P43900 (PHEA_HAEIN) 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:	HI_1145

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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.
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	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_0000119188
Regions
	Domain	1 – 92	92	Chorismate mutase
	Domain	105 – 285	181	Prephenate dehydratase
	Domain	298 – 364	67	ACT
	Region	286 – 385	100	Regulatory (Phe-binding)
Sites
	Site	278	1	Essential for prephenate dehydratase activity Potential

Sequences

	Sequence		Length	Mass (Da)
	P43900 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 2289BC7FF73C44EC	FASTA	385	44,001
	10 20 30 40 50 60 MALELSDIRQ QITQIDRSLL KLLSERHRLA FDVVRSKEIS QKSLRDVERE QQLLQELVQF 70 80 90 100 110 120 AENENYQLEA QYITSIFQKI IEDSVLTQQV YLQNKLNEQR NQNLHIAFLG KRGSYSNLAA 130 140 150 160 170 180 RNYAARYQKQ FVELGCQSFE QVFEKVQTGE ADFGVLPLEN TTSGAINEVY DLLQHTDLSL 190 200 210 220 230 240 VGELAYPIKH CVLVNDKTDL NQIDTLYSHP QVIQQCSQFI HSLDRVHIEY CESSSHAMQL 250 260 270 280 290 300 VASLNKPNIA ALGNEDGGKL YGLSVLKTNI ANQENNITRF IVVAKEPREV SSQIPTKTLL 310 320 330 340 350 360 LMTTSQQAGA LVDALLVFKK HQINMTKLES RPIYGKPWEE MFYLEIEANI HHPDTKQALE 370 380 ELKNYSNYLK ILGCYPSEIV KPVSV

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22800.1.
PIR	B64186.
RefSeq	NP_439303.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43900.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	950108.
GenomeReviews	Gene locus HI_1145 in contig L42023_GR.
KEGG	hin:HI1145.
PATRIC	20190965. VBIHaeInf48452_1195.
TIGR	HI_1145.
Phylogenomic databases
HOGENOM	HBG693866.
OMA	YCESSSH.
PhylomeDB	P43900.
ProtClustDB	CLSK869985.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1145-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]
Gene3D	G3DSA:1.20.59.10. Chorismate_mutase. 1 hit.
KO	K14170.
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]
SUPFAM	SSF48600. Chorismate_mut. 1 hit.
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_HAEIN

Accession

Primary (citable) accession number: P43900

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program