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Database: UniProt
Entry: B8NIZ8_ASPFN
LinkDB: B8NIZ8_ASPFN
Original site: B8NIZ8_ASPFN 
ID   B8NIZ8_ASPFN            Unreviewed;       364 AA.
AC   B8NIZ8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=Alcohol dehydrogenase, putative {ECO:0000313|EMBL:EED50293.1};
GN   ORFNames=AFLA_071150 {ECO:0000313|EMBL:EED50293.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED50293.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED50293.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; EQ963479; EED50293.1; -; Genomic_DNA.
DR   RefSeq; XP_002380674.1; XM_002380633.1.
DR   AlphaFoldDB; B8NIZ8; -.
DR   STRING; 332952.B8NIZ8; -.
DR   EnsemblFungi; EED50293; EED50293; AFLA_071150.
DR   VEuPathDB; FungiDB:AFLA_009058; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OMA; IVDQKFV; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd05283; CAD1; 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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF3; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01980)-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.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          16..354
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   364 AA;  39001 MW;  9EA742A900CBF3AF CRC64;
     MSSTTPDTFK GWVANNATSP LTFTTFHPKP FTETDIEVAI SHCGICGTDI HTLRSGWGPA
     DYPCVVGHEI IGTVTRIGSE VPTLASSPAS REIRIGDRVG IGAQSMSCLK ADSLNAQTDR
     RTTVPDSRGR TTRAYGGFAM RWRGPAHFAF KIPGSLPSAE AAPLLCGGVT VFAPLRKYGA
     GPGKSVGIVG IGGLGHLGIL FARALGCDRV VGISRTSSKR KDAIEGLGAD AFIATDEEKK
     WGRMHSRSLD LIICTVDAPD MPLSQYLRLL KVDGTFVQVG APEKPLPQLT AFSLIQKGVK
     VTGSNVGSPE DIRLMLQLAA EKRVLPWIQK RPMEDVNAAL ADMDAGKARY RYVLVNETEK
     QAKL
//
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