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Database: UniProt
Entry: A0A1J0A5T2_9ENTE
LinkDB: A0A1J0A5T2_9ENTE
Original site: A0A1J0A5T2_9ENTE 
ID   A0A1J0A5T2_9ENTE        Unreviewed;       275 AA.
AC   A0A1J0A5T2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
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=BHY08_05190 {ECO:0000313|EMBL:APB31273.1};
OS   Vagococcus teuberi.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Vagococcus.
OX   NCBI_TaxID=519472 {ECO:0000313|EMBL:APB31273.1, ECO:0000313|Proteomes:UP000191200};
RN   [1] {ECO:0000313|EMBL:APB31273.1, ECO:0000313|Proteomes:UP000191200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21459 {ECO:0000313|EMBL:APB31273.1,
RC   ECO:0000313|Proteomes:UP000191200};
RA   Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA   Stevens M.J., Meile L.;
RT   "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour
RT   milk fene.";
RL   Submitted (SEP-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; CP017267; APB31273.1; -; Genomic_DNA.
DR   RefSeq; WP_071456864.1; NZ_CP017267.1.
DR   KEGG; vte:BHY08_05190; -.
DR   KO; K04518; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; GCF_001870205:G1FCI-1050-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000191200; Chromosome.
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; PS00857; PREPHENATE_DEHYDR_1; 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:UP000191200};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191200}.
FT   DOMAIN        2    178       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      193    270       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   275 AA;  31108 MW;  F606645B9816722A CRC64;
     MEVGYLGPKN SFTYKAASYY FDDSLLQPYA SIANCLSALK KNQVDYAVVP IENSLEGSVH
     TSMDGLFQEK DITVCREIIL PIQQNLLVND LTIIPKKILS HPQALAQSQQ FLETYYPDVL
     IEQVPSTTFA AEYVAEHPSE SVAAIASKEA ASEYGLEILS AGIQDNRFNQ TRFWLLGKEL
     LNHDNRLPEK MTLFITLPKN APGILHKVLS AFAWREIDLS KIESRPLKTE LGEYYFIIDV
     LIHDNIKLVE YALEEITLLG AKYQQLGYYP IVIKE
//
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