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Database: UniProt
Entry: P57472
LinkDB: P57472
Original site: P57472 
ID   CMPDT_BUCAI             Reviewed;         385 AA.
AC   P57472; Q9L4J2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
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; Synonyms=aroQ/pheA; OrderedLocusNames=BU392;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN.
RX   PubMed=10781569; DOI=10.1128/jb.182.10.2967-2969.2000;
RA   Jimenez N., Gonzalez-Candelas F., Silva F.J.;
RT   "Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays
RT   changes in the regulatory domain that suggest its desensitization to
RT   inhibition by phenylalanine.";
RL   J. Bacteriol. 182:2967-2969(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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:0000269|PubMed:10781569}.
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DR   EMBL; AJ239043; CAB90996.1; -; Genomic_DNA.
DR   EMBL; BA000003; BAB13095.1; -; Genomic_DNA.
DR   RefSeq; NP_240209.1; NC_002528.1.
DR   RefSeq; WP_010896095.1; NC_002528.1.
DR   AlphaFoldDB; P57472; -.
DR   SMR; P57472; -.
DR   STRING; 107806.10039061; -.
DR   PRIDE; P57472; -.
DR   EnsemblBacteria; BAB13095; BAB13095; BAB13095.
DR   KEGG; buc:BU392; -.
DR   PATRIC; fig|107806.10.peg.406; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_035008_1_0_6; -.
DR   OMA; PLMIYRE; -.
DR   BRENDA; 4.2.1.51; 1015.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000001806; 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; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119182"
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;  44338 MW;  7EFD783A4C62F9E7 CRC64;
     MPANNSLLIF RDEINNIDKK IVKLLAERKN LVFKIAQSKI ENNQAIRDIE REKKMLQKLI
     FLGKKYNLKS EYITQLFQLI IEESVATQKK LLKKFCNHNK LIPANFSFLG PKGSYSHIAA
     YKYADLNFQK CITNECSTFE EVVLSVENNQ SDYAVLPIEN TCSGSINEVF DILKKTNLFI
     IGEINIFINH NLLTLKKIEL NKIKTIYSHP QPFQQCSDFI KKFPEWKIKY TKSTADAMKK
     IKKYNDVTNA ALGSEIGSKI YGLEILMKNL ANKENNITRF ILLNRNPKKI SKNIPTTTTL
     IFTTGQEAGS LSKVLSILQE KKLIMKKLTS QKIYKNPWEE MFYIDIQVNL SSTLMQDALE
     KIKKITRFIK ILGCYPSEKI TPIAP
//
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