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Database: UniProt
Entry: P57472
LinkDB: P57472
Original site: P57472 
ID   PHEA_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-SEP-2014, entry version 99.
DE   RecName: Full=P-protein;
DE   Includes:
DE     RecName: Full=Chorismate mutase;
DE              Short=CM;
DE              EC=5.4.99.5;
DE   Includes:
DE     RecName: Full=Prephenate dehydratase;
DE              Short=PDT;
DE              EC=4.2.1.51;
GN   Name=pheA; Synonyms=aroQ/pheA; OrderedLocusNames=BU392;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
OS   (Acyrthosiphon pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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)
RT   displays changes in the regulatory domain that suggest its
RT   desensitization to 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
RT   Buchnera sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- CATALYTIC ACTIVITY: Chorismate = prephenate.
CC   -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate
CC       biosynthesis; prephenate from chorismate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The regulatory domain shows changes in the ESRP sequence,
CC       which is involved in the allosteric binding of phenylalanine.
CC       These changes suggest the desensitization of the enzyme to
CC       inhibition by phenylalanine and would permit the overproduction of
CC       phenylalanine.
CC   -!- SIMILARITY: Contains 1 ACT domain.
CC   -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
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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   ProteinModelPortal; P57472; -.
DR   EnsemblBacteria; BAB13095; BAB13095; BAB13095.
DR   GeneID; 1109745; -.
DR   KEGG; buc:BU392; -.
DR   PATRIC; 21244324; VBIBucAph127364_0406.
DR   eggNOG; COG0077; -.
DR   HOGENOM; HOG000018972; -.
DR   KO; K14170; -.
DR   OMA; IDVQANL; -.
DR   OrthoDB; EOG6WHNT1; -.
DR   BioCyc; BAPH107806:GBZJ-392-MONOMER; -.
DR   BRENDA; 4.2.1.51; 1015.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
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; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR002701; Chorismate_mutase.
DR   InterPro; IPR020822; Chorismate_mutase_type_II.
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   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   4: Predicted;
KW   Allosteric enzyme; Amino-acid biosynthesis;
KW   Aromatic amino acid biosynthesis; Complete proteome; Cytoplasm;
KW   Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    385       P-protein.
FT                                /FTId=PRO_0000119182.
FT   DOMAIN        1     92       Chorismate mutase.
FT   DOMAIN      105    285       Prephenate dehydratase.
FT   DOMAIN      299    376       ACT.
FT   REGION      286    385       Regulatory.
FT   SITE        278    278       Essential for prephenate dehydratase
FT                                activity (Potential).
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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