ID   PHEA_MYCSJ              Reviewed;         315 AA.
AC   A3Q7Q1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   01-MAY-2013, entry version 40.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=Mjls_5415;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Miller C.D., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Contains 1 ACT domain.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
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DR   EMBL; CP000580; ABO01179.1; -; Genomic_DNA.
DR   RefSeq; YP_001073669.1; NC_009077.1.
DR   ProteinModelPortal; A3Q7Q1; -.
DR   STRING; 164757.Mjls_5415; -.
DR   EnsemblBacteria; ABO01179; ABO01179; Mjls_5415.
DR   GeneID; 4881112; -.
DR   KEGG; mjl:Mjls_5415; -.
DR   PATRIC; 18097111; VBIMycSp51234_5455.
DR   eggNOG; COG0077; -.
DR   HOGENOM; HOG000018970; -.
DR   KO; K04518; -.
DR   OMA; CRKWLDA; -.
DR   ProtClustDB; PRK11898; -.
DR   BioCyc; MSP164757:GHV3-5468-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; ISS:UniProtKB.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 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;
KW   Complete proteome; Lyase; Phenylalanine biosynthesis.
FT   CHAIN         1    315       Prephenate dehydratase.
FT                                /FTId=PRO_0000382040.
FT   DOMAIN        3    190       Prephenate dehydratase.
FT   DOMAIN      203    269       ACT.
FT   SITE        183    183       Essential for activity (By similarity).
SQ   SEQUENCE   315 AA;  32750 MW;  F88568295FA344D4 CRC64;
     MPRIAYLGPQ GTFTESALLQ MISGAMVPGG DADDTAVTPV PTDSTPAGLE AVRSGAADYA
     CVPIENSIEG SVLPTLDSLA VGAPLQIFAE LTLAVSFSIV VRPDHDGDVA TVAAFPVAAA
     QVRRWLAEHL PAAQLVPAHS NAAAAADVAG GRADAGISTA LAAERYGLRS LAAGVVDEPN
     ARTRFVLVGR PAPPPARTGA DRTSVALRLP NTPGALVAAM TELSIRDIDL TRIESRPTRT
     ELGTYVFFLD CVGHLEDDAV AEALKALHRR CEDVRYLGSW PTGTAAGAPP PSSDEATRWL
     TRLREGLPTP PEGGR
//