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Entry: A0A0H4P182_9BACI
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ID   A0A0H4P182_9BACI        Unreviewed;       369 AA.
AC   A0A0H4P182;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE            EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN   ORFNames=BSM4216_2334 {ECO:0000313|EMBL:AKP47574.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP47574.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP47574.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP47574.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001162};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005067}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007964}.
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DR   EMBL; CP012024; AKP47574.1; -; Genomic_DNA.
DR   RefSeq; WP_048623563.1; NZ_CP012024.1.
DR   AlphaFoldDB; A0A0H4P182; -.
DR   STRING; 1479.BSM4216_2334; -.
DR   KEGG; bsm:BSM4216_2334; -.
DR   eggNOG; COG0287; Bacteria.
DR   OrthoDB; 9802008at2; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000036353; Chromosome.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04909; ACT_PDH-BS; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AKP47574.1};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT   DOMAIN          3..294
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   DOMAIN          299..369
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   369 AA;  41023 MW;  F8AED124E1BBB27F CRC64;
     MKGTVLIAGI GLIGGSLALT IKEAHPHATV IGFDIKESER KLAKALGVVD EESDSFIELA
     ARADLIILAV PVKQTEILIE ELVQNADKLK KNVIVTDTGS TKARIMQKGK KLNDLGISFI
     GGHPMAGSHK SGVAAAKKIL FENAFYLLTP DEQTSTEELN TLKEWLKGTK AKMIEVTPEE
     HDQLTGVISH FPHVIASSLV HQARHFDQQN PLVSRLAAGG FRDITRIASS NPEMWKDVSL
     HNKETLIQLL EVWQKEMHKF AELLKDENGE GLYEYFAAAK TFRDQLPSSS KGAIPAFYDL
     YVDVPDYPGV ISEITGYLAE ERISITNIRI METREDVYGV LVISFQNDHD RMKAKKCIQK
     HTNYDVFLA
//
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