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Database: UniProt
Entry: A0A1W5ZVB6_9BACI
LinkDB: A0A1W5ZVB6_9BACI
Original site: A0A1W5ZVB6_9BACI 
ID   A0A1W5ZVB6_9BACI        Unreviewed;       366 AA.
AC   A0A1W5ZVB6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE            EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN   ORFNames=HM131_10570 {ECO:0000313|EMBL:ARI77256.1};
OS   Halobacillus mangrovi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=402384 {ECO:0000313|EMBL:ARI77256.1, ECO:0000313|Proteomes:UP000192527};
RN   [1] {ECO:0000313|EMBL:ARI77256.1, ECO:0000313|Proteomes:UP000192527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTB 131 {ECO:0000313|EMBL:ARI77256.1,
RC   ECO:0000313|Proteomes:UP000192527};
RA   Lee S.-J., Park M.-K., Kim J.-Y., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F.,
RA   Lee D.-W.;
RT   "The whole genome sequencing and assembly of Halobacillus mangrovi
RT   strain.";
RL   Submitted (APR-2017) 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; CP020772; ARI77256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W5ZVB6; -.
DR   STRING; 402384.HM131_10570; -.
DR   KEGG; hmn:HM131_10570; -.
DR   OrthoDB; 9802008at2; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000192527; 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   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;  41095 MW;  1AD6F2FCA4E32571 CRC64;
     MKETVLIVGL GLIGGSLAMN VSEKEDVFVI GMDKDEETMN MALKQGVIHQ ASKSFSKAVK
     EADILILATP ISITIEFLNQ LEDVDLSKPL LVTDVSSVKN KVLEAANKLT HPRLSFVGGH
     PMAGSHKQGY TAAKPHLFEN AIYVLTPSIH ATEAEAERLK QLFSKTGARF LTFTTSEHDE
     MTAVISHFPH LIASSLVHQA REWQKTHPYI EHLAAGGFKD ITRIASSNPK LWQDIFFQNR
     TLLISMLDDW IDEMQTVRNF LQEQESEQTY QYLVEAKQYR DGLPVREKGA IPSFYDIYVD
     IHDQPGAIHD VIGLLADENI SIKNIQILEI REGITGVLRI SFATSEDQVG SKKLLEKHQY
     EVMLQQ
//
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