P0A9J8 (PHEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase Lyase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine biosynthetic process Inferred from mutant phenotype PubMed 7030214. Source: EcoCyc chorismate metabolic process Inferred from electronic annotation. Source: InterPro tyrosine biosynthetic process Inferred from mutant phenotype PubMed 7030214. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chorismate mutase activity Inferred from direct assay Ref.9. Source: EcoCyc prephenate dehydratase activity Inferred from direct assay Ref.9. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

P-protein

PRO_0000119185

Regions

Domain

1 – 92

92

Chorismate mutase

Domain

105 – 285

181

Prephenate dehydratase

Region

286 – 386

101

Regulatory (Phe-binding)

Sites

Binding site

11

1

Substrate

Binding site

28

1

Substrate

Binding site

39

1

Substrate

Binding site

48

1

Substrate

Binding site

52

1

Substrate

Binding site

84

1

Substrate

Binding site

88

1

Substrate

Site

278

1

Essential for prephenate dehydratase activity Potential

Experimental info

Mutagenesis

11

1

R → A: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

11

1

R → K: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

28

1

R → A: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

28

1

R → K: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

39

1

K → A: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

39

1

K → Q: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

39

1

K → R: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

52

1

E → A: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

52

1

E → D: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

52

1

E → Q: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

88

1

Q → A: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

88

1

Q → E: Important decrease in catalytic efficiency and affinity. Ref.8

Mutagenesis

88

1

Q → K: Important decrease in catalytic efficiency and affinity. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

386

Helix Strand Turn

Details...

Helix

6 – 41

36

Helix

49 – 65

17

Helix

70 – 93

24

Sequences

	Sequence		Length	Mass (Da)
	P0A9J8 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 4B0960854C75A4F1	FASTA	386	43,111
	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

References

	« Hide 'large scale' referencesShow '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. , 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 277:1453-1474(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.

PIR

KMECPW. A30261.

RefSeq

NP_417090.1. NC_000913.2.
YP_490822.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ECM	X-ray	2.20	A/B	1-109	[»]

ProteinModelPortal

P0A9J8.

SMR

P0A9J8. Positions 6-100, 106-375.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36017N.

IntAct

P0A9J8. 17 interactions.

MINT

MINT-1248118.

STRING

511145.b2599.

Proteomic databases

PaxDb

P0A9J8.

PRIDE

P0A9J8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75648; AAC75648; b2599.
BAA16484; BAA16484; BAA16484.

GeneID

12934467.
947081.

KEGG

ecj:Y75_p2547.
eco:b2599.

PATRIC

32120597. VBIEscCol129921_2697.

Organism-specific databases

EchoBASE

EB0701.

EcoGene

EG10707. pheA.

Phylogenomic databases

eggNOG

COG0077.

HOGENOM

HOG000018972.

KO

K14170.

OMA

WREVMSA.

ProtClustDB

PRK10622.

Enzyme and pathway databases

BioCyc

EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
ECOL316407:JW2580-MONOMER.
MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.

SABIO-RK

P0A9J8.

UniPathway

UPA00120; UER00203.
UPA00121; UER00345.

Gene expression databases

Genevestigator

P0A9J8.

Family and domain databases

Gene3D

1.20.59.10. 1 hit.

InterPro

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]

Pfam

PF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]

PIRSF

PIRSF001500. Chor_mut_pdt_Ppr. 1 hit.

SMART

SM00830. CM_2. 1 hit.
[Graphical view]

SUPFAM

SSF48600. Chorismate_mut. 1 hit.

TIGRFAMs

TIGR01797. CM_P_1. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9J8.

Entry information

Entry name

PHEA_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program