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Database: UniProt
Entry: G3JQ80_CORMM
LinkDB: G3JQ80_CORMM
Original site: G3JQ80_CORMM 
ID   G3JQ80_CORMM            Unreviewed;       331 AA.
AC   G3JQ80;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:EGX89331.1};
GN   ORFNames=CCM_07582 {ECO:0000313|EMBL:EGX89331.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX89331.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX89331.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX89331.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; JH126404; EGX89331.1; -; Genomic_DNA.
DR   RefSeq; XP_006672786.1; XM_006672723.1.
DR   AlphaFoldDB; G3JQ80; -.
DR   STRING; 983644.G3JQ80; -.
DR   GeneID; 18169593; -.
DR   KEGG; cmt:CCM_07582; -.
DR   VEuPathDB; FungiDB:CCM_07582; -.
DR   eggNOG; KOG1197; Eukaryota.
DR   HOGENOM; CLU_026673_3_1_1; -.
DR   InParanoid; G3JQ80; -.
DR   OMA; KGMTAHY; -.
DR   OrthoDB; 148501at2759; -.
DR   Proteomes; UP000001610; Unassembled WGS sequence.
DR   GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:InterPro.
DR   CDD; cd05286; QOR2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047618; QOR-like.
DR   PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1.
DR   PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN          17..328
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   331 AA;  34939 MW;  4A51E59723E06938 CRC64;
     MAPVPATMKA VSIAKNGGPE VLQYTDVPVP QPQPDEILVR NRMAGVNFID TYFRSGQYPS
     PAFPRILGQD GAGEVVAVGS AVAVPHAVGS TVVYMNGTGT YAEYSTVKAT SAIAVPAGVT
     VEDAVAVYLQ GLTAWTFIRR AGLTQAGEWA FVHAAAGGVG SLLVQLLKGL GAKVIATASS
     EEKLKIVKDL GADHVINSND DWVAKVNEIT GGHGADSIYD GVGKATFHKD LEIIAVGGSL
     VMLGNASGNV EPFDIRSTLG PKNVRLSRPI VFAYIKEHEA LEKYAGEVFE FVRSGKLKVL
     QHGTYDLKDV AKAHADIESR KTVGKLLIKI S
//
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