ADH_CUPNE
ID ADH_CUPNE Reviewed; 366 AA.
AC P14940;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:Q0KDL6};
DE EC=1.1.1.4 {ECO:0000250|UniProtKB:Q0KDL6};
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:Q0KDL6};
GN Name=adh;
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2846513; DOI=10.1128/jb.170.11.5248-5256.1988;
RA Jendrossek D., Steinbuechel A., Schlegel H.G.;
RT "Alcohol dehydrogenase gene from Alcaligenes eutrophus: subcloning,
RT heterologous expression in Escherichia coli, sequencing, and location of
RT Tn5 insertions.";
RL J. Bacteriol. 170:5248-5256(1988).
CC -!- FUNCTION: Multifunctional alcohol dehydrogenase exhibiting NAD(+)-
CC dependent dehydrogenase activities for 2,3-butanediol, ethanol and
CC acetaldehyde, and reductase activities for acetoin (NADH-dependent),
CC and diacetyl and acetaldehyde (independently of whether NADH or NADPH
CC is the reductant). The rate of oxidation of 2,3-butanediol is much
CC higher than for the oxidation of ethanol. Has acetaldehyde
CC dehydrogenase activity leading to acetate formation. May function in
CC the release of excess reducing power in the absence of exogenous
CC hydrogen acceptors such as oxygen. {ECO:0000250|UniProtKB:Q0KDL6}.
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 Evidence={ECO:0000250|UniProtKB:Q0KDL6};
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 Evidence={ECO:0000250|UniProtKB:Q0KDL6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH;
CC Xref=Rhea:RHEA:24340, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC ChEBI:CHEBI:16982, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:Q0KDL6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q0KDL6};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; J03362; AAA21953.1; -; Genomic_DNA.
DR PIR; A30196; A30196.
DR AlphaFoldDB; P14940; -.
DR SMR; P14940; -.
DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; 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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..366
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000160747"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 38566 MW; 6F531C8D7FEA874B CRC64;
MTAMMKAAVF VEPGRIELAD KPIPDIGPND ALVRITTTTI CGTDVHILKG EYPVAKGLTV
GHEPVGIIEK LGSAVTGYRE GQRVIAGAIC PNFNSYAAQD GVASQDGSYL MASGQCGCHG
YKATAGWRFG NMIDGTQAEY VLVPDAQANL TPIPDGLTDE QVLMCPDIMS TGFKGAENAN
IRIGHTVAVF AQGPIGLCAT AGARLCGATT IIAIDGNDHR LEIARKMGAD VVLNFRNCDV
VDEVMKLTGG RGVDASIEAL GTQATFEQSL RVLKPGGTLS SLGVYSSDLT IPLSAFAAGL
GDHKINTALC PGGKERMRRL INVIESGRVD LGALVTHQYR LDDIVAAYDL FANQRDGVLK
IAIKPH
