P-protein - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A9J8 (PHEA_ECOLI)

Last modified June 16, 2009. Version 41. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    P-protein
Including the following 2 domains:
    1- Recommended name:
            Chorismate mutase
                Short name=CM
              EC=5.4.99.5
    2- Recommended name:
            Prephenate dehydratase
                Short name=PDT
              EC=4.2.1.51

Gene names

Name:	pheA
Ordered Locus Names:	b2599, JW2580

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Chorismate = prephenate. Prephenate = phenylpyruvate + H₂O + CO₂.
Pathway	Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular location	Cytoplasm.
Sequence similarities	Contains 1 chorismate mutase domain. Contains 1 prephenate dehydratase domain.

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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
Gene Ontology (GO)
Biological process	L-phenylalanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chorismate mutase activity Inferred from electronic annotation. Source: EC prephenate dehydratase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
eutD	P77218	1	EBI-556114,EBI-1128886

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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

Chorismate mutase

Domain

105 – 285

181

Prephenate dehydratase

Region

286 – 386

101

Regulatory (Phe-binding)

Sites

Site

278

Essential for prephenate dehydratase activity Potential

Secondary structure

386

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A9J8-1 [UniParc].

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

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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: 6396419] [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. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [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: 9278503] [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: 16738553] [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: 2254312] [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: 360214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[7]	"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.
[8]	"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: 9497350] [Abstract] Cited for: DOMAINS.

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Cross-references

Sequence databases

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

AP_003180.1.
NP_417090.1.

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9J8. 17 interactions.

Genome annotation databases

GeneID

947081.

GenomeReviews

Gene locus JW2580 in contig AP009048_GR.
Gene locus b2599 in contig U00096_GR.

KEGG

ecj:JW2580.
eco:b2599.

Organism-specific databases

EchoBASE

EB0701.

EcoGene

EG10707. pheA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9J8.

OMA

P0A9J8. TLYSHPQ.

Enzyme and pathway databases

BioCyc

EcoCyc:CHORISMUTPREPHENDEHYDRAT-MON.
MetaCyc:CHORISMUTPREPHENDEHYDRAT-MON.

Family and domain databases

InterPro

IPR008242. Chor_mutase/pphenate_deHydtase.
IPR002701. Chorismate_mut.
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.

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...

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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:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents