ID A0A395H966_9EURO Unreviewed; 389 AA.
AC A0A395H966;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:RAL03705.1};
GN ORFNames=BO80DRAFT_487348 {ECO:0000313|EMBL:RAL03705.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL03705.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL03705.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL03705.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC 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; KZ824426; RAL03705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395H966; -.
DR STRING; 1448316.A0A395H966; -.
DR VEuPathDB; FungiDB:BO80DRAFT_487348; -.
DR OrthoDB; 2619844at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-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 Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 22..387
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 389 AA; 41077 MW; 429EED07903F3C66 CRC64;
MANIPPTVTG RALVSHSPYK TGGWKLQNVS LRPLRENELL VEVVASGVCQ TDLHFAGLET
GLGVNYPRVM GHEGAGYVRQ IGPNVTAARV NDPILMSFSS CQTCEGCRRG HPAHCHIFDP
INFEATRENY VFRGENQDGS GEADIYGQFF GQSSFASWTI VQEQAVVNVS GLVEGKEELQ
LLAPLGCGIQ TGAGAVINAA GAKGEDTVAV LGLGGVGLSA VMGARIAGCK TIIGIARNEA
RLELALAVGA THVVRIDSNA DLSAVTEGVR AITKGIGADI TLETTGAPGL VAEGIRMTAN
KGRVVQLGSA PENAVLNLPI HEFMVAGKQY MGVVEGDVVP REFVPKMIDW VKAGLLPLRK
MVGFYQAGDF ETALSDMRSG KTIKPVLVW
//
