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Database: UniProt
Entry: A4T6G3
LinkDB: A4T6G3
Original site: A4T6G3 
ID   PHEA_MYCGI              Reviewed;         309 AA.
AC   A4T6G3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   29-OCT-2014, entry version 50.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=Mflv_1145;
OS   Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens
OS   (strain ATCC 700033 / PYR-GCK)).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
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., Miller C.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-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. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU01007}.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00517}.
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DR   EMBL; CP000656; ABP43627.1; -; Genomic_DNA.
DR   RefSeq; YP_001132415.1; NC_009338.1.
DR   STRING; 350054.Mflv_1145; -.
DR   EnsemblBacteria; ABP43627; ABP43627; Mflv_1145.
DR   GeneID; 4972471; -.
DR   KEGG; mgi:Mflv_1145; -.
DR   PATRIC; 18030316; VBIMycGil17082_1170.
DR   eggNOG; COG0077; -.
DR   HOGENOM; HOG000018970; -.
DR   KO; K04518; -.
DR   OMA; EHGDWAK; -.
DR   OrthoDB; EOG6WHNT1; -.
DR   BioCyc; MGIL350054:GHK8-1149-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; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 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    309       Prephenate dehydratase.
FT                                /FTId=PRO_0000382034.
FT   DOMAIN        3    191       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      205    282       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   SITE        184    184       Essential for activity. {ECO:0000250}.
SQ   SEQUENCE   309 AA;  32171 MW;  4E6E0668B4E3FEE6 CRC64;
     MPGIAYLGPE GTFTEAALRA LDAQGLIPAT QSGAGSVTPL ATDSTPAALA AVRAGDADFA
     CVPIENSIDG PVIPTLDSLA DGVPLQIYAE LTLDVSFTIA VRPGVTAADV RTVAAFPVAA
     AQVKRWLSEN LPNVELVPSN SNAAAARDVA DGRAEAAVST ALATERYGLD TLAAGIVDEP
     NARTRFVLVG CPGPPPKRTG SDRTSVVLRL DNVPGALVTA MNELAIRGID LTGIESRPTR
     TELGTYRFYL DFVGHIDDDA VAGALRALHR RCADVRYLGS WPTGETGGAA PPPLDEATAW
     LQRLREGRP
//
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