Reviewed, UniProtKB/Swiss-Prot P27603 (PHEA_PSEST)

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

Pseudomonas stutzeri (Pseudomonas perfectomarina)

Taxonomic identifier

316 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 ACT domain. 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	amino acid binding Inferred from electronic annotation. Source: InterPro 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 – 365	365	P-protein		PRO_0000119190
Regions
	Domain	1 – 96	96	Chorismate mutase
	Domain	97 – 272	176	Prephenate dehydratase
	Domain	283 – 359	77	ACT
	Region	273 – 365	93	Regulatory (Phe-binding)
Sites
	Site	265	1	Essential for prephenate dehydratase activity Potential

Sequences

	Sequence		Length	Mass (Da)
	P27603-1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 88E2457FDB132FD4	FASTA	365	40,744
	10 20 30 40 50 60 MSEADQLKAL RVRIDSLDER ILDLISERAR CAQEVARVKT ASWPKAEEAV FYRPEREAWV 70 80 90 100 110 120 LKHIMELNKG PLDNEEMARL FREIMSSCLA LEQPLRVAYL GPEGTFSQAA ALKHFGHSVI 130 140 150 160 170 180 SKPMAAIDEV FREVVAGAVN FGVVPVENST EGAVNHTLDS FLEHDIVICG EVELRIHHHL 190 200 210 220 230 240 LVGETTKTDR ITRIYSHAQS LAQCRKWLDA HYPNVERVAV SSNADAAKRV KSEWNSAAIA 250 260 270 280 290 300 GDMAAQLYGL SKLAEKIEDR PVNSTRFLII GSQEVPPTGD DKTSIIVSMR NKPGALHELL 310 320 330 340 350 360 MPFHSNGIDL TRIETRPSRS GKWTYVFFID CMGHHQDPLI KNVLEKIGHE AVALKVLGSY PKAVL

References

[1]	"Cloning, sequencing, and expression of the P-protein gene (pheA) of Pseudomonas stutzeri in Escherichia coli: implications for evolutionary relationships in phenylalanine biosynthesis." Fischer R.S., Zhao G., Jensen R.A. J. Gen. Microbiol. 137:1293-1301(1991) [PubMed: 1919506] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JM300 / DSM 10701.
[2]	"A probable mixed-function supraoperon in Pseudomonas exhibits gene organization features of both intergenomic conservation and gene shuffling." Xie G., Bonner C.A., Jensen R.A. J. Mol. Evol. 49:108-121(1999) [PubMed: 10368439] [Abstract] Cited for: SEQUENCE REVISION. Strain: JM300 / DSM 10701.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF038578 Genomic DNA. Translation: AAD47360.1.
PIR	A44764.
3D structure databases
HSSP	HSSP built from PDB template 1PHZ based on UniProtKB P04176.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.51. 421. 5.4.99.5. 421.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR008242. Chor_mutase/pphenate_deHydtase. IPR002701. Chorismate_mut. IPR010957. CM_P2. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Pfam	PF01842. ACT. 1 hit. PF01817. CM_2. 1 hit. PF00800. PDT. 1 hit. [Graphical view]
PIRSF	PIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
TIGRFAMs	TIGR01807. CM_P2. 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_PSEST

Accession

Primary (citable) accession number: P27603
Secondary accession number(s): Q9RI01

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	June 6, 2002
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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