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 01-MAY-2013, entry version 91.
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 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 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; WREVMSA; -.
DR ProtClustDB; CLSK316081; -.
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:0004106; F:chorismate mutase activity; IEA:EC.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA: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; 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; Chorismate_mut; 1.
DR TIGRFAMs; TIGR01797; CM_P_1; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; FALSE_NEG.
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 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
//
