ID A0A2T3Z0A6_9HYPO Unreviewed; 449 AA.
AC A0A2T3Z0A6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
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=M441DRAFT_60520 {ECO:0000313|EMBL:PTB38259.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB38259.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB38259.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB38259.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prephenate = 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|PIRNR:PIRNR036510};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC {ECO:0000256|PIRNR:PIRNR036510}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036510}.
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DR EMBL; KZ679266; PTB38259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3Z0A6; -.
DR STRING; 1042311.A0A2T3Z0A6; -.
DR OrthoDB; 1348131at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000240493; Unassembled WGS sequence.
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:tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR046825; PDH_C.
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; PF03807; F420_oxidored; 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|PIRNR:PIRNR036510};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036510};
KW NADP {ECO:0000256|PIRNR:PIRNR036510};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036510};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 16..297
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 449 AA; 50440 MW; FC0B8992EC330535 CRC64;
MASTPVASIP AGMENFTVGL IGMGDMGRMY AERLSEAGWR ILACDREDKY DSLKEKYNGK
KNIEILRNGH LVSRASDYII YSVEAAFIDR VIAQYGPSTK MGAIVGGQTS CKSPEIAAFE
AHLPSDVYIL SCHSLHGPGV DPKGQPLVLI QHRAPDEALH KVEAVLSCLQ SKFVYLSAKE
HDRITADTQA VTHAAFLSMG KAWHANAQYP WELSRYIGGL ENVKMNIMLR IYSQKWHVYA
GLAILNPEAR DQVAQYAKSV TELYKLMLEG NLEGLKARIY AARDKVFGPS KTWANRPLLE
ASILTSFSLG TLTAETPARP NNHLSLLAMV DCWAELGIVP YDHMLCSTPL FRLRLGVTEH
LFRNTEMLDE TLRTATEDKR YRSDDLEFTF AARGWAECVT LGHFETWEKR FVSTQEFFQP
RFADAKKVGD EMMKKVQASM DENLKLDEK
//
