CPLX[2]

Phenylalanine synthesis, bifunctional: chorismate mutase (N) and prephenate dehydratase (central); also contains Phe-binding regulatory domain (C); FPA resistance[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0004106

chorismate mutase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008242

F

Seeded from EcoCyc (v14.0)

complete

GO:0004106

chorismate mutase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010952

F

Seeded from EcoCyc (v14.0)

complete

GO:0004106

chorismate mutase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:5.4.99.5

F

Seeded from EcoCyc (v14.0)

complete

GO:0004106

chorismate mutase activity

PMID:7030214[5]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc (v14.0)

complete

GO:0004106

chorismate mutase activity

PMID:9497350[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0004664

prephenate dehydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001086

F

Seeded from EcoCyc (v14.0)

complete

GO:0004664

prephenate dehydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008242

F

Seeded from EcoCyc (v14.0)

complete

GO:0004664

prephenate dehydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018528

F

Seeded from EcoCyc (v14.0)

complete

GO:0004664

prephenate dehydratase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:4.2.1.51

F

Seeded from EcoCyc (v14.0)

complete

GO:0004664

prephenate dehydratase activity

PMID:7030214[5]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc (v14.0)

complete

GO:0004664

prephenate dehydratase activity

PMID:9497350[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008242

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010952

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0006571

tyrosine biosynthetic process

PMID:7030214[5]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001086

P

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008242

P

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010952

P

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018528

P

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0584

P

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

PMID:7030214[5]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0042803

protein homodimerization activity

PMID:4557843[7]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of CHORISMUTPREPHENDEHYDRAT-CPLX

could be indirect

Protein

eutD

PMID:16606699[8]

Experiment(s):EBI-1143449
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID RERDLLERLI
TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN PHSARIAFLG PKGSYSHLAA
RQYAARHFEQ FIESGCAKFA DIFNQVETGQ ADYAVVPIEN TSSGAINDVY DLLQHTSLSI
VGEMTLTIDH CLLVSGTTDL STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK
VAQAKSPHVA ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL
LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL ESAEMQKALK
ELGEITRSMK VLGCYPSENV VPVDPT
Length

386

Mol. Wt

43.111 kDa

pI

6.7 (calculated)

Extinction coefficient

27,390 - 27,890 (calc based on 11 Y, 2 W, and 4 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

11..91

PF01817 Chorismate mutase type II

PMID:19920124[9]

Domain

106..288

PF00800 Prephenate dehydratase

PMID:19920124[9]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=pheA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130520

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947081

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0008545

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A9J8

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10707

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10707

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947081

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000699

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0701

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 5.3 Baldwin, GS & Davidson, BE (1981) A kinetic and structural comparison of chorismate mutase/prephenate dehydratase from mutant strains of Escherichia coli K 12 defective in the PheA gene. Arch. Biochem. Biophys. 211 66-75 PubMed
  6. ↑ 6.0 6.1 Zhang, S et al. (1998) Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. J. Biol. Chem. 273 6248-53 PubMed
  7. ↑ Davidson, BE et al. (1972) Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. I. Purification, molecular weight, and amino acid composition. J. Biol. Chem. 247 4441-6 PubMed
  8. ↑ Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  9. ↑ 9.0 9.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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