ID G2QES0_THET4 Unreviewed; 445 AA.
AC G2QES0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 10-JUN-2026, entry version 54.
DE RecName: Full=Prephenate dehydrogenase [NADP(+)] {ECO:0000256|PIRNR:PIRNR036510};
DE Short=PRDH {ECO:0000256|PIRNR:PIRNR036510};
DE EC=1.3.1.13 {ECO:0000256|PIRNR:PIRNR036510};
GN ORFNames=MYCTH_2304552 {ECO:0000313|EMBL:AEO57853.1};
OS Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729 {ECO:0000313|EMBL:AEO57853.1, ECO:0000313|Proteomes:UP000007322};
RN [1] {ECO:0000313|EMBL:AEO57853.1, ECO:0000313|Proteomes:UP000007322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799
RC {ECO:0000313|Proteomes:UP000007322};
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prephenate + NADP(+) = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADPH; Xref=Rhea:RHEA:21640, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00051295,
CC ECO:0000256|PIRNR:PIRNR036510};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00060605, ECO:0000256|PIRNR:PIRNR036510}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007964, ECO:0000256|PIRNR:PIRNR036510}.
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DR EMBL; CP003004; AEO57853.1; -; Genomic_DNA.
DR RefSeq; XP_003663098.1; XM_003663050.1.
DR AlphaFoldDB; G2QES0; -.
DR FunCoup; G2QES0; 217.
DR STRING; 573729.G2QES0; -.
DR GeneID; 11507724; -.
DR KEGG; mtm:MYCTH_2304552; -.
DR VEuPathDB; FungiDB:MYCTH_2304552; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; G2QES0; -.
DR OMA; WRVNACD; -.
DR OrthoDB; 5399569at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000007322; Chromosome 3.
DR GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006571; P:L-tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
DR FunFam; 1.10.3660.10:FF:000004; Prephenate dehydrogenase [NADP(+)]; 1.
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; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
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 Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF20463; PDH_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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR036510};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|PIRNR:PIRNR036510};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036510};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036510};
KW Reference proteome {ECO:0000313|Proteomes:UP000007322};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 10..291
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 445 AA; 49768 MW; 8C637C54E950F314 CRC64;
MAAFPGAEDF VVGLIGMGDM GKMYARRLSS AGWRIMACDR EDKYNELVAE FANHKNIQIL
RNGHLVSRAS NYIIYSVEAA AIGRVVAEYG PSTRLGAIVG GQTSCKDPEI KAFEEHLPSD
VDIVSCHSLH GPNVDPRGQP LVLIKHRASD ESFAKVEAVL RCLGSKHVYL SAAEHDRITA
DTQAVTHAAF LSMGKAWHAN QQFPWEGRRY VGGIENVKIN LMLRIYAQKW HVYAGLAILN
PEAHKQISQF ARSTTELFYL MLEGRRDELR ERVYAAKEKV FGREDCPKWG ERPLLPVGVL
DRFSLNADAN ATSNAPPMPN NHLSLLAMVD CWSALGIVPY DHMICSTPLF RLWLGVAEHL
FRTPGLLDES LRVGIEDTSF RRDDLQFTIA ASGWAECVAL RQFDTWRERF EVTQKFFEPR
FKGAIEMGQA MIKAVLESDK EGGSG
//
