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Database: UniProt
Entry: A0A366EJ80_9BACI
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ID   A0A366EJ80_9BACI        Unreviewed;       366 AA.
AC   A0A366EJ80;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE            EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN   ORFNames=DES48_101276 {ECO:0000313|EMBL:RBP01539.1};
OS   Paraliobacillus ryukyuensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX   NCBI_TaxID=200904 {ECO:0000313|EMBL:RBP01539.1, ECO:0000313|Proteomes:UP000252254};
RN   [1] {ECO:0000313|EMBL:RBP01539.1, ECO:0000313|Proteomes:UP000252254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15140 {ECO:0000313|EMBL:RBP01539.1,
RC   ECO:0000313|Proteomes:UP000252254};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) 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}.
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:RBP01539.1}.
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DR   EMBL; QNRI01000001; RBP01539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366EJ80; -.
DR   STRING; 200904.GCA_900168775_01834; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000252254; Unassembled WGS sequence.
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; 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; 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; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-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   Reference proteome {ECO:0000313|Proteomes:UP000252254};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT   DOMAIN          3..291
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   DOMAIN          296..366
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   366 AA;  41472 MW;  3593C8933BC2B80B CRC64;
     MTKKILIVGL GLIGASLAIN IKKQEDTYLI GYDTDEETLE YAQVHQIVNE VTTKFTEKIT
     DVDYCLLAAP VSKTVDLIKQ IQQISFNRPI IITDVSSVKQ PIMDAVARLD QPNVSFIGGH
     PMAGSHKKGI HAAKEHLFEN ALYILTPDTN ATDEQMEALK RLLAHTKSSF LQLNPTEHDE
     MTSVISHFPH LIASSLVQQA KKWQKKHDRI PHLAAGGFRD ITRIASSNPA MWQDIFFQNK
     KIIHHLLTDW INEMQDLQKL LTNDDRTTMY DYLKQAKEYR DGLDARKRGA LPSFYDVYVD
     IFDQTGALLK VVSILAEGDI SIKNIEILEI REGITGVLRV SLMTQKQQVN AHQLLTKHGY
     ETMLQE
//
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