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Database: UniProt
Entry: A0A1H9RKT8_9BACI
LinkDB: A0A1H9RKT8_9BACI
Original site: A0A1H9RKT8_9BACI 
ID   A0A1H9RKT8_9BACI        Unreviewed;       300 AA.
AC   A0A1H9RKT8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   11-DEC-2019, entry version 7.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|RuleBase:RU361254};
DE            Short=PDT {ECO:0000256|RuleBase:RU361254};
DE            EC=4.2.1.51 {ECO:0000256|RuleBase:RU361254};
GN   Name=pheA {ECO:0000256|RuleBase:RU361254};
GN   ORFNames=SAMN05518684_103215 {ECO:0000313|EMBL:SER73382.1};
OS   Salipaludibacillus aurantiacus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=1601833 {ECO:0000313|EMBL:SER73382.1, ECO:0000313|Proteomes:UP000198571};
RN   [1] {ECO:0000313|EMBL:SER73382.1, ECO:0000313|Proteomes:UP000198571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S9 {ECO:0000313|EMBL:SER73382.1,
RC   ECO:0000313|Proteomes:UP000198571};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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         Evidence={ECO:0000256|RuleBase:RU361254};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|RuleBase:RU361254}.
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DR   EMBL; FOGT01000003; SER73382.1; -; Genomic_DNA.
DR   BioCyc; GCF_900111295:BMW59_RS04870-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198571; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198571}.
FT   DOMAIN          3..183
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          203..280
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            176
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   300 AA;  33557 MW;  F8ED5D4B356290BB CRC64;
     MERTGYLGPQ GSFTEAAAKA LVPNDERVPF RSIPDTMDAV KEGTVSRAVV PMENAIEGSV
     NITLDYFIHH QRMNMAAEIS APIEQHLLVA PSHLKSWDRV KKVYSHPHAI AQCHQFLRTY
     LPEAEISYVN STAAAAKYIQ ENQQENAAAI ANDIAAEAYG LKIAQKKIND YENNRTRFML
     FTNEEAPFTN GFISAKTDYK TTMMVGLSSD YSGALHQVLA AFAWRKINLS KIESRPTKTG
     LGNYFFIIDA AMKQDDILIP SVCEELKTLG CEVQILGSYP CFTWEELSGF QKEMVKKEVT
//
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