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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   25-MAY-2022, entry version 82.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=Mflv_1145;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
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., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., 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:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; CP000656; ABP43627.1; -; Genomic_DNA.
DR   RefSeq; WP_011892043.1; NC_009338.1.
DR   AlphaFoldDB; A4T6G3; -.
DR   SMR; A4T6G3; -.
DR   STRING; 350054.Mflv_1145; -.
DR   EnsemblBacteria; ABP43627; ABP43627; Mflv_1145.
DR   KEGG; mgi:Mflv_1145; -.
DR   eggNOG; COG0077; Bacteria.
DR   HOGENOM; CLU_035008_0_0_11; -.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; SSF55021; 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; Lyase;
KW   Phenylalanine biosynthesis.
FT   CHAIN           1..309
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000382034"
FT   DOMAIN          3..191
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          205..282
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   SITE            184
FT                   /note="Essential for activity"
FT                   /evidence="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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