ID   A0A430HYN1_9CORY        Unreviewed;       362 AA.
AC   A0A430HYN1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:RSZ63819.1};
GN   ORFNames=EAH68_06165 {ECO:0000313|EMBL:RSZ63819.1};
OS   Corynebacterium hylobatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1859290 {ECO:0000313|EMBL:RSZ63819.1, ECO:0000313|Proteomes:UP000274907};
RN   [1] {ECO:0000313|EMBL:RSZ63819.1, ECO:0000313|Proteomes:UP000274907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 101343 {ECO:0000313|EMBL:RSZ63819.1,
RC   ECO:0000313|Proteomes:UP000274907};
RA   Chen X.;
RT   "YIM 101343 draft genome.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSZ63819.1}.
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DR   EMBL; RXHJ01000006; RSZ63819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430HYN1; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000274907; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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          10..359
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  37745 MW;  88CBEE1976ABDDC1 CRC64;
     MKAAVVPSAG AGFEIVDVQI AAPEAKEVLI DVKAVGLCHS DYTLASADLG FPFPAVFGHE
     ISGVVREVGE NVTALRVGDP VVAALVRYCG ECERCLSGQS YYCRNVDFTL REKGQSPRLS
     VDGQGLTQAF GLGGFAEQAL VHENQLAKIP AGIPFENAAL LGCGVITGAG AVLNTAKVGR
     GETVAVIGAG GVGLNAISAA VLAGASRIVA LDISDEKLAK ASGFGATDTI NSLATDPVQA
     IHEIIPEGID HVFDFVGSER VAQQGLDMLS YGGALYLVGI GGADVTVTVN AMKFMRNRNR
     LESVYMGSAN LQVDIPFFAG LEARGLLRLD ELISETIALE DINDGYRRLK EGAVSRLVVV
     NP
//