ID Q9SER2_9BRAS Unreviewed; 379 AA.
AC Q9SER2;
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:AAF23536.1};
OS Boechera fendleri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Boechereae; Boechera.
OX NCBI_TaxID=81974 {ECO:0000313|EMBL:AAF23536.1};
RN [1] {ECO:0000313|EMBL:AAF23536.1}
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:AAF23536.1}
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; AF110438; AAF23536.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9SER2; -.
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; 41248 MW; BA8A0E68967E645A CRC64;
MITTGQIIRC KAAVAWEAGK PLVMEEVEVA PPQKHEVRIK ILFTSLCHTD VYFWEAKGQT
PRFPRIFGHE 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
//