ID   A0A162KQZ7_CORDF        Unreviewed;       441 AA.
AC   A0A162KQZ7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   SubName: Full=Alcohol dehydrogenase superfamily, zinc-type {ECO:0000313|EMBL:OAA78608.1};
GN   ORFNames=LEL_05431 {ECO:0000313|EMBL:OAA78608.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78608.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA78608.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78608.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAA78608.1}.
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DR   EMBL; AZHF01000003; OAA78608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162KQZ7; -.
DR   STRING; 1081108.A0A162KQZ7; -.
DR   OrthoDB; 2656459at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08276; MDR7; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR45033; -; 1.
DR   PANTHER; PTHR45033:SF1; OXIDOREDUCTASE (EUROFUNG); 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT   DOMAIN          42..424
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          333..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  46627 MW;  281011B438BE237B CRC64;
     MTIPTSIQHS GAAPVAAPEG IRRNWVHVTA PKNKQWTTAM DGVDKLKLAE ADLPTPNDGE
     VLVKIHAVSI NYRDIEGKPQ GLAPLVSNHL ANTGTVCEGV FNHYNTQASE AVVPCSDMCG
     TVVDASKSKS ARFQNGARVM AIYLQSHLYG DVDEEDLASS LGLPLPGVLA QYRCFPAESL
     VAVPDYLSDA EASCLPLATT TAWTALNWMR PLASTNEVRD GGPSRRTVLL QGTTPVALAG
     LQIAKAAGLR AVMTGSTDDF TARAKAELGA DEAINYQTHW AWEGEVLKAT DDRGADVIFE
     TGGGARTLQK SFKCVAFGGL INCIGSLSGR TDDGEDGDGG GGGGDGGDGK TPKLHRLNVT
     ALALARNVTI KGVLNGGRDR LEEALAFYQE KGIKPVVDKT YAFGKAPEAL AYVKKGKHFG
     KVVVTVEDEP DDKDGEKKPK A
//