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Database: UniProt
Entry: A0A235G1S8_9NOCA
LinkDB: A0A235G1S8_9NOCA
Original site: A0A235G1S8_9NOCA 
ID   A0A235G1S8_9NOCA        Unreviewed;       304 AA.
AC   A0A235G1S8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-JUN-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=BDB13_1062 {ECO:0000313|EMBL:OYD67538.1};
OS   Rhodococcus sp. OK302.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD67538.1, ECO:0000313|Proteomes:UP000215121};
RN   [1] {ECO:0000313|EMBL:OYD67538.1, ECO:0000313|Proteomes:UP000215121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK302 {ECO:0000313|EMBL:OYD67538.1,
RC   ECO:0000313|Proteomes:UP000215121};
RA   Pelletier D.;
RT   "Populus root and rhizosphere microbial communities from Tennessee,
RT   USA.";
RL   Submitted (AUG-2017) 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}.
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:OYD67538.1}.
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DR   EMBL; NPJZ01000001; OYD67538.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000215121; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000215121};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215121}.
FT   DOMAIN        3    185       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      199    273       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        178    178       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   304 AA;  31616 MW;  FFA8429308617C8D CRC64;
     MPKIAYFGPS GTFTEIALAQ FEAEGTFDGP VERVPAGSPP ATLDLVRDGV VDGAVVPFEN
     SVEGGVAPTL DSLALGSPLQ IVAETEIEVS FSILTRPGVT ADQVRTIGAY PHASAQVRGW
     IAANLPNAEV VLASSNAGAA LDVQAGTVDA GVSTALAGRM LDLASLADNV ADVGGAVTRF
     VLVTKAAPVP ARTGADRTAL VLHLDNAPGS LVTALSEFAA RGIDLTRIES RPMRTELGTY
     RFFVDCVGHV EDSLVAEAMR ALHRKSGVRF LGSWATADST GPQPPSDEEA ISWIEDLKRG
     EGER
//
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