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Database: UniProt
Entry: A0A0H4P2B4_9BACI
LinkDB: A0A0H4P2B4_9BACI
Original site: A0A0H4P2B4_9BACI 
ID   A0A0H4P2B4_9BACI        Unreviewed;       281 AA.
AC   A0A0H4P2B4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   10-APR-2019, entry version 16.
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=BSM4216_2734 {ECO:0000313|EMBL:AKP47969.1};
OS   Bacillus smithii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP47969.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP47969.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP47969.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B.,
RA   Vriesendorp B., van de Weijer A.H.P., Schaap P.J., de Vos W.M.,
RA   van der Oost J., van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain
RT   DSM 4216T.";
RL   Submitted (JUL-2015) 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; CP012024; AKP47969.1; -; Genomic_DNA.
DR   RefSeq; WP_003355511.1; NZ_CP012024.1.
DR   STRING; 665952.HMPREF1015_00416; -.
DR   EnsemblBacteria; AKP47969; AKP47969; BSM4216_2734.
DR   KEGG; bsm:BSM4216_2734; -.
DR   KO; K04518; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000036353; Chromosome.
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:UP000036353};
KW   Lyase {ECO:0000256|RuleBase:RU361254, ECO:0000313|EMBL:AKP47969.1};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036353}.
FT   DOMAIN        2    182       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      200    277       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;  31395 MW;  EC37C6BBDCF4BDDD CRC64;
     MKISYLGPAA TFTDLAVCSA FPKAEKKACM TIPECMDEVM EGKADLAVVP LENTLEGTVN
     LTIDYLTQEV DLKIIAELIA PIRQHLLMHP QNAERWKNIE KVMSHPHAIA QCYKFLHTYF
     EKVPCEEAAS TAAAARYVSE HPEELTAAIG NSLSAEKYGL TIVKENIHDY DFNHTKFIVL
     SKEEQKLELP YESGVEKTTI MVTLPSDQAG ALHQVLSALA WRKINLSKIE SRPVKTGLGN
     YFFIIDINQR MDDILLPNAF AEMEALGCTV KVLGSYLSYQ I
//
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