ID S8DQ35_FOMSC Unreviewed; 468 AA.
AC S8DQ35;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 10-JUN-2026, entry version 47.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=FOMPIDRAFT_1063037 {ECO:0000313|EMBL:EPS94777.1};
OS Fomitopsis schrenkii (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fomitopsis.
OX NCBI_TaxID=2126942 {ECO:0000313|EMBL:EPS94777.1, ECO:0000313|Proteomes:UP000015241};
RN [1] {ECO:0000313|EMBL:EPS94777.1, ECO:0000313|Proteomes:UP000015241}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FP-58527 {ECO:0000313|Proteomes:UP000015241};
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; KE504223; EPS94777.1; -; Genomic_DNA.
DR AlphaFoldDB; S8DQ35; -.
DR FunCoup; S8DQ35; 95.
DR STRING; 743788.S8DQ35; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; S8DQ35; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000015241; 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 FunFam; 3.40.50.720:FF:000339; Prephenate dehydrogenase [NADP(+)]; 1.
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; IPR050812; Preph/Arog_dehydrog.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR012385; Prephenate_DH_fun.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF27505; 6PGD_Tyr1_C; 1.
DR PIRSF; PIRSF036510; PDH_fung; 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:UP000015241}.
FT DOMAIN 16..298
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 468 AA; 52241 MW; A602E8BB74EF13FD CRC64;
MINPDVTPDS PIDEQPAIGI IGMGSMGTMY AKFLCEGGWK KIYVCDQPTK YETLKTKYED
NPNVHVLVDG HQVSRISDFI MYSVEAEYIE RVVSTYGPST KVGAIVSGQT SVKAPEKIAF
EKYLPPDVHI VSCHSLHGPT VSPLGQPLVI IKHRAPEWAV RLVENILRPL RSRYVYLSYE
DHDIVTANTQ AVTHAAFLSM GTAWANEKEY PWETGHAVGG IETVKVNIML RIYSNKWHVY
AGLAILNPSA KIQIDQFARS TTEIYKLMIS GDDAGMRRRI YDARDKVFGT KARDGSVTTR
APILLSEDIL DRFSLWRHRR GSAATSVGQD IAENGEAPPN THLANSHLSL LAMVDCWAAL
GIQPFVHLDL AATPLFRMLL GVSEYLFRSQ ARLDHAIHAA LYDTTYRAND LEFVVAARGW
SQCISFGSFE LYKDRFTETC KFFEPRFEDA TKLGSAMLQA ILESSPSS
//