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Database: UniProt
Entry: A0A224X847_9LACT
LinkDB: A0A224X847_9LACT
Original site: A0A224X847_9LACT 
ID   A0A224X847_9LACT        Unreviewed;       275 AA.
AC   A0A224X847;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   16-OCT-2019, entry version 17.
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=RsY01_1100 {ECO:0000313|EMBL:GAX47500.1};
OS   Lactococcus reticulitermitis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=2025039 {ECO:0000313|EMBL:GAX47500.1, ECO:0000313|Proteomes:UP000218689};
RN   [1] {ECO:0000313|Proteomes:UP000218689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs-Y01 {ECO:0000313|Proteomes:UP000218689};
RA   Ohkuma M., Yuki M.;
RT   "Draft genome sequence of Lactococcus sp. strain Rs-Y01, isolated from
RT   the gut of the lower termite Reticulitermes speratus.";
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:GAX47500.1}.
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DR   EMBL; BEDT01000002; GAX47500.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000218689; Unassembled WGS sequence.
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; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF00800; PDT; 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:UP000218689};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254}.
FT   DOMAIN        2    181       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      197    269       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   275 AA;  30853 MW;  E70B99798C7F7C25 CRC64;
     MKIGFLGPKA SFTYAVAHAA FPDDSHQLLA FDSITEVIRS YEQGLVDYAI VPVENSIEGS
     VHQTVDYLFL QAEHIRAQAE IIQPIKQQLM ATSSDKKIEK IFSHPQAIAQ SLKYVQHHFP
     DAKIESTDST AYAAKFVAEH PEKNFAAIAP VASSLAYGLT IIAQDIQEID ENFTRFWLLG
     ETTPQIDLPA VTEKMTLALT LSDNLPGALY KALQIFADFG INLTKIESRP LKTFLGEYFF
     LIDAQFSENY LYLIHALEKL GITVKRLGKY KVYQM
//
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