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Database: UniProt
Entry: A0A0B0CZ99_9BACI
LinkDB: A0A0B0CZ99_9BACI
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ID   A0A0B0CZ99_9BACI        Unreviewed;       291 AA.
AC   A0A0B0CZ99;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
DE            Short=PDT {ECO:0000256|RuleBase:RU361254};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
GN   Name=pheA {ECO:0000256|RuleBase:RU361254};
GN   ORFNames=LD39_11740 {ECO:0000313|EMBL:KHE70324.1};
OS   Halobacillus sp. BBL2006.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE70324.1, ECO:0000313|Proteomes:UP000030879};
RN   [1] {ECO:0000313|EMBL:KHE70324.1, ECO:0000313|Proteomes:UP000030879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBL2006 {ECO:0000313|EMBL:KHE70324.1,
RC   ECO:0000313|Proteomes:UP000030879};
RA   Kirchner G., Treves D., Francis J.III.;
RT   "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT   BBL2006.";
RL   Submitted (SEP-2014) 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; EC=4.2.1.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00000913,
CC         ECO:0000256|RuleBase:RU361254};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741, ECO:0000256|RuleBase:RU361254}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHE70324.1}.
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DR   EMBL; JRNX01000377; KHE70324.1; -; Genomic_DNA.
DR   RefSeq; WP_035546619.1; NZ_JRNX01000377.1.
DR   AlphaFoldDB; A0A0B0CZ99; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000030879; 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   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13633; PBP2_Sa-PDT_like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU361254};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222,
KW   ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030879}.
FT   DOMAIN          5..182
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          201..278
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            175
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   291 AA;  32161 MW;  D657A861AE708E8A CRC64;
     MENQRIGYLG PKGTFTKMAV DALFDGGSFI SYESIPACLD AVERGDIETG VVPLENAIEG
     SVHLTIDYLV HQVNQSIIAE MTVPIKQHLL VNPDYQGEKI KKIYSHSHAI AQCHQYLHKH
     FPDAELEYTA STGKAAEIVA ASGNDVAAIG NHLAAEENGL KLLDTNIHDY DNNHTRFAVV
     QKNAKALKVK DHPVSRHKTT VMVTLPKDYA GALHQVLAAF SWRKMNLSKI ESRPMKTGLG
     NYFFLIDVDQ PYDQVLFPGV QAELEALGCQ LKVLGTYPAY QIDVPTPVRK P
//
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