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Database: UniProt
Entry: A0A150F454_9BACI
LinkDB: A0A150F454_9BACI
Original site: A0A150F454_9BACI 
ID   A0A150F454_9BACI        Unreviewed;       285 AA.
AC   A0A150F454;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-FEB-2019, entry version 19.
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=AXI58_03150 {ECO:0000313|EMBL:KXZ15271.1};
OS   Bacillus nakamurai.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1793963 {ECO:0000313|EMBL:KXZ15271.1, ECO:0000313|Proteomes:UP000075430};
RN   [1] {ECO:0000313|EMBL:KXZ15271.1, ECO:0000313|Proteomes:UP000075430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-41092 {ECO:0000313|EMBL:KXZ15271.1,
RC   ECO:0000313|Proteomes:UP000075430};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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}.
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:KXZ15271.1}.
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DR   EMBL; LSBA01000036; KXZ15271.1; -; Genomic_DNA.
DR   RefSeq; WP_061522930.1; NZ_LSBA01000036.1.
DR   EnsemblBacteria; KXZ15271; KXZ15271; AXI58_03150.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000075430; 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; 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:UP000075430};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
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;  31881 MW;  A7C83CAA7048F599 CRC64;
     MKVGYLGPEA TFTHLAVSSC FQNSMTQAAY HTIPACMDAA VAGEVDLAFV PLENALEGSV
     NLTIDYLIHE QPLSIVGEMT LPIHQHLLVH PSRENEWKHL EKIYSHSHAI AQCHKFLHRH
     FSSVPYEYAK STGAAAKYVS EHSELPIGVI ANEMAAATYG LRIVKRDIQD YQDNHTRFII
     LSPEKDVSFE VNKKLSSRPK TTLMVTLPQD DQSGALHRVL SAFSWRNLNL SKIESRPTKT
     GLGNYFFIID IEQAMDKVLI PGAIQELEAL GCRVKLLGTY QSYCL
//
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