ID   CMPDT_ECOLI             Reviewed;         386 AA.
AC   P0A9J8; P07022; P78204;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000305};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000303|PubMed:4261395};
DE   AltName: Full=P-protein {ECO:0000303|Ref.10};
DE   Includes:
DE     RecName: Full=Chorismate mutase {ECO:0000303|PubMed:4261395};
DE              Short=CM {ECO:0000305};
DE              EC=5.4.99.5 {ECO:0000269|PubMed:4261395};
DE   Includes:
DE     RecName: Full=Prephenate dehydratase {ECO:0000303|PubMed:4261395};
DE              Short=PDT {ECO:0000305};
DE              EC=4.2.1.51 {ECO:0000269|PubMed:4261395};
GN   Name=pheA {ECO:0000303|PubMed:360214};
GN   OrderedLocusNames=b2599, JW2580;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=6396419; DOI=10.1016/0022-2836(84)90269-9;
RA   Hudson G.S., Davidson B.E.;
RT   "Nucleotide sequence and transcription of the phenylalanine and tyrosine
RT   operons of Escherichia coli K12.";
RL   J. Mol. Biol. 180:1023-1051(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX   PubMed=2254312; DOI=10.1016/s0021-9258(18)45772-9;
RA   Gavini N., Davidson B.E.;
RT   "pheAo mutants of Escherichia coli have a defective pheA attenuator.";
RL   J. Biol. Chem. 265:21532-21535(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX   PubMed=360214; DOI=10.1073/pnas.75.9.4271;
RA   Zurawski G.R., Brown K., Killingly D., Yanofsky C.;
RT   "Nucleotide sequence of the leader region of the phenylalanine operon of
RT   Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:4271-4275(1978).
RN   [7]
RP   FUNCTION AS A CHORISMATE MUTASE AND PREPHENATE DEHYDRATASE, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=4261395; DOI=10.1016/s0021-9258(19)45005-9;
RA   Dopheide T.A., Crewther P., Davidson B.E.;
RT   "Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II.
RT   Kinetic properties.";
RL   J. Biol. Chem. 247:4447-4452(1972).
RN   [8]
RP   MUTAGENESIS OF ARG-11; ARG-28; LYS-39; GLU-52 AND GLN-88, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   DOI=10.1021/ja953151o;
RA   Liu D.R., Cload S.T., Pastor R.M., Schultz P.G.;
RT   "Analysis of active site residues in Escherichia coli chorismate mutase by
RT   site-directed mutagenesis.";
RL   J. Am. Chem. Soc. 118:1789-1790(1996).
RN   [9]
RP   DOMAIN.
RX   PubMed=9497350; DOI=10.1074/jbc.273.11.6248;
RA   Zhang S., Pohnert G., Kongsaeree P., Wilson D.B., Clardy J., Ganem B.;
RT   "Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of
RT   catalytic and regulatory domains using genetically engineered proteins.";
RL   J. Biol. Chem. 273:6248-6253(1998).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-109 IN COMPLEX WITH SUBSTRATE
RP   ANALOGS, AND SUBUNIT.
RX   DOI=10.1021/ja00117a038;
RA   Lee A.Y., Karplus P.A., Ganem B., Clardy J.;
RT   "Atomic structure of the buried catalytic pocket of Escherichia coli
RT   chorismate mutase.";
RL   J. Am. Chem. Soc. 117:3627-3628(1995).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000269|PubMed:4261395}.
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:4261395};
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:0000269|PubMed:4261395};
CC   -!- ACTIVITY REGULATION: Both activities are inhibited by L-phenylalanine.
CC       {ECO:0000269|PubMed:4261395}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45 uM for chorismate (at pH 7.8 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:4261395};
CC         KM=1 mM for prephenate (at pH 7.8 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:4261395};
CC         KM=147 uM for chorismate (at pH 4.9) {ECO:0000269|Ref.8};
CC         KM=296 uM for chorismate (at pH 7.5) {ECO:0000269|Ref.8};
CC         Note=kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.
CC         {ECO:0000269|Ref.8};
CC       pH dependence:
CC         Optimum pH is 7.3 for chorismate mutase activity.
