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Database: UniProt
Entry: G2FNS2_9FIRM
LinkDB: G2FNS2_9FIRM
Original site: G2FNS2_9FIRM 
ID   G2FNS2_9FIRM            Unreviewed;       300 AA.
AC   G2FNS2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Prephenate dehydrogenase family protein {ECO:0000313|EMBL:EGW40715.1};
GN   ORFNames=DOT_1339 {ECO:0000313|EMBL:EGW40715.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW40715.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW40715.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW40715.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:EGW40715.1}.
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DR   EMBL; AGAF01000064; EGW40715.1; -; Genomic_DNA.
DR   RefSeq; WP_009615373.1; NZ_AGAF01000064.1.
DR   AlphaFoldDB; G2FNS2; -.
DR   PATRIC; fig|913865.3.peg.1232; -.
DR   eggNOG; COG0287; Bacteria.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
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}.
FT   DOMAIN          19..300
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   300 AA;  32852 MW;  A7293B0471F2B029 CRC64;
     MLDSPEVILT PGWSGLRIPK ACIFGLGLIG GSWAGALHQI GWEVFAVDPE EASIDEAVRR
     GWIQAGWTEM PHFLEVDLIV LALPLQELAK GYDQLVGRIP KGAVVTDVGS IKMEICHKSR
     ISAQTGSCDF HFVAGHPMTG SEQSGFGVAD PGLFKGYPYV LTPEVDCPQQ VVQKLVGIVQ
     QFGAKVVFRE PREHDAEVAM VSHIPHLLAV ALTLATQDAS KEQGSALELA GRSFRDLTRI
     ADSSPEMWKE VLLRNAPAIL DGLTLWEKRI IELRECIQQG AGEDIAEAFR KAHEVRKFIN
//
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