ID   CMPDT_STUST             Reviewed;         365 AA.
AC   P27603; Q9RI01;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   04-NOV-2026, entry version 121.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000305};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000305};
DE   AltName: Full=P-protein {ECO:0000303|PubMed:1919506};
DE   Includes:
DE     RecName: Full=Chorismate mutase {ECO:0000303|PubMed:1919506};
DE              Short=CM {ECO:0000303|PubMed:1919506};
DE              EC=5.4.99.5 {ECO:0000269|PubMed:1919506};
DE   Includes:
DE     RecName: Full=Prephenate dehydratase {ECO:0000303|PubMed:1919506};
DE              Short=PDT {ECO:0000303|PubMed:1919506};
DE              EC=4.2.1.51 {ECO:0000269|PubMed:1919506};
GN   Name=pheA {ECO:0000303|PubMed:1919506};
OS   Stutzerimonas stutzeri (Pseudomonas stutzeri).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 10701 / IAM 15110 / JCM 21571 / JM300;
RX   PubMed=1919506; DOI=10.1099/00221287-137-6-1293;
RA   Fischer R.S., Zhao G., Jensen R.A.;
RT   "Cloning, sequencing, and expression of the P-protein gene (pheA) of
RT   Pseudomonas stutzeri in Escherichia coli: implications for evolutionary
RT   relationships in phenylalanine biosynthesis.";
RL   J. Gen. Microbiol. 137:1293-1301(1991).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=DSM 10701 / IAM 15110 / JCM 21571 / JM300;
RX   PubMed=10368439; DOI=10.1007/pl00006523;
RA   Xie G., Bonner C.A., Jensen R.A.;
RT   "A probable mixed-function supraoperon in Pseudomonas exhibits gene
RT   organization features of both intergenomic conservation and gene
RT   shuffling.";
RL   J. Mol. Evol. 49:108-121(1999).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000269|PubMed:1919506}.
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:0000269|PubMed:1919506};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prephenate + H(+) = 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:0000269|PubMed:1919506};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1. {ECO:0000305}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
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DR   EMBL; AF038578; AAD47360.1; -; Genomic_DNA.
DR   PIR; A44764; A44764.
DR   AlphaFoldDB; P27603; -.
DR   SMR; P27603; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   OMA; AACMHGI; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004106; F:chorismate mutase activity; EXP:UniProtKB.
DR   GO; GO:0004664; F:prephenate dehydratase activity; EXP:UniProtKB.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13630; PBP2_PDT_1; 1.
DR   FunFam; 3.40.190.10:FF:000029; Chorismate mutase/Prephenate dehydratase; 1.
DR   FunFam; 3.40.190.10:FF:000034; Chorismate mutase/prephenate dehydratase; 1.
DR   FunFam; 1.20.59.10:FF:000004; Prephenate dehydratase; 1.
DR   FunFam; 3.30.70.260:FF:000012; Prephenate dehydratase; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   NCBIfam; TIGR01807; CM_P2; 1.
DR   NCBIfam; NF008865; pheA; 1.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF48600; Chorismate mutase II; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis.
FT   CHAIN           1..365
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119190"
FT   DOMAIN          1..96
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          97..272
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          284..361
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         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT   SITE            265
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   365 AA;  40744 MW;  88E2457FDB132FD4 CRC64;
     MSEADQLKAL RVRIDSLDER ILDLISERAR CAQEVARVKT ASWPKAEEAV FYRPEREAWV
     LKHIMELNKG PLDNEEMARL FREIMSSCLA LEQPLRVAYL GPEGTFSQAA ALKHFGHSVI
     SKPMAAIDEV FREVVAGAVN FGVVPVENST EGAVNHTLDS FLEHDIVICG EVELRIHHHL
     LVGETTKTDR ITRIYSHAQS LAQCRKWLDA HYPNVERVAV SSNADAAKRV KSEWNSAAIA
     GDMAAQLYGL SKLAEKIEDR PVNSTRFLII GSQEVPPTGD DKTSIIVSMR NKPGALHELL
     MPFHSNGIDL TRIETRPSRS GKWTYVFFID CMGHHQDPLI KNVLEKIGHE AVALKVLGSY
     PKAVL
//