Reviewed, UniProtKB/Swiss-Prot Q8K9F8 (PHEA_BUCAP)

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:	BUsg_379

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	385 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 – 385	385	P-protein		PRO_0000119183
Regions
	Domain	1 – 92	92	Chorismate mutase
	Domain	105 – 285	181	Prephenate dehydratase
	Region	286 – 385	100	Regulatory
Sites
	Site	278	1	Essential for prephenate dehydratase activity Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8K9F8-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E8ED3D4C4B05F48F	FASTA	385	43,888
	10 20 30 40 50 60 MPSKNDLLSF RSEINNIDKN IVQLLAKRKK LVLNIAESKI KNNQPIRDIE REKILLEKLT 70 80 90 100 110 120 NLGKKNNLNT NYITRLFQLI IEESVLTQKK LLNKFCNDNN LDLASFSFLG PKGSYSHIAA 130 140 150 160 170 180 SQYAEQNFKT CIENACLSFN EVIQSVENNQ TDYAVLPIEN SCSGFINEIF DILKKTNLFI 190 200 210 220 230 240 IGEINISINH CLLAIKKIEL NKIKAVYSHP QPFQQCSYFI KKFPNWKIQY TNSTADAMKK 250 260 270 280 290 300 IVKYNITTNA ALGSELGSKI YGLKVLYKNL ANKKKNITRF ILLSRKPVSI SSKIPTKTTL 310 320 330 340 350 360 IFNTGQESGA LAEVLLILKK NKLIMKKLTS QNIYKNPWEE MFYIDVQANL SSSLMQETLE 370 380 KIGKITKFIK ILGCYPSENI TPIIP

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67931.1.
RefSeq	NP_660720.1.
3D structure databases
SMR	Q8K9F8. Positions 5-94, 106-379.
ModBase	Search...
Genome annotation databases
GeneID	1005778.
GenomeReviews	Gene locus BUsg_379 in contig AE013218_GR.
KEGG	bas:BUsg379.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG693866.
OMA	LESRPIY.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG379-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. 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]
TIGRFAMs	TIGR01797. CM_P_1. 1 hit.
PROSITE	PS51168. CHORISMATE_MUT_2. 1 hit. PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. False negative. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHEA_BUCAP

Accession

Primary (citable) accession number: Q8K9F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 1, 2002
Last modified:	February 9, 2010
This is version 58 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)