ID   O49114_LEACR            Unreviewed;       322 AA.
AC   O49114;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   SubName: Full=Alcohol dehydrogenase 1 {ECO:0000313|EMBL:AAC79421.1};
DE   Flags: Fragment;
GN   Name=Adh1 {ECO:0000313|EMBL:AAC79421.1};
OS   Leavenworthia crassa (Fleshy-fruit glade-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Leavenworthia.
OX   NCBI_TaxID=70805 {ECO:0000313|EMBL:AAC79421.1};
RN   [1] {ECO:0000313|EMBL:AAC79421.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:AAC79421.1};
RA   Liu F.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAC79421.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:AAC79421.1};
RX   PubMed=9580984;
RA   Charlesworth D., Liu F.L., Zhang L.;
RT   "The evolution of the alcohol dehydrogenase gene family by loss of introns
RT   in plants of the genus Leavenworthia (Brassicaceae).";
RL   Mol. Biol. Evol. 15:552-559(1998).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; AF037563; AAC79421.1; -; Genomic_DNA.
DR   AlphaFoldDB; O49114; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08301; alcohol_DH_plants; 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   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF26; ALCOHOL DEHYDROGENASE CLASS-P; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
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          6..105
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          148..279
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC79421.1"
SQ   SEQUENCE   322 AA;  34634 MW;  8DDFE55373CA384A CRC64;
     GQTPLFPRIF GHEAGGIVES VGEGVTDLQP GDHVLPIFTG ECGDCPHCHS EESNMCDLLR
     INTDRVGMIH DGESRFSIKG KPIHHFLGTS TFSEYTVVHS GQVAKINPEA PLDKVCIVSC
     GLSTGLGATL NVAKPKKGQS VAVFGLGAVG LGAAEGARIA GASRIIGVDL NSNRFEQAKK
     FGVTEFVNPK EHDKPVQQVI AEMTNGGVDR SVECTGSVQA MIQAFECVHD GWGVAVLVGV
     PSKDDAFKTH PMNFLNERTL KGTFFGNYKP KTDIPGVVEK YMNKELELEK FITHTVPFSE
     INKAFDYMLN GEGIRCIITM GA
//