CMPDT_BUCAP
ID CMPDT_BUCAP Reviewed; 385 AA.
AC Q8K9F8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=BUsg_379;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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}.
CC -!- DOMAIN: The regulatory domain shows changes in the ESRP sequence, which
CC is involved in the allosteric binding of phenylalanine. These changes
CC suggest the desensitization of the enzyme to inhibition by
CC phenylalanine and would permit the overproduction of phenylalanine.
CC {ECO:0000250|UniProtKB:P57472}.
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DR EMBL; AE013218; AAM67931.1; -; Genomic_DNA.
DR RefSeq; WP_011053898.1; NC_004061.1.
DR AlphaFoldDB; Q8K9F8; -.
DR SMR; Q8K9F8; -.
DR STRING; 198804.BUsg_379; -.
DR EnsemblBacteria; AAM67931; AAM67931; BUsg_379.
DR KEGG; bas:BUsg_379; -.
DR eggNOG; COG0077; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR HOGENOM; CLU_035008_1_0_6; -.
DR OMA; PLMIYRE; -.
DR OrthoDB; 1280729at2; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000000416; 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; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Cytoplasm; Isomerase; Lyase;
KW Multifunctional enzyme; Phenylalanine biosynthesis.
FT CHAIN 1..385
FT /note="Bifunctional chorismate mutase/prephenate
FT dehydratase"
FT /id="PRO_0000119183"
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..385
FT /note="Regulatory"
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 385 AA; 43888 MW; E8ED3D4C4B05F48F CRC64;
MPSKNDLLSF RSEINNIDKN IVQLLAKRKK LVLNIAESKI KNNQPIRDIE REKILLEKLT
NLGKKNNLNT NYITRLFQLI IEESVLTQKK LLNKFCNDNN LDLASFSFLG PKGSYSHIAA
SQYAEQNFKT CIENACLSFN EVIQSVENNQ TDYAVLPIEN SCSGFINEIF DILKKTNLFI
IGEINISINH CLLAIKKIEL NKIKAVYSHP QPFQQCSYFI KKFPNWKIQY TNSTADAMKK
IVKYNITTNA ALGSELGSKI YGLKVLYKNL ANKKKNITRF ILLSRKPVSI SSKIPTKTTL
IFNTGQESGA LAEVLLILKK NKLIMKKLTS QNIYKNPWEE MFYIDVQANL SSSLMQETLE
KIGKITKFIK ILGCYPSENI TPIIP
