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 01-MAY-2013, entry version 95.
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 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; WREVMSA; -.
DR ProtClustDB; CLSK2748389; -.
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:EC.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA: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; Chorismate_mut; 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 278 354 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
//
