Reviewed, UniProtKB/Swiss-Prot Q02286 (PHEA_ENTAG)

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

Organism

Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)

Taxonomic identifier

549 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea

Protein attributes

Sequence length	387 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.
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	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 – 387	387	P-protein		PRO_0000119187
Regions
	Domain	1 – 92	92	Chorismate mutase
	Domain	105 – 285	181	Prephenate dehydratase
	Region	286 – 387	102	Regulatory (Phe-binding)
Sites
	Site	278	1	Essential for prephenate dehydratase activity Potential
Experimental info
	Sequence conflict	301	1	I → K in AAA24853. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q02286-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 8C4F29C5678E42C6	FASTA	387	43,183
	10 20 30 40 50 60 MNPDNPLLAL RDKISAVDKK LLTLLAERRL LAVEVAQAKL ATHRPIRDVE RERALLENLI 70 80 90 100 110 120 VLGKAHNLDA HYITRLFQLV IEDSVLTQQA LLQKNLNHPH AHAARIAFLG PKGSYSHLAA 130 140 150 160 170 180 RNYASRHFDS MVECGCLKFH DIIKQVENGV ADYAVMPIEN TSSGSINDVY DLLQQTSLSI 190 200 210 220 230 240 VGELTLPIDH CVLVNGPTDL QQIETVYSHP QPFQQCSQFI NRFPHWKIEY TESTAAAMEK 250 260 270 280 290 300 VAALNSPKVA ALGSEAGGEL YQLQVLERNL ANQQQNHTRF IVLARKAIEV SDQVPAKTTL 310 320 330 340 350 360 IMATGQQAGA LVDALLVLRQ HNLIMSKLES RPINGNPWEE MFYIDVQGNL QSERMQQALQ 370 380 ELQTMTRSLK VLGCYPSENV VPAEPGR

References

[1]	"A monofunctional prephenate dehydrogenase created by cleavage of the 5' 109 bp of the tyrA gene from Erwinia herbicola." Xia T., Zhao G., Fischer R.S., Jensen R.A. J. Gen. Microbiol. 138:1309-1316(1992) [PubMed: 1512561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Loss of allosteric control but retention of the bifunctional catalytic competence of a fusion protein formed by excision of 260 base pairs from the 3' terminus of pheA from Erwinia herbicola." Xia T., Zhao G., Jensen R.A. Appl. Environ. Microbiol. 58:2792-2798(1992) [PubMed: 1444388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-301.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60420 Genomic DNA. Translation: CAA42949.1. M74134 Genomic DNA. Translation: AAA24853.1.
PIR	S26053.
3D structure databases
SMR	Q02286. Positions 6-97, 104-379.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.51. 3054. 5.4.99.5. 3054.
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. 1 hit. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHEA_ENTAG

Accession

Primary (citable) accession number: Q02286

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	February 9, 2010
This is version 68 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)