ID   A0A386HNE3_9BACT        Unreviewed;       300 AA.
AC   A0A386HNE3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AYD46991.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:AYD46991.1};
GN   ORFNames=D6B99_04800 {ECO:0000313|EMBL:AYD46991.1};
OS   Arachidicoccus soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Arachidicoccus.
OX   NCBI_TaxID=2341117 {ECO:0000313|EMBL:AYD46991.1, ECO:0000313|Proteomes:UP000266118};
RN   [1] {ECO:0000313|EMBL:AYD46991.1, ECO:0000313|Proteomes:UP000266118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIS59-12 {ECO:0000313|EMBL:AYD46991.1,
RC   ECO:0000313|Proteomes:UP000266118};
RA   Weon H.-Y., Kwon S.-W., Lee S.A.;
RT   "Arachidicoccus sp. nov., a bacterium isolated from soil.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP032489; AYD46991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A386HNE3; -.
DR   KEGG; ark:D6B99_04800; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000266118; 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:InterPro.
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; 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; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AYD46991.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266118}.
FT   DOMAIN          1..286
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   300 AA;  33250 MW;  FEB01412EBFA270C CRC64;
     MTTAVIGLGL IGGTFALALK DEKISTSIIG VENNEIHASK ALQLGLVDEV LPLIEAVKKA
     DLIILATPVT IASEQLTEIL NNISTQIVTD TGSTKLGLIE AIKNHPKRGR YVPSHPMWGT
     EFSGPEAARH NVLNGIVNII CDKNDSDEDA LEFIENIYNR IGMRLVYMNS VAHDTHLAYV
     SHISHISSFA LANTVLGKEK EEDTIFNLAS SGFESTVRLA KSNAATWVPV FKQNKENVLD
     VLNEYISQLR KFKSALEKEN WEYLNELIEN SNEIKRVLDK NVKDENISLK QISKQVVSKK
//