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Database: UniProt
Entry: A0A1G9QU39_9FIRM
LinkDB: A0A1G9QU39_9FIRM
Original site: A0A1G9QU39_9FIRM 
ID   A0A1G9QU39_9FIRM        Unreviewed;       296 AA.
AC   A0A1G9QU39;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 6.
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=SAMN04488692_11824 {ECO:0000313|EMBL:SDM14380.1};
OS   Halarsenatibacter silvermanii.
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halarsenatibacter.
OX   NCBI_TaxID=321763 {ECO:0000313|EMBL:SDM14380.1, ECO:0000313|Proteomes:UP000199476};
RN   [1] {ECO:0000313|EMBL:SDM14380.1, ECO:0000313|Proteomes:UP000199476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLAS-1 {ECO:0000313|EMBL:SDM14380.1,
RC   ECO:0000313|Proteomes:UP000199476};
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;
CC         EC=4.2.1.51; 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; FNGO01000018; SDM14380.1; -; Genomic_DNA.
DR   BioCyc; GCF_900103135:BLT15_RS09585-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000199476; 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   Complete proteome {ECO:0000313|Proteomes:UP000199476};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199476}.
FT   DOMAIN        2    183       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      199    276       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        176    176       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   296 AA;  33488 MW;  03344BCB665326D3 CRC64;
     MEILYLGPEG TFTDMAARRY FGGCDEHEFH PRPDIGELAR EVDENDGLWG VIPIENSLEG
     SVNLTLDLLA HEIDVKIGAE MNLRINHYLI GKNDQNPAEI RRIISHPQAL AQCRQNLNRI
     ISGEFETEST SSTAAAVSEL KKRDNRTAAI GTRRAAENND LEILVEQLQD NISNWTRFIL
     IGPEDRPDFG HDETIKTSLI SIPVEDRPGI LYEILEEFAV RELNLTKIES RPTRQELGEY
     LFFIDFEGSR YKEEADRAIA GVEEKSSHLK ILGSYPVYEN NYGKIETPLC EKTGGK
//
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