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Database: UniProt
Entry: O67085
LinkDB: O67085
Original site: O67085 
ID   CMPDT_AQUAE             Reviewed;         362 AA.
AC   O67085;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE   AltName: Full=P-protein {ECO:0000250|UniProtKB:P0A9J8};
DE   Includes:
DE     RecName: Full=Chorismate mutase {ECO:0000250|UniProtKB:P0A9J8};
DE              Short=CM {ECO:0000250|UniProtKB:P0A9J8};
DE              EC=5.4.99.5 {ECO:0000250|UniProtKB:P0A9J8};
DE   Includes:
DE     RecName: Full=Prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE              Short=PDT {ECO:0000250|UniProtKB:P0A9J8};
DE              EC=4.2.1.51 {ECO:0000250|UniProtKB:P0A9J8};
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 aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC         Evidence={ECO:0000250|UniProtKB:P0A9J8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC         Evidence={ECO:0000250|UniProtKB:P0A9J8};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P0A9J8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
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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   AlphaFoldDB; O67085; -.
DR   SMR; O67085; -.
DR   STRING; 224324.aq_951; -.
DR   EnsemblBacteria; AAC07041; AAC07041; aq_951.
DR   KEGG; aae:aq_951; -.
DR   PATRIC; fig|224324.8.peg.746; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_035008_0_1_0; -.
DR   InParanoid; O67085; -.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
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   SUPFAM; SSF55021; SSF55021; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..362
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119181"
FT   DOMAIN          1..92
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          93..267
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          279..356
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   SITE            260
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000255"
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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