CMPDT_AQUAE
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
