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Database: UniProt
Entry: A0A0G1L738_9BACT
LinkDB: A0A0G1L738_9BACT
Original site: A0A0G1L738_9BACT 
ID   A0A0G1L738_9BACT        Unreviewed;       289 AA.
AC   A0A0G1L738;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   ORFNames=UW93_C0003G0076 {ECO:0000313|EMBL:KKT91796.1};
OS   Parcubacteria group bacterium GW2011_GWC1_45_13.
OC   Bacteria.
OX   NCBI_TaxID=1618914 {ECO:0000313|EMBL:KKT91796.1, ECO:0000313|Proteomes:UP000034639};
RN   [1] {ECO:0000313|EMBL:KKT91796.1, ECO:0000313|Proteomes:UP000034639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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         Evidence={ECO:0000256|ARBA:ARBA00000913};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKT91796.1}.
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DR   EMBL; LCKG01000003; KKT91796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1L738; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000034639; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04880; ACT_AAAH-PDT-like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT   DOMAIN          2..196
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   SITE            188
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   289 AA;  31240 MW;  2CDADE50106843E9 CRC64;
     MKITYLGPAG ATFSAMAYDK LAFMFDAPKT GDSGTELLLA QSNEEILPLM LKHGGYGVMA
     METKAQGRID PPVNSFIELL EAYDERCPVS IVAAIRMRLN FALMARPGLS VDKVKMILAH
     KQALGACRKR LETLGAELIE ALSNGQAAED VATKDDLAYA AALGPSVAAE KYGLVILNGA
     FEDKEAVTTF FLLSAEGSAS WTCEENRGLM VFRTKHKPGA LVSVLTPFAR LGINLIHIHS
     LYSGNGEYDF AVETECGFTE LGSHLLAGRN AREFMTKHIV FGPFAILDV
//
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