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Database: UniProt
Entry: A0A0H3E6C8_BACA1
LinkDB: A0A0H3E6C8_BACA1
Original site: A0A0H3E6C8_BACA1 
ID   A0A0H3E6C8_BACA1        Unreviewed;       285 AA.
AC   A0A0H3E6C8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   16-OCT-2019, entry version 22.
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   OrderedLocusNames=BATR1942_11715 {ECO:0000313|EMBL:ADP33274.1};
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP33274.1, ECO:0000313|Proteomes:UP000006867};
RN   [1] {ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A.,
RA   Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Tapia R., Bishop-Lilly K.,
RA   Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADP33274.1, ECO:0000313|Proteomes:UP000006867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942 {ECO:0000313|EMBL:ADP33274.1,
RC   ECO:0000313|Proteomes:UP000006867};
RX   PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA   Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA   Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA   Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA   Skowronski E.W.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus var. globigii, a historical biowarfare simulant.";
RL   PLoS ONE 6:E17836-E17836(2011).
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; CP002207; ADP33274.1; -; Genomic_DNA.
DR   RefSeq; WP_003325255.1; NC_014639.1.
DR   STRING; 720555.BATR1942_11715; -.
DR   EnsemblBacteria; ADP33274; ADP33274; BATR1942_11715.
DR   KEGG; bae:BATR1942_11715; -.
DR   KO; K04518; -.
DR   OMA; HTRFVIL; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; BATR720555:G1GOO-2296-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000006867; 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; 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:UP000006867};
KW   Lyase {ECO:0000256|RuleBase:RU361254, ECO:0000313|EMBL:ADP33274.1};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254}.
FT   DOMAIN        2    183       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      204    281       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        176    176       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   285 AA;  31860 MW;  D4314467433AA5F6 CRC64;
     MKVGYLGPEA TFTHLAVSSC FQNDVTHVAY HTIPECMDAA VAGEIDFAFV PLENALEGSV
     NLTIDYLIHE QPLPIVGEMT LPIHQHLLVH PSRENKWESL GQIYSHSHAI AQCHKFLHKH
     FKTVPYEYAK STGAAAKYVS ENPQLNIGVI ANEMAAATYE LKIVKHDIQD YRDNHTRFVI
     LSPDENAGYE VNPHLVSRPK TTLMVTLPQD DQSGALHRVL SAFSWRNLNL SKIESRPTKT
     GLGHYFFIID IEMALDAVLI PGAIQELETL GCSVKLLGNY QSYKL
//
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