ID   A0A0C2SVP5_AMAMK        Unreviewed;       500 AA.
AC   A0A0C2SVP5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   10-JUN-2026, entry version 31.
DE   RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN   ORFNames=M378DRAFT_15770 {ECO:0000313|EMBL:KIL58149.1};
OS   Amanita muscaria (strain Koide BX008).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX   NCBI_TaxID=946122 {ECO:0000313|EMBL:KIL58149.1, ECO:0000313|Proteomes:UP000054549};
RN   [1] {ECO:0000313|EMBL:KIL58149.1, ECO:0000313|Proteomes:UP000054549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Koide BX008 {ECO:0000313|EMBL:KIL58149.1,
RC   ECO:0000313|Proteomes:UP000054549};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN818346; KIL58149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2SVP5; -.
DR   FunCoup; A0A0C2SVP5; 101.
DR   STRING; 946122.A0A0C2SVP5; -.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   InParanoid; A0A0C2SVP5; -.
DR   OrthoDB; 5399569at2759; -.
DR   Proteomes; UP000054549; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
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:L-tyrosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 2.
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; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR050812; Preph/Arog_dehydrog.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF27505; 6PGD_Tyr1_C; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000054549}.
FT   DOMAIN          21..321
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   500 AA;  55309 MW;  CD4291C405AAB4CA CRC64;
     MSTLSIQDPA AGPAHPTHAQ PTIGLIGMGA MGRMYARVLS SAGWKKIYVC DIPSKYDGLK
     REYADSPGIK VFQDGHAVSR ASDFIVYSVE AEHIDDVVKQ FGPCASLSLI SHPSPTNYSS
     ATKLHAVVAG QTSVKAPERD AFEKHLPQDV HIVSCHSLHG PNVSPVGQPL VIIKHRGPTE
     ALTLVENILR CFRSRYVYLS YEDHDRVTAN TQAVTHAAFL SMGTAWAASQ SYPWEQGLYV
     GGLETAKVNL TLRIYSNQWH VYAGLAILNP SARVQIDQYA KSATELFKLM LAGGNGTEED
     KKAFGARVEW GGKVIFGSGG EKKKRRPILL SEDVLDRFSL GKFNHLGSNN NDTQGGTIPP
     TRYRPNSHLS LLAMVDSWAH LIINPYIHLS LAATPLFRLF LGVAEHLFLS PELLSTSIHS
     ALHDTWHRAD DLEFVIAARG WSEAVSLGNF EGYKWRFERT KRFLDSRFEE GVRVGTEMIK
     ALMETEVERE KEEEGEGAQE
//