CMPDT_ECOLI
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 03-AUG-2022, entry version 134.
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}; OrderedLocusNames=b2599, JW2580;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=1.0 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; P0A9J8; -.
DR PRIDE; P0A9J8; -.
DR EnsemblBacteria; AAC75648; AAC75648; b2599.
DR EnsemblBacteria; BAA16484; BAA16484; BAA16484.
DR GeneID; 58463063; -.
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 PhylomeDB; P0A9J8; -.
DR BioCyc; EcoCyc:CHORISMUTPREPHENDEHYDRAT-MON; -.
DR BioCyc; MetaCyc:CHORISMUTPREPHENDEHYDRAT-MON; -.
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: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 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 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
