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Database: UniProt
Entry: Q9SER7_ARABL
LinkDB: Q9SER7_ARABL
Original site: Q9SER7_ARABL 
ID   Q9SER7_ARABL            Unreviewed;       379 AA.
AC   Q9SER7;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AAF23529.1};
OS   Arabis blepharophylla (Coast rock-cress) (Erysimum blepharophyllum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=81973 {ECO:0000313|EMBL:AAF23529.1};
RN   [1] {ECO:0000313|EMBL:AAF23529.1}
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:AAF23529.1}
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; AF110431; AAF23529.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9SER7; -.
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..161
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;  41129 MW;  0B5D2ED166683CC0 CRC64;
     MITTGQIIRC KAAVAWEAGK PLVMEEVEVA PPQKHEVRIK ILFTSLCHTD VYFWEAKGQT
     PLFPRIFGHE AGGIVESVGE GVTDLAPGDH VLPIFTGECG DCPHCHSEES NMCDLLRINT
     ERGGMIHDGE SRFSIDGKPI YHFVGTSTFS EYTVIHSGQV AKINPDAPLD KVCIVSCGLS
     TGLGATLNVA KPKKGQSVAI FGLGAVGLAA AEGARIAGAS RIIGVDLNSK RFDEAKKFGV
     TEFVNPKDHD KPVQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK
     DDAFKTHPMN FLNERTLKGT FFGNYKPKTD IPGVVEQYMN KELEIEKFIT HTVPFSEINK
     AFDYMLKGEG NRCIIRMGA
//
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