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Database: UniProt
Entry: G0RJV5_HYPJQ
LinkDB: G0RJV5_HYPJQ
Original site: G0RJV5_HYPJQ 
ID   G0RJV5_HYPJQ            Unreviewed;       450 AA.
AC   G0RJV5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-FEB-2025, entry version 42.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR48661.1};
GN   ORFNames=TRIREDRAFT_62034 {ECO:0000313|EMBL:EGR48661.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR48661.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR48661.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; GL985064; EGR48661.1; -; Genomic_DNA.
DR   RefSeq; XP_006965399.1; XM_006965337.1.
DR   AlphaFoldDB; G0RJV5; -.
DR   STRING; 431241.G0RJV5; -.
DR   EnsemblFungi; EGR48661; EGR48661; TRIREDRAFT_62034.
DR   GeneID; 18486853; -.
DR   KEGG; tre:TRIREDRAFT_62034; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_62034; -.
DR   eggNOG; ENOG502QPT5; Eukaryota.
DR   HOGENOM; CLU_031468_9_0_1; -.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT   DOMAIN          59..231
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          269..402
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   450 AA;  49238 MW;  33649BA6F2796279 CRC64;
     MAAYSTQSRQ PAWLTSLLSN TSPAPKLYAW SPDNLRGSVP SSLSPSADQP DPSDLDRRIF
     ILGIGNLGRL YASCLSMHSP RPPITLVVHK QELLAQWIHG PGLEITRSGR LYRGKDEFQI
     ELWTEQAPTH GPVREVAHAN KIRNLIVATK ASAAMTEADR LRRYLDSSSS VTFLQNGMSK
     LWPPYGQKYV AQRYPDNDAP NFLACVTNHG VLSEGPFKSL HASPADSAVG PVLLNNTARP
     LAPSVAYLTD AIASAPCLNS RSLTRAELWA SQLQKLVVNS TINPLTAVLR CKNGALFENS
     NGIVAKVIVR LLHESSAILQ TLINHPIATE ILAASSDVKP GKSLEAVREE LSLRFSFAEL
     HSMLYNIGQV VKDNTSSMLQ DVRAGKPTEI HDFNGWLVET ADFLEQSSIG QPRELDVSCH
     RTLIAMVESG TIVDDTELAK QLLPGMSHTW
//
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