ID   G0Z9K9_MALDO            Unreviewed;       377 AA.
AC   G0Z9K9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
DE   Flags: Fragment;
GN   Name=Adh1-2 {ECO:0000313|EMBL:AEL75218.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:AEL75218.1};
RN   [1] {ECO:0000313|EMBL:AEL75218.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zheng X.Y., Teng Y.W.;
RT   "Molecular evolution of Adh and LEAFY and the phylogenetic utility of their
RT   introns in Pyrus (Rosaceae).";
RL   Submitted (JAN-2011) 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   -!- 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; HQ912045; AEL75218.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0Z9K9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF40; ALCOHOL DEHYDROGENASE 2; 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          36..157
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          206..337
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
FT   NON_TER         377
FT                   /evidence="ECO:0000313|EMBL:AEL75218.1"
SQ   SEQUENCE   377 AA;  41061 MW;  3DE56E54A58D4D08 CRC64;
     MSNTAGQVIR CRAAVAWEAG KPLVIGEVEV APPQANEVRL KILFTSLCHT DVYFWEAKGQ
     NPLFPRIYGH EAGGIVESVG EGVTDLKAGD HVLPVFTGEC KDCAHCKSEE SNMCDLLRIN
     TDRGVMLNDG KSRFSIKGKP IYHFVGTSTF SEYTVVHVGC LAKINPSAPL DKVCVLSCGI
     STGLGATLNV AKPKKGSTVA VFGLGAVGLA AAEEARMSGA SRIIGVDLNS SRFEEAKKFG
     VTEFVNPKEH KKPVQEVIAE LTNGGVDRSI EYTGNVEAMI SAFECVHDGW GVAVLVGVPH
     KEAVFKTHPV NFLNERTLKG TFFGNYKPRT DIPSVVEKYM NKELELEKFI THRVPFSEIN
     KAFEYMLKGE GLRCIIH
//