ID   A0A1C1CGC0_9EURO        Unreviewed;       356 AA.
AC   A0A1C1CGC0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   Name=adh1 {ECO:0000313|EMBL:OCT47506.1};
GN   ORFNames=CLCR_03579 {ECO:0000313|EMBL:OCT47506.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT47506.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL   Submitted (JUL-2015) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:OCT47506.1}.
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DR   EMBL; LGRB01000013; OCT47506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1CGC0; -.
DR   STRING; 86049.A0A1C1CGC0; -.
DR   VEuPathDB; FungiDB:CLCR_03579; -.
DR   VEuPathDB; FungiDB:G647_01876; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   Proteomes; UP000094526; 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; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF3; ALCOHOL DEHYDROGENASE 1-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:UP000094526};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          18..350
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   356 AA;  38284 MW;  75CBAD733495E93A CRC64;
     MSYKIPTEQW AQVIDKVGGP LQYKKIPVAK PGPEEVLVNI KYSGVCHTDL HALNGDWPIP
     TKLPLVGGHE GAGIVVARGD LVTDEICKIG EAVGVKWLND SCLSCTFCQQ ADEPLCLTPK
     LSGYTVDGSF QQYCIASARH VAHIPEGVPL DEISPVLCAG ITVYKGLKES GARPGQTVAI
     VGAGGGLGTL AQQYAKAMGL HTIAIDSGDE KKALCQKMGS EHFIDFGKSS DIVKDVKNAT
     KDGLGPHAVI LVAVSEKPFQ QAAEYVRPRG TVIVIGLPAK AYIRAPVFES VLKMVRIQCS
     YVGNRQDSEE AIDFFARGLI KVPFKTVDLK DLPKVYEMMH AGQIAGRYVL KMPDAE
//