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Database: UniProt
Entry: O67085
LinkDB: O67085
Original site: O67085 
ID   PHEA_AQUAE              Reviewed;         362 AA.
AC   O67085;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-SEP-2014, entry version 100.
DE   RecName: Full=P-protein;
DE   Includes:
DE     RecName: Full=Chorismate mutase;
DE              Short=CM;
DE              EC=5.4.99.5;
DE   Includes:
DE     RecName: Full=Prephenate dehydratase;
DE              Short=PDT;
DE              EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=aq_951;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- CATALYTIC ACTIVITY: Chorismate = prephenate.
CC   -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate
CC       biosynthesis; prephenate from chorismate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Contains 1 ACT domain.
CC   -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
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DR   EMBL; AE000657; AAC07041.1; -; Genomic_DNA.
DR   PIR; B70382; B70382.
DR   RefSeq; NP_213648.1; NC_000918.1.
DR   RefSeq; WP_010880586.1; NC_000918.1.
DR   ProteinModelPortal; O67085; -.
DR   STRING; 224324.aq_951; -.
DR   EnsemblBacteria; AAC07041; AAC07041; aq_951.
DR   GeneID; 1193627; -.
DR   KEGG; aae:aq_951; -.
DR   PATRIC; 20959248; VBIAquAeo85532_0746.
DR   eggNOG; COG0077; -.
DR   HOGENOM; HOG000018971; -.
DR   KO; K14170; -.
DR   OMA; IDVQANL; -.
DR   OrthoDB; EOG6WHNT1; -.
DR   BioCyc; AAEO224324:GJBH-681-MONOMER; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR002701; Chorismate_mutase.
DR   InterPro; IPR020822; Chorismate_mutase_type_II.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Isomerase; Lyase;
KW   Multifunctional enzyme; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    362       P-protein.
FT                                /FTId=PRO_0000119181.
FT   DOMAIN        1     92       Chorismate mutase.
FT   DOMAIN       93    267       Prephenate dehydratase.
FT   DOMAIN      279    356       ACT.
FT   REGION      268    362       Regulatory (Phe-binding).
FT   SITE        260    260       Essential for prephenate dehydratase
FT                                activity (Potential).
SQ   SEQUENCE   362 AA;  41187 MW;  97FBA945E126436E CRC64;
     MEELKELRKE IDRIDEEILR LLNERAKLAK RIGEIKSKAN LPIHVPERER EIFEKILRLN
     KEVYGGVFPQ EALVHIYREI ISACLSLEKK IKVAYLGPKA TFTHQAALEF FGFSAHYTPC
     STIRDVFVEV ETKRADYGVV PVENTIEGVV NYTLDMFLES DVKIAGEIVI PITLHLLSAS
     DSIENVEKVY SHKMALAQCR SWLEKNLPSV QVIEVESTAK ACEIALEDER AGAVASEVAA
     YTYHLNILAR NIQDSGDNFT RFLVIAKRDL KPTGSDKTSI LFGVKDEPGA LYKALEVFYK
     HGINLTKIES RPSKKKAWDY VFFVDLEGHK EEERVEKALK ELKEKTQFLK VLGSYPKALL
     QE
//
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