Q9HZ67 (PHEA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
P-protein

Including the following 2 domains:

1. Chorismate mutase
   Short name=CM
   EC=5.4.99.5
2. Prephenate dehydratase
   Short name=PDT
   EC=4.2.1.51

Gene names

Name:	pheA
Ordered Locus Names:	PA3166

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
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	Complete proteome Multifunctional enzyme Reference proteome
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_0000287803
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) By similarity
Sites
	Site	265	1	Essential for prephenate dehydratase activity Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9HZ67 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 0C9DE686BB1E041D	FASTA	365	40,632
	10 20 30 40 50 60 MADQDQLKAL RLRIDSLDEK LLELISERAR CAQDVARVKT QTLGEGEAPV FYRPEREAWV 70 80 90 100 110 120 LKHIMQLNKG PLDNEEVARL FREIMSSCLA LEQPLKVAYL GPEGTFTQAA ALKHFGNAVI 130 140 150 160 170 180 STPMAAIDEV FREVAAGAVN FGVVPVENST EGAVNHTLDS FLEHDMVICG EVELRIHHHL 190 200 210 220 230 240 LVGETTKTDN ITRIYSHAQS LAQCRKWLDS HYPSVERVAV SSNADAAKRV KSEWNSAAIA 250 260 270 280 290 300 GDMAASLYDL SKLHEKIEDR PDNSTRFLII GNQEVPPTGD DKTSIIVSMR NKPGALHELL 310 320 330 340 350 360 VPFHNNGIDL TRIETRPSRS GKWTYVFFID FVGHHKEPLI KDVLEKIGQE AVALKVLGSY PKAVL

References

[1]

"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004091 Genomic DNA. Translation: AAG06554.1.
PIR	G83250.
RefSeq	NP_251856.1. NC_002516.2.
3D structure databases
HSSP	HSSP built from PDB template 1PHZ based on UniProtKB P04176.
ProteinModelPortal	Q9HZ67.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	882699.
GenomeReviews	Gene locus PA3166 in contig AE004091_GR.
KEGG	pae:PA3166.
PATRIC	19840897. VBIPseAer58763_3309.
Organism-specific databases
PseudoCAP	PA3166.
Phylogenomic databases
HOGENOM	HBG693866.
OMA	CRKWLDA.
ProtClustDB	CLSK867790.
Enzyme and pathway databases
BioCyc	PAER208964:PA3166-MONOMER.
Family and domain databases
InterPro	IPR002912. ACT-bd. IPR008242. Chor_mutase/pphenate_deHydtase. IPR002701. Chorismate_mutase. IPR020822. Chorismate_mutase_type_II. IPR010957. G/b/e-P-prot_chorismate_mutase. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Gene3D	G3DSA:1.20.59.10. Chorismate_mutase. 1 hit.
KO	K14170.
Pfam	PF01842. ACT. 1 hit. 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]
SUPFAM	SSF48600. Chorismate_mut. 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_PSEAE

Accession

Primary (citable) accession number: Q9HZ67

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program