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
//