ID   O65293_9ROSI            Unreviewed;       228 AA.
AC   O65293;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Alcohol dehydrogenase D {ECO:0000313|EMBL:AAC14972.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:AAC14972.1};
DE   Flags: Fragment;
GN   Name=AdhD {ECO:0000313|EMBL:AAC14972.1};
OS   Gossypium marchantii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=47628 {ECO:0000313|EMBL:AAC14972.1};
RN   [1] {ECO:0000313|EMBL:AAC14972.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Seelanan T., Brubaker C.L., Stewart J.M., Craven L.A., Wendel J.F.;
RT   "Molecular systematics of Gossypium L. sect. Grandicalyx (Malvaceae).";
RL   Submitted (APR-1998) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF059393; AAC14972.1; -; Genomic_DNA.
DR   AlphaFoldDB; O65293; -.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF62; ALCOHOL DEHYDROGENASE 2; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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   ECO:0000313|EMBL:AAC14972.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          2..89
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          163..228
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC14972.1"
FT   NON_TER         228
FT                   /evidence="ECO:0000313|EMBL:AAC14972.1"
SQ   SEQUENCE   228 AA;  24163 MW;  DFBE6F380488C630 CRC64;
     FTSLCHTDVY FWEAKGQTPL FPRIFGHEAG GIVESVGEGV THLKPGDHVL PVFTGECGNC
     RHCKSKESNM CDLLRINTDR GVMLSDGKTR FSINGKPIYH FVGTSTFSEY TVAHVGSVAK
     INPAAPLDKV CILSCGISTG LGATLNVAKP AKGSTVAIFG LGAVGLAAAE GARIAGASRI
     IGVDLNPNRF EEAKKFGCTE FVNPKDHNKP VQEVLAEMTN GGVDRSVE
//