ADHQ_RABIT
ID ADHQ_RABIT Reviewed; 379 AA.
AC O46650;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Alcohol dehydrogenase class-2 isozyme 2;
DE EC=1.1.1.1;
GN Name=ADH2-2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=9492289; DOI=10.1046/j.1432-1327.1998.2510236.x;
RA Svensson S., Hedberg J., Hoeoeg J.-O.;
RT "Structural and functional divergence of class II alcohol dehydrogenase
RT -- cloning and characterisation of rabbit liver isoforms of the enzyme.";
RL Eur. J. Biochem. 251:236-243(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-II subfamily. {ECO:0000305}.
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DR EMBL; AJ002389; CAA05363.1; -; mRNA.
DR RefSeq; NP_001171758.1; NM_001184829.1.
DR AlphaFoldDB; O46650; -.
DR SMR; O46650; -.
DR STRING; 9986.ENSOCUP00000021279; -.
DR GeneID; 100345521; -.
DR KEGG; ocu:100345521; -.
DR CTD; 100345521; -.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; O46650; -.
DR OMA; CIGCATI; -.
DR OrthoDB; 664798at2759; -.
DR TreeFam; TF300429; -.
DR Proteomes; UP000001811; Unplaced.
DR ExpressionAtlas; O46650; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IEA:InterPro.
DR GO; GO:0035276; F:ethanol binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR028632; Zinc_ADH_II.
DR PANTHER; PTHR43880:SF14; PTHR43880:SF14; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..379
FT /note="Alcohol dehydrogenase class-2 isozyme 2"
FT /id="PRO_0000160685"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 205..210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 40497 MW; A650C7DEA2337777 CRC64;
MSTKGKVIKC KAAIAWEAGK PLSIEEVEVA PPKAHEVRVQ IIAASVCRSD TYVINPAFKE
GLLPVILGHE CAGIVESVGP GVNNFKPGDK VIPLYVPHCR KCKFCQSPLT NFCTKFSEHK
NPIIEQELMD DKTSRFTCKG KSIYHFLGIS AFSQYTVVKD INLAKIDDDA NLKRVCLIGC
GFSTGYGAAI NDAKVTPGST CAVFGLGGVG LSAVIGCKTA GASRIIAVDI NSDKFAKAKA
LGATDCLNPR ELNKPVQDVI VEMTNGGVDF AIDCAGGSEV MKATVDCTTV GWGSCTFVGV
NVNDKGLTIS PVELILGRTL RGSSFGGWDV DTVPKLVSDY KNGKFNLEAL VTHTLPFEKI
NEALDLLKQG KSIRTILIY
