ID   Q9SEQ3_9BRAS            Unreviewed;       379 AA.
AC   Q9SEQ3;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AAF23546.1};
OS   Boechera lyallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Boechereae; Boechera.
OX   NCBI_TaxID=81977 {ECO:0000313|EMBL:AAF23546.1};
RN   [1] {ECO:0000313|EMBL:AAF23546.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Koch M., Bernhard H., Mitchell-Olds T.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAF23546.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11018155;
RA   Koch M.A., Haubold B., Mitchell-Olds T.;
RT   "Comparative evolutionary analysis of chalcone synthase and alcohol
RT   dehydrogenase loci in Arabidopsis, Arabis, and related genera
RT   (Brassicaceae).";
RL   Mol. Biol. Evol. 17:1483-1498(2000).
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; AF110448; AAF23546.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9SEQ3; -.
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          35..162
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          205..335
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   379 AA;  41179 MW;  A6703D617CB3B1B5 CRC64;
     MSTTGQIIRC KAAVAWEAGK PLVMEEVEVA PPQKHEVRIK ILFTSLCHTD VYFWEAKGQT
     PLFPRIFGHE AGGIVESVGE GVTDLQPGDH VLPVFTGECG DCRHCHSEES NMCDLLRINT
     ERGVMIHDGE SRFSINGKPI HHFVGTSTFS EYTVVHSGQV AKINPDAPLD KVCIVSCGLS
     TGLGATLNVA KPKKGQSVAI FGLGAVGLAA AEGARIAGAS RVIGVDLNPK RFDEAKKFGV
     TEFVNPKDHD KPVQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK
     DDAFKSHPMN FLNERTLKGT FFGNYKPKTD IPGIVEMYMN KELELEKFIT HTVPFSEINK
     AFDYMLKGES IRCIITMGA
//