ID J0WTY9_AURST Unreviewed; 459 AA.
AC J0WTY9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 10-JUN-2026, entry version 52.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:EJD37025.1};
GN ORFNames=AURDEDRAFT_116964 {ECO:0000313|EMBL:EJD37025.1};
OS Auricularia subglabra (strain TFB-10046 / SS5) (White-rot fungus)
OS (Auricularia delicata (strain TFB10046)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Auriculariaceae; Auricularia.
OX NCBI_TaxID=717982 {ECO:0000313|EMBL:EJD37025.1, ECO:0000313|Proteomes:UP000006514};
RN [1] {ECO:0000313|Proteomes:UP000006514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFB10046 {ECO:0000313|Proteomes:UP000006514};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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DR EMBL; JH687849; EJD37025.1; -; Genomic_DNA.
DR AlphaFoldDB; J0WTY9; -.
DR FunCoup; J0WTY9; 14.
DR KEGG; adl:AURDEDRAFT_116964; -.
DR eggNOG; KOG2380; Eukaryota.
DR InParanoid; J0WTY9; -.
DR OMA; WRVNACD; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000006514; 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:UP000006514}.
FT DOMAIN 23..307
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 459 AA; 50372 MW; 2E4FB0C3B6F1E70F CRC64;
MNATLALYTM RAPSPNDPVE QHPVIGLIGM GEMGRMYAHR LSAAGWRRIH VCDLPQNAEK
LSRDMQGVPG VTAHVDGHGV ARIADVLLYN VEAEHIARVV AQFGPSTRVG AIVGGQTSVK
APERDAFEKY LPEDTHIVSV HSLHGPTVNP EGQPLVIITH RAPDWATNVV EAILTPLRSR
HIRLTYDEHD LVTANTQAVT HAAFLSMGTA WSSQGEYPWE GGAGLFVGGI ETVKVNIAIR
IYSNKWHVYA GLAILNPIAR SQIAQFARSS TELFQLMISG AEDALRERVH RARHAVFGPG
SATPDVAAVP LLQEDVLDQF QLGNANSNGR RTSLKMAPEN SHLSLLAMVD CWAALNINPF
AHLAVAATPI FRLWIGIAQT LFLNEPRLER AIVAAVRDVT YRANDLEFVV AARGWAQCVA
HGSFELYERR FAETAQFFEP RFEEATRVGG SMIRAVMEK
//