Q9ZHY3 (PHEA_NEIG1) 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:	NGO1510

Organism

Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

Taxonomic identifier

242231 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	362 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 ACT domain. Contains 1 chorismate mutase domain. Contains 1 prephenate dehydratase domain.
Sequence caution	The sequence AAD05425.1 differs from that shown. Reason: Erroneous initiation. The sequence AAW90148.1 differs from that shown. Reason: Erroneous initiation.

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 – 362	362	P-protein		PRO_0000119189
Regions
	Domain	3 – 91	89	Chorismate mutase
	Domain	92 – 269	178	Prephenate dehydratase
	Domain	280 – 356	77	ACT
	Region	270 – 362	93	Regulatory (Phe-binding)
Sites
	Site	262	1	Essential for prephenate dehydratase activity Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9ZHY3 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: BEC6582338E84DE2	FASTA	362	39,354
	10 20 30 40 50 60 MSQTIDELLI PHRNAIDTID AEILRLLNER AQHAHAIGEL KGTGAVYRPE REVAVLRRIQ 70 80 90 100 110 120 DLNKGPLPDE SVARLFREVM SECLAVERPL TIAYLGPQGT FTQQAAIKHF GHAAHTMACP 130 140 150 160 170 180 TIDDCFKQVE TRQADYLVAP VENSTEGSVG RTLDLLAVTA LQACGEVVLR IHHNLLRKNN 190 200 210 220 230 240 GSTEGIAKVF SHAQALAQCN DWLGRRLPNA ERIAVSSNAE AARLVAESDD GTVAAIAGRT 250 260 270 280 290 300 AAEIYGLDMV AECIEDEPNN TTRFLVMGHH ETGASGSDKT SLAVSAPNRA GAVASLLQPL 310 320 330 340 350 360 TESGISMTKF ESRPSKSVLW EYLFFIDIEG HRRDAQIQTA LERLGERASF VKAIGSYPTA VL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential roles of homologous recombination pathways in Neisseria gonorrhoeae pilin antigenic variation, DNA transformation and DNA repair." Mehr I.J., Seifert H.S. Mol. Microbiol. 30:697-710(1998) [PubMed: 10094619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Neisseria gonorrhoeae." Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF047375 Genomic DNA. Translation: AAD05425.1. Different initiation. AE004969 Genomic DNA. Translation: AAW90148.1. Different initiation.
RefSeq	YP_208560.1. NC_002946.2.
3D structure databases
ProteinModelPortal	Q9ZHY3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9ZHY3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000002795; EBNEIP00000002636; EBNEIG00000002795.
GeneID	3281542.
GenomeReviews	Gene locus NGO1510 in contig AE004969_GR.
KEGG	ngo:NGO1510.
NMPDR	fig|242231.4.peg.1527.
PATRIC	20336494. VBINeiGon24812_1795.
Phylogenomic databases
eggNOG	COG0077.
GeneTree	EBGT00050000020499.
HOGENOM	HBG693866.
PhylomeDB	Q9ZHY3.
ProtClustDB	CLSK877559.
Enzyme and pathway databases
BioCyc	NGON242231:NGO1510-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_NEIG1

Accession

Primary (citable) accession number: Q9ZHY3
Secondary accession number(s): Q5F6N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program