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Database: UniProt
Entry: P27603
LinkDB: P27603
Original site: P27603 
ID   PHEA_PSEST              Reviewed;         365 AA.
AC   P27603; Q9RI01;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   29-OCT-2014, entry version 85.
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   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JM300 / DSM 10701;
RX   PubMed=1919506;
RA   Fischer R.S., Zhao G., Jensen R.A.;
RT   "Cloning, sequencing, and expression of the P-protein gene (pheA) of
RT   Pseudomonas stutzeri in Escherichia coli: implications for
RT   evolutionary relationships in phenylalanine biosynthesis.";
RL   J. Gen. Microbiol. 137:1293-1301(1991).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=JM300 / DSM 10701;
RX   PubMed=10368439; DOI=10.1007/PL00006523;
RA   Xie G., Bonner C.A., Jensen R.A.;
RT   "A probable mixed-function supraoperon in Pseudomonas exhibits gene
RT   organization features of both intergenomic conservation and gene
RT   shuffling.";
RL   J. Mol. Evol. 49:108-121(1999).
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 ACT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU01007}.
CC   -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00515}.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00517}.
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DR   EMBL; AF038578; AAD47360.1; -; Genomic_DNA.
DR   PIR; A44764; A44764.
DR   ProteinModelPortal; P27603; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
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; TIGR01807; CM_P2; 1.
DR   PROSITE; PS51671; ACT; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis.
FT   CHAIN         1    365       P-protein.
FT                                /FTId=PRO_0000119190.
FT   DOMAIN        1     96       Chorismate mutase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00515}.
FT   DOMAIN       97    272       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      284    361       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   REGION      273    365       Regulatory (Phe-binding).
FT   SITE        265    265       Essential for prephenate dehydratase
FT                                activity. {ECO:0000255}.
SQ   SEQUENCE   365 AA;  40744 MW;  88E2457FDB132FD4 CRC64;
     MSEADQLKAL RVRIDSLDER ILDLISERAR CAQEVARVKT ASWPKAEEAV FYRPEREAWV
     LKHIMELNKG PLDNEEMARL FREIMSSCLA LEQPLRVAYL GPEGTFSQAA ALKHFGHSVI
     SKPMAAIDEV FREVVAGAVN FGVVPVENST EGAVNHTLDS FLEHDIVICG EVELRIHHHL
     LVGETTKTDR ITRIYSHAQS LAQCRKWLDA HYPNVERVAV SSNADAAKRV KSEWNSAAIA
     GDMAAQLYGL SKLAEKIEDR PVNSTRFLII GSQEVPPTGD DKTSIIVSMR NKPGALHELL
     MPFHSNGIDL TRIETRPSRS GKWTYVFFID CMGHHQDPLI KNVLEKIGHE AVALKVLGSY
     PKAVL
//
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