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Database: UniProt
Entry: P0A9J9
LinkDB: P0A9J9
Original site: P0A9J9 
ID   CMPDT_ECO57             Reviewed;         386 AA.
AC   P0A9J9; P07022; P78204;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Z3891, ECs3462;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG57710.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36885.1; -; Genomic_DNA.
DR   PIR; F91061; F91061.
DR   RefSeq; NP_311489.1; NC_002695.1.
DR   RefSeq; WP_000200120.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A9J9; -.
DR   SMR; P0A9J9; -.
DR   STRING; 155864.EDL933_3760; -.
DR   EnsemblBacteria; AAG57710; AAG57710; Z3891.
DR   EnsemblBacteria; BAB36885; BAB36885; ECs_3462.
DR   GeneID; 58463063; -.
DR   GeneID; 914858; -.
DR   KEGG; ece:Z3891; -.
DR   KEGG; ecs:ECs_3462; -.
DR   PATRIC; fig|386585.9.peg.3616; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_035008_1_0_6; -.
DR   OMA; PLMIYRE; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; IPR010952; CM_P_1.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
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   TIGRFAMs; TIGR01797; CM_P_1; 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..386
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119186"
FT   DOMAIN          1..92
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          105..285
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          299..376
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   SITE            278
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  43111 MW;  4B0960854C75A4F1 CRC64;
     MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID RERDLLERLI
     TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN PHSARIAFLG PKGSYSHLAA
     RQYAARHFEQ FIESGCAKFA DIFNQVETGQ ADYAVVPIEN TSSGAINDVY DLLQHTSLSI
     VGEMTLTIDH CLLVSGTTDL STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK
     VAQAKSPHVA ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL
     LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL ESAEMQKALK
     ELGEITRSMK VLGCYPSENV VPVDPT
//
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