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Database: UniProt
Entry: A0A1W9PNI4_9BACT
LinkDB: A0A1W9PNI4_9BACT
Original site: A0A1W9PNI4_9BACT 
ID   A0A1W9PNI4_9BACT        Unreviewed;       281 AA.
AC   A0A1W9PNI4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   10-APR-2019, entry version 9.
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=B5M50_01970 {ECO:0000313|EMBL:OQX59889.1};
OS   candidate division KSB1 bacterium 4484_219.
OC   Bacteria; candidate division KSB1.
OX   NCBI_TaxID=1968530 {ECO:0000313|EMBL:OQX59889.1};
RN   [1] {ECO:0000313|EMBL:OQX59889.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4484_219 {ECO:0000313|EMBL:OQX59889.1};
RX   PubMed=28835260; DOI=10.1186/s40168-017-0322-2;
RA   Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT   "Genomic insights into potential interdependencies in microbial
RT   hydrocarbon and nutrient cycling in hydrothermal sediments.";
RL   Microbiome 5:106-106(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OQX59889.1}.
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DR   EMBL; MZGM01000024; OQX59889.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
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; PF01842; ACT; 1.
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}.
FT   DOMAIN        6    182       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      194    271       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        175    175       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   281 AA;  31559 MW;  8976182013410FB4 CRC64;
     MAKSCYVAYQ GEKGAYSEEA IIQCFGSEVD TCGFETSEEV VEAVQANKAE FGFLPAENSI
     AGTITQTYDL LLESKLTIVG EYYFRIHHNL LALPGVSITE ITNVYSHPHA LAQCQQFLKK
     YSLKPLPEWD TAGSARKIRQ ENLLTSAAIA SKRAAQIHNL QVLFESIEDV SHNTTRFFIL
     GKGEVARAEK SKTSILFSVR DTPGALLHCL EVFATYGLNL TKIESRPERN RPWHYIFYLD
     FEGYIEDPPV EQALVQLLKR ALFVKVLGSY PEGALPEWQK T
//
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