ID   PHEA_ENTAG              Reviewed;         387 AA.
AC   Q02286;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-APR-2013, entry version 80.
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;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pantoea.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1512561;
RA   Xia T., Zhao G., Fischer R.S., Jensen R.A.;
RT   "A monofunctional prephenate dehydrogenase created by cleavage of the
RT   5' 109 bp of the tyrA gene from Erwinia herbicola.";
RL   J. Gen. Microbiol. 138:1309-1316(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-301.
RX   PubMed=1444388;
RA   Xia T., Zhao G., Jensen R.A.;
RT   "Loss of allosteric control but retention of the bifunctional
RT   catalytic competence of a fusion protein formed by excision of 260
RT   base pairs from the 3' terminus of pheA from Erwinia herbicola.";
RL   Appl. Environ. Microbiol. 58:2792-2798(1992).
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   -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
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DR   EMBL; X60420; CAA42949.1; -; Genomic_DNA.
DR   EMBL; M74134; AAA24853.1; -; Genomic_DNA.
DR   PIR; S26053; S26053.
DR   ProteinModelPortal; Q02286; -.
DR   SMR; Q02286; 6-97.
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; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis.
FT   CHAIN         1    387       P-protein.
FT                                /FTId=PRO_0000119187.
FT   DOMAIN        1     92       Chorismate mutase.
FT   DOMAIN      105    285       Prephenate dehydratase.
FT   REGION      286    387       Regulatory (Phe-binding).
FT   SITE        278    278       Essential for prephenate dehydratase
FT                                activity (Potential).
FT   CONFLICT    301    301       I -> K (in Ref. 2; AAA24853).
SQ   SEQUENCE   387 AA;  43183 MW;  8C4F29C5678E42C6 CRC64;
     MNPDNPLLAL RDKISAVDKK LLTLLAERRL LAVEVAQAKL ATHRPIRDVE RERALLENLI
     VLGKAHNLDA HYITRLFQLV IEDSVLTQQA LLQKNLNHPH AHAARIAFLG PKGSYSHLAA
     RNYASRHFDS MVECGCLKFH DIIKQVENGV ADYAVMPIEN TSSGSINDVY DLLQQTSLSI
     VGELTLPIDH CVLVNGPTDL QQIETVYSHP QPFQQCSQFI NRFPHWKIEY TESTAAAMEK
     VAALNSPKVA ALGSEAGGEL YQLQVLERNL ANQQQNHTRF IVLARKAIEV SDQVPAKTTL
     IMATGQQAGA LVDALLVLRQ HNLIMSKLES RPINGNPWEE MFYIDVQGNL QSERMQQALQ
     ELQTMTRSLK VLGCYPSENV VPAEPGR
//