CC         {ECO:0000269|PubMed:4261395};
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   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.10}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; M10431; AAA24330.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75648.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16484.1; -; Genomic_DNA.
DR   EMBL; M58024; AAA62784.1; -; Genomic_DNA.
DR   EMBL; V00314; CAA23601.1; -; Genomic_DNA.
DR   PIR; A30261; KMECPW.
DR   RefSeq; NP_417090.1; NC_000913.3.
DR   RefSeq; WP_000200120.1; NZ_SSUR01000056.1.
DR   PDB; 1ECM; X-ray; 2.20 A; A/B=1-109.
DR   PDB; 5VHT; X-ray; 2.00 A; A/B=1-92.
DR   PDBsum; 1ECM; -.
DR   PDBsum; 5VHT; -.
DR   AlphaFoldDB; P0A9J8; -.
DR   SMR; P0A9J8; -.
DR   BioGRID; 4263461; 19.
DR   DIP; DIP-36017N; -.
DR   IntAct; P0A9J8; 17.
DR   STRING; 511145.b2599; -.
DR   BindingDB; P0A9J8; -.
DR   ChEMBL; CHEMBL3341586; -.
DR   DrugBank; DB08648; 8-Hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid.
DR   jPOST; P0A9J8; -.
DR   PaxDb; 511145-b2599; -.
DR   EnsemblBacteria; AAC75648; AAC75648; b2599.
DR   GeneID; 947081; -.
DR   KEGG; ecj:JW2580; -.
DR   KEGG; eco:b2599; -.
DR   PATRIC; fig|1411691.4.peg.4140; -.
DR   EchoBASE; EB0701; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_035008_1_0_6; -.
DR   InParanoid; P0A9J8; -.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 9802281at2; -.
DR   PhylomeDB; P0A9J8; -.
DR   BioCyc; EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER; -.
DR   BioCyc; MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER; -.
DR   BRENDA; 5.4.99.5; 2026.
DR   SABIO-RK; P0A9J8; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   EvolutionaryTrace; P0A9J8; -.
DR   PRO; PR:P0A9J8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004106; F:chorismate mutase activity; IDA:EcoCyc.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IMP:EcoCyc.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13631; PBP2_Ct-PDT_like; 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; IPR010952; CM_P_1.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   NCBIfam; TIGR01797; CM_P_1; 1.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 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   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Cytoplasm; Isomerase; Lyase; Multifunctional enzyme;
KW   Phenylalanine biosynthesis; Reference proteome.
FT   CHAIN           1..386
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119185"
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   REGION          286..386
FT                   /note="Regulatory (Phe-binding)"
FT                   /evidence="ECO:0000305|PubMed:9497350"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|Ref.10"
FT   SITE            278
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         11
FT                   /note="R->A,K: Important decrease in catalytic efficiency
FT                   and affinity."
FT                   /evidence="ECO:0000269|Ref.8"
FT   MUTAGEN         28
FT                   /note="R->A,K: Important decrease in catalytic efficiency
FT                   and affinity."
FT                   /evidence="ECO:0000269|Ref.8"
FT   MUTAGEN         39
FT                   /note="K->A,Q,R: Important decrease in catalytic efficiency
FT                   and affinity."
FT                   /evidence="ECO:0000269|Ref.8"
FT   MUTAGEN         52
FT                   /note="E->A,D,Q: Important decrease in catalytic efficiency
FT                   and affinity."
FT                   /evidence="ECO:0000269|Ref.8"
FT   MUTAGEN         88
FT                   /note="Q->A,E,K: Important decrease in catalytic efficiency
FT                   and affinity."
FT                   /evidence="ECO:0000269|Ref.8"
FT   HELIX           6..42
FT                   /evidence="ECO:0007829|PDB:5VHT"
FT   HELIX           49..65
FT                   /evidence="ECO:0007829|PDB:5VHT"
FT   HELIX           70..92
FT                   /evidence="ECO:0007829|PDB:5VHT"
FT   HELIX           96..99
FT                   /evidence="ECO:0007829|PDB:1ECM"
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
//