Reviewed, UniProtKB/Swiss-Prot Q89AE5 (PHEA_BUCBP)

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:	bbp_355

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Predicted.

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.
Domain	The regulatory domain shows changes in the ESRP sequence, which is involved in the allosteric binding of phenylalanine. These changes suggest the desensitization of the enzyme to inhibition by phenylalanine and would permit the overproduction of phenylalanine.
Sequence similarities	Contains 1 chorismate mutase domain. Contains 1 prephenate dehydratase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase Lyase
Technical term	Allosteric enzyme 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 371	371	P-protein		PRO_0000119184
Regions
	Domain	1 – 92	92	Chorismate mutase
	Domain	104 – 284	181	Prephenate dehydratase
	Region	285 – 371	87	Regulatory By similarity
Sites
	Site	277	1	Essential for prephenate dehydratase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AE5-1 [UniParc]. Last modified May 30, 2003. Version 1. Checksum: 78AEEB3DD55FCEB4	FASTA	371	43,136
	10 20 30 40 50 60 MTLKNALLAF RNAINILDKN LINLLAKRKQ LSLNIAHTKV KNNYPVRDIE REQMLLKNLT 70 80 90 100 110 120 ILGEKHFLNK KYIESLFSII LEDSVLTQKK WIKKYNLNKY KLEKISFLGS FGSYSHLAAQ 130 140 150 160 170 180 KYAKKHSKIL TDKIYKNFSD VITSVEQQQS TYAILPIENQ SSGLIIEVYK LLQKTPLFII 190 200 210 220 230 240 GNIYIHANHC LLAKKYTPIL KIQKIYSHIQ PFKQCSKFIS LFPNWKLSNT TSTSEAIQHV 250 260 270 280 290 300 AKENDNTIAA LGNESYGELN KLEVIAKNIS NKRNNITQFI ILAQKKTYIT NKKTHLKTII 310 320 330 340 350 360 LISKKNENCE KIIRNILHKN KITLLKLKYY VTSKVLLEKI FFIEIENIYC IKHILKQFTI 370 EIKCIKILGC F

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO27074.1.
RefSeq	NP_777969.1.
3D structure databases
SMR	Q89AE5. Positions 5-94, 104-371.
ModBase	Search...
Genome annotation databases
GeneID	1058143.
GenomeReviews	Gene locus bbp_355 in contig AE016826_GR.
KEGG	bab:bbp355.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG693866.
OMA	AKENDNT.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_355-MONOMER.
Family and domain databases
InterPro	IPR008242. Chor_mutase/pphenate_deHydtase. IPR002701. Chorismate_mutase. IPR020822. Chorismate_mutase_type_II. IPR010952. CM_P_1. IPR001086. Preph_deHydtase. [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]
TIGRFAMs	TIGR01797. CM_P_1. 1 hit.
PROSITE	PS51168. CHORISMATE_MUT_2. 1 hit. PS00857. PREPHENATE_DEHYDR_1. False negative. PS00858. PREPHENATE_DEHYDR_2. False negative. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHEA_BUCBP

Accession

Primary (citable) accession number: Q89AE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2003
Last sequence update:	May 30, 2003
Last modified:	February 9, 2010
This is version 52 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)