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Database: UniProt
Entry: Q89AE5
LinkDB: Q89AE5
Original site: Q89AE5 
ID   CMPDT_BUCBP             Reviewed;         371 AA.
AC   Q89AE5;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=bbp_355;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27074.1; -; Genomic_DNA.
DR   RefSeq; WP_011091475.1; NC_004545.1.
DR   AlphaFoldDB; Q89AE5; -.
DR   SMR; Q89AE5; -.
DR   STRING; 224915.bbp_355; -.
DR   EnsemblBacteria; AAO27074; AAO27074; bbp_355.
DR   GeneID; 56470894; -.
DR   KEGG; bab:bbp_355; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   HOGENOM; CLU_035008_1_0_6; -.
DR   OMA; PAINTRC; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000601; 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; 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   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   TIGRFAMs; TIGR01797; CM_P_1; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 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..371
FT                   /note="Bifunctional chorismate mutase/prephenate
FT                   dehydratase"
FT                   /id="PRO_0000119184"
FT   DOMAIN          1..92
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT   DOMAIN          104..284
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   REGION          285..371
FT                   /note="Regulatory"
FT                   /evidence="ECO:0000250"
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            277
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  43136 MW;  78AEEB3DD55FCEB4 CRC64;
     MTLKNALLAF RNAINILDKN LINLLAKRKQ LSLNIAHTKV KNNYPVRDIE REQMLLKNLT
     ILGEKHFLNK KYIESLFSII LEDSVLTQKK WIKKYNLNKY KLEKISFLGS FGSYSHLAAQ
     KYAKKHSKIL TDKIYKNFSD VITSVEQQQS TYAILPIENQ SSGLIIEVYK LLQKTPLFII
     GNIYIHANHC LLAKKYTPIL KIQKIYSHIQ PFKQCSKFIS LFPNWKLSNT TSTSEAIQHV
     AKENDNTIAA LGNESYGELN KLEVIAKNIS NKRNNITQFI ILAQKKTYIT NKKTHLKTII
     LISKKNENCE KIIRNILHKN KITLLKLKYY VTSKVLLEKI FFIEIENIYC IKHILKQFTI
     EIKCIKILGC F
//
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