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Database: UniProt
Entry: A0A1Y3M1R0_9MICC
LinkDB: A0A1Y3M1R0_9MICC
Original site: A0A1Y3M1R0_9MICC 
ID   A0A1Y3M1R0_9MICC        Unreviewed;       310 AA.
AC   A0A1Y3M1R0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   18-SEP-2019, entry version 10.
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=B8W74_09815 {ECO:0000313|EMBL:OUM42370.1}, CI784_11815
GN   {ECO:0000313|EMBL:PPB45712.1};
OS   Arthrobacter agilis.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=37921 {ECO:0000313|EMBL:OUM42370.1, ECO:0000313|Proteomes:UP000195940};
RN   [1] {ECO:0000313|EMBL:PPB45712.1, ECO:0000313|Proteomes:UP000238766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.15723 {ECO:0000313|EMBL:PPB45712.1,
RC   ECO:0000313|Proteomes:UP000238766};
RX   PubMed=7547308; DOI=.1099/00207713-45-4-837;
RA   Koch C., Schumann P., Stackebrandt E.;
RT   "Reclassification of Micrococcus agilis (Ali-Cohen 1889) to the genus
RT   Arthrobacter as Arthrobacter agilis comb. nov. and emendation of the
RT   genus Arthrobacter.";
RL   Int. J. Syst. Bacteriol. 45:837-839(1995).
RN   [2] {ECO:0000313|EMBL:OUM42370.1, ECO:0000313|Proteomes:UP000195940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4042 {ECO:0000313|EMBL:OUM42370.1,
RC   ECO:0000313|Proteomes:UP000195940};
RA   Crovadore J., Blanc P., Chablais R., Cochard B., Grizard D.,
RA   Lefort F.;
RT   "Two whole genome sequences of Arthrobacter agilis isolates 4041 and
RT   4042 strain commercialized as biostimulants.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PPB45712.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15723 {ECO:0000313|EMBL:PPB45712.1};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) 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:OUM42370.1}.
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DR   EMBL; NFSD01000032; OUM42370.1; -; Genomic_DNA.
DR   EMBL; PRKX01000028; PPB45712.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000195940; Unassembled WGS sequence.
DR   Proteomes; UP000238766; 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:UP000195940,
KW   ECO:0000313|Proteomes:UP000238766};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195940}.
FT   DOMAIN        6    186       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      201    276       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        179    179       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   310 AA;  32426 MW;  5FC165C1A2C85C52 CRC64;
     MTPPSSYTYL GPEGTFTEAA LLQVPGAGGA RRVPALTVGS ALDAVRAGSV DAAMVPIENS
     VEGGVSATLD AIAVGAPLRI LREELVPITF VLAGRPGAGL GDVRRIATHG HAWAQCRTWV
     DTNISDAEYF PASSTAAAAH GLAEGEEGYD AAICSPLVAE RLGLAVLARD IGDVTDAVTR
     FVLVGRPEDL PPRTGADKTT LVIPLPEDHP GALMQILDQF AARGVNLSRI ESRPTGQFLG
     DYFFSVDADG HVEDARVADA LKGLHRISPG LRFLGSYARA DRRSPAVERH TSDDAFAAAD
     GWLGDILGGR
//
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