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P0A9J8 (PHEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-protein

Including the following 2 domains:

  1. Chorismate mutase
    Short name=CM
    EC=5.4.99.5
  2. Prephenate dehydratase
    Short name=PDT
    EC=4.2.1.51
Gene names
Name:pheA
Ordered Locus Names:b2599, JW2580
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. Ref.7

Catalytic activity

Chorismate = prephenate.

Prephenate = phenylpyruvate + H2O + CO2.

Enzyme regulation

Inhibited by L-phenylalanine. Ref.7

Pathway

Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.

Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.

Subunit structure

Homodimer. Ref.10

Subcellular location

Cytoplasm.

Sequence similarities

Contains 1 ACT domain.

Contains 1 chorismate mutase domain.

Contains 1 prephenate dehydratase domain.

Biophysicochemical properties

Kinetic parameters:

KM=45 µM for chorismate (at pH 7.8 and at 37 degrees Celsius, Ref.7) Ref.7 Ref.8

KM=100 µM for prephenate (at pH 7.8 and at 37 degrees Celsius, Ref.7)

KM=147 µM for chorismate (at pH 4.9)

KM=296 µM for chorismate (at pH 7.5)

Temperature dependence:

Optimum temperature is 7.3 degrees Celsius for chorismate mutase.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386P-protein
PRO_0000119185

Regions

Domain1 – 9292Chorismate mutase
Domain105 – 285181Prephenate dehydratase
Domain299 – 37678ACT
Region286 – 386101Regulatory (Phe-binding)

Sites

Binding site111Substrate
Binding site281Substrate
Binding site391Substrate
Binding site481Substrate
Binding site521Substrate
Binding site841Substrate
Binding site881Substrate
Site2781Essential for prephenate dehydratase activity Potential

Experimental info

Mutagenesis111R → A: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis111R → K: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis281R → A: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis281R → K: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis391K → A: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis391K → Q: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis391K → R: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis521E → A: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis521E → D: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis521E → Q: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis881Q → A: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis881Q → E: Important decrease in catalytic efficiency and affinity. Ref.8
Mutagenesis881Q → K: Important decrease in catalytic efficiency and affinity. Ref.8

Secondary structure

....... 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9J8 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 4B0960854C75A4F1

FASTA38643,111
        10         20         30         40         50         60 
MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID RERDLLERLI 

        70         80         90        100        110        120 
TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN PHSARIAFLG PKGSYSHLAA 

       130        140        150        160        170        180 
RQYAARHFEQ FIESGCAKFA DIFNQVETGQ ADYAVVPIEN TSSGAINDVY DLLQHTSLSI 

       190        200        210        220        230        240 
VGEMTLTIDH CLLVSGTTDL STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK 

       250        260        270        280        290        300 
VAQAKSPHVA ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL 

       310        320        330        340        350        360 
LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL ESAEMQKALK 

       370        380 
ELGEITRSMK VLGCYPSENV VPVDPT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKMECPW. A30261.
RefSeqNP_417090.1. NC_000913.3.
YP_490822.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECMX-ray2.20A/B1-109[»]
ProteinModelPortalP0A9J8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36017N.
IntActP0A9J8. 17 interactions.
MINTMINT-1248118.
STRING511145.b2599.

Proteomic databases

PaxDbP0A9J8.
PRIDEP0A9J8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75648; AAC75648; b2599.
BAA16484; BAA16484; BAA16484.
GeneID12934467.
947081.
KEGGecj:Y75_p2547.
eco:b2599.
PATRIC32120597. VBIEscCol129921_2697.

Organism-specific databases

EchoBASEEB0701.
EcoGeneEG10707. pheA.

Phylogenomic databases

eggNOGCOG0077.
HOGENOMHOG000018972.
KOK14170.
OMAIDVQANL.
OrthoDBEOG6WHNT1.
PhylomeDBP0A9J8.

Enzyme and pathway databases

BioCycEcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
ECOL316407:JW2580-MONOMER.
MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
SABIO-RKP0A9J8.
UniPathwayUPA00120; UER00203.
UPA00121; UER00345.

Gene expression databases

GenevestigatorP0A9J8.

Family and domain databases

Gene3D1.20.59.10. 1 hit.
InterProIPR002912. 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]
PfamPF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMSSF48600. SSF48600. 1 hit.
TIGRFAMsTIGR01797. CM_P_1. 1 hit.
PROSITEPS51671. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP0A9J8.
PROP0A9J8.

Entry information

Entry namePHEA_ECOLI
AccessionPrimary (citable) accession number: P0A9J8
Secondary accession number(s): P07022, P78204
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene