SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A9J8

- PHEA_ECOLI

UniProt

P0A9J8 - PHEA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
P-protein
Gene
pheA, b2599, JW2580
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.1 Publication

Catalytic activityi

Chorismate = prephenate.
Prephenate = phenylpyruvate + H2O + CO2.

Enzyme regulationi

Inhibited by L-phenylalanine.1 Publication

Kineticsi

  1. KM=45 µM for chorismate (at pH 7.8 and at 37 degrees Celsius, 1 Publication)2 Publications
  2. KM=100 µM for prephenate (at pH 7.8 and at 37 degrees Celsius, 1 Publication)
  3. KM=147 µM for chorismate (at pH 4.9)
  4. KM=296 µM for chorismate (at pH 7.5)

Temperature dependencei

Optimum temperature is 7.3 degrees Celsius for chorismate mutase.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111Substrate
Binding sitei28 – 281Substrate
Binding sitei39 – 391Substrate
Binding sitei48 – 481Substrate
Binding sitei52 – 521Substrate
Binding sitei84 – 841Substrate
Binding sitei88 – 881Substrate
Sitei278 – 2781Essential for prephenate dehydratase activity Reviewed prediction

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. chorismate mutase activity Source: EcoCyc
  3. prephenate dehydratase activity Source: EcoCyc

GO - Biological processi

  1. L-phenylalanine biosynthetic process Source: EcoCyc
  2. chorismate metabolic process Source: InterPro
  3. tyrosine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
ECOL316407:JW2580-MONOMER.
MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
SABIO-RKP0A9J8.
UniPathwayiUPA00120; UER00203.
UPA00121; UER00345.

Names & Taxonomyi

Protein namesi
Recommended name:
P-protein
Including the following 2 domains:
Chorismate mutase (EC:5.4.99.5)
Short name:
CM
Prephenate dehydratase (EC:4.2.1.51)
Short name:
PDT
Gene namesi
Name:pheA
Ordered Locus Names:b2599, JW2580
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10707. pheA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111R → A: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi11 – 111R → K: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi28 – 281R → A: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi28 – 281R → K: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi39 – 391K → A: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi39 – 391K → Q: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi39 – 391K → R: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi52 – 521E → A: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi52 – 521E → D: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi52 – 521E → Q: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi88 – 881Q → A: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi88 – 881Q → E: Important decrease in catalytic efficiency and affinity. 1 Publication
Mutagenesisi88 – 881Q → K: Important decrease in catalytic efficiency and affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386P-protein
PRO_0000119185Add
BLAST

Proteomic databases

PaxDbiP0A9J8.
PRIDEiP0A9J8.

Expressioni

Gene expression databases

GenevestigatoriP0A9J8.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-36017N.
IntActiP0A9J8. 17 interactions.
MINTiMINT-1248118.
STRINGi511145.b2599.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 4136
Helixi49 – 6517
Helixi70 – 9324

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECMX-ray2.20A/B1-109[»]
ProteinModelPortaliP0A9J8.

Miscellaneous databases

EvolutionaryTraceiP0A9J8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292Chorismate mutase
Add
BLAST
Domaini105 – 285181Prephenate dehydratase
Add
BLAST
Domaini299 – 37678ACT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 386101Regulatory (Phe-binding)
Add
BLAST

Sequence similaritiesi

Contains 1 ACT domain.

Phylogenomic databases

eggNOGiCOG0077.
HOGENOMiHOG000018972.
KOiK14170.
OMAiIDVQANL.
OrthoDBiEOG6WHNT1.
PhylomeDBiP0A9J8.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
InterProiIPR002912. ACT_dom.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR010952. CM_P_1.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01797. CM_P_1. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9J8-1 [UniParc]FASTAAdd to Basket

