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Database: UniProt
Entry: Q9SEQ7_ARAHI
LinkDB: Q9SEQ7_ARAHI
Original site: Q9SEQ7_ARAHI 
ID   Q9SEQ7_ARAHI            Unreviewed;       379 AA.
AC   Q9SEQ7;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AAF23542.1};
OS   Arabis hirsuta (Hairy rock-cress) (Turritis hirsuta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=78191 {ECO:0000313|EMBL:AAF23542.1};
RN   [1] {ECO:0000313|EMBL:AAF23542.1}
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:AAF23542.1}
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; AF110444; AAF23542.1; -; Genomic_DNA.
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..336
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   379 AA;  41042 MW;  5147DF1652A3BDA4 CRC64;
     MITTGQIIRC KAAVAFEAGK PLVMEEVEVA PPQKNEVRIK ILFTSLCHTD VYFWEAKGQT
     PLFPRIFGHE AGGIVESVGE GVTDLAPGDH VLPIFTGECG DCPHCHSEES NMCDLLRINT
     ERGVMINDGE SRFSIDGKPI YHFVGTSTFS EYTVVHSGQV AKINPDAPLD KVCIVSCGLS
     TGXGATLNVA KPKKGQSVAI FGLGAVGLAA AEGARIAGAS RIIGVDLNSK RFDEAKKFGV
     TEFVNPKDHD KPVQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK
     DDAYKTHPMN FLNERTLKGT FFGNYKPKTD IPGLVEKYMN KELEIEKFIT HTVPFSEINR
     AFDYMLKGEG IXCKITMGA
//
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