« Hide

MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID    50
RERDLLERLI TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN 100
PHSARIAFLG PKGSYSHLAA RQYAARHFEQ FIESGCAKFA DIFNQVETGQ 150
ADYAVVPIEN TSSGAINDVY DLLQHTSLSI VGEMTLTIDH CLLVSGTTDL 200
STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK VAQAKSPHVA 250
ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL 300
LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL 350
ESAEMQKALK ELGEITRSMK VLGCYPSENV VPVDPT 386
Length:386
Mass (Da):43,111
Last modified:April 1, 1988 - v1
Checksum:i4B0960854C75A4F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10431 Genomic DNA. Translation: AAA24330.1.
U00096 Genomic DNA. Translation: AAC75648.1.
AP009048 Genomic DNA. Translation: BAA16484.1.
M58024 Genomic DNA. Translation: AAA62784.1.
V00314 Genomic DNA. Translation: CAA23601.1.
PIRiA30261. KMECPW.
RefSeqiNP_417090.1. NC_000913.3.
YP_490822.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75648; AAC75648; b2599.
BAA16484; BAA16484; BAA16484.
GeneIDi12934467.
947081.
KEGGiecj:Y75_p2547.
eco:b2599.
PATRICi32120597. VBIEscCol129921_2697.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10431 Genomic DNA. Translation: AAA24330.1 .
U00096 Genomic DNA. Translation: AAC75648.1 .
AP009048 Genomic DNA. Translation: BAA16484.1 .
M58024 Genomic DNA. Translation: AAA62784.1 .
V00314 Genomic DNA. Translation: CAA23601.1 .
PIRi A30261. KMECPW.
RefSeqi NP_417090.1. NC_000913.3.
YP_490822.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ECM X-ray 2.20 A/B 1-109 [» ]
ProteinModelPortali P0A9J8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36017N.
IntActi P0A9J8. 17 interactions.
MINTi MINT-1248118.
STRINGi 511145.b2599.

Proteomic databases

PaxDbi P0A9J8.
PRIDEi P0A9J8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75648 ; AAC75648 ; b2599 .
BAA16484 ; BAA16484 ; BAA16484 .
GeneIDi 12934467.
947081.
KEGGi ecj:Y75_p2547.
eco:b2599.
PATRICi 32120597. VBIEscCol129921_2697.

Organism-specific databases

EchoBASEi EB0701.
EcoGenei EG10707. pheA.

Phylogenomic databases

eggNOGi COG0077.
HOGENOMi HOG000018972.
KOi K14170.
OMAi IDVQANL.
OrthoDBi EOG6WHNT1.
PhylomeDBi P0A9J8.

Enzyme and pathway databases

UniPathwayi UPA00120 ; UER00203 .
UPA00121 ; UER00345 .
BioCyci EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
ECOL316407:JW2580-MONOMER.
MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
SABIO-RK P0A9J8.

Miscellaneous databases

EvolutionaryTracei P0A9J8.
PROi P0A9J8.

Gene expression databases

Genevestigatori P0A9J8.

Family and domain databases

Gene3Di 1.20.59.10. 1 hit.
InterProi IPR002912. ACT_dom.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR010952. CM_P_1.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view ]
Pfami PF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view ]
PIRSFi PIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTi SM00830. CM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF48600. SSF48600. 1 hit.
TIGRFAMsi TIGR01797. CM_P_1. 1 hit.
PROSITEi PS51671. ACT. 1 hit.
PS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12."
    Hudson G.S., Davidson B.E.
    J. Mol. Biol. 180:1023-1051(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "pheAo mutants of Escherichia coli have a defective pheA attenuator."
    Gavini N., Davidson B.E.
    J. Biol. Chem. 265:21532-21535(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
  6. "Nucleotide sequence of the leader region of the phenylalanine operon of Escherichia coli."
    Zurawski G.R., Brown K., Killingly D., Yanofsky C.
    Proc. Natl. Acad. Sci. U.S.A. 75:4271-4275(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
  7. "Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties."
    Dopheide T.A., Crewther P., Davidson B.E.
    J. Biol. Chem. 247:4447-4452(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHORISMATE MUTASE AND PREPHENATE DEHYDRATASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  8. "Analysis of active site residues in Escherichia coli chorismate mutase by site-directed mutagenesis."
    Liu D.R., Cload S.T., Pastor R.M., Schultz P.G.
    J. Am. Chem. Soc. 118:1789-1790(1996)
    Cited for: MUTAGENESIS OF ARG-11; ARG-28; LYS-39; GLU-52 AND GLN-88, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins."
    Zhang S., Pohnert G., Kongsaeree P., Wilson D.B., Clardy J., Ganem B.
    J. Biol. Chem. 273:6248-6253(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  10. "Atomic structure of the buried catalytic pocket of Escherichial coli chorismate mutase."
    Lee A.Y., Karplus P.A., Ganem B., Clardy J.
    J. Am. Chem. Soc. 117:3627-3628(1995)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-109 IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

Entry informationi

Entry nameiPHEA_ECOLI
AccessioniPrimary (citable) accession number: P0A9J8
Secondary accession number(s): P07022, P78204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi