ADH_CUPNH
ID ADH_CUPNH Reviewed; 366 AA.
AC Q0KDL6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1 {ECO:0000269|PubMed:2144274, ECO:0000269|PubMed:6378632};
DE EC=1.1.1.4 {ECO:0000269|PubMed:2144274, ECO:0000269|PubMed:6378632};
DE EC=1.2.1.3 {ECO:0000269|PubMed:2144274, ECO:0000269|PubMed:6378632};
GN Name=adh; OrderedLocusNames=H16_A0757;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [2]
RP PROTEIN SEQUENCE OF 2-33, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=2144274; DOI=10.1128/jb.172.9.4844-4851.1990;
RA Jendrossek D., Kruger N., Steinbuchel A.;
RT "Characterization of alcohol dehydrogenase genes of derepressible wild-type
RT Alcaligenes eutrophus H16 and constitutive mutants.";
RL J. Bacteriol. 172:4844-4851(1990).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP SUBUNIT.
RC STRAIN=N9A / DSM 518;
RX PubMed=6378632; DOI=10.1111/j.1432-1033.1984.tb08229.x;
RA Steinbuchel A., Schlegel H.G.;
RT "A multifunctional fermentative alcohol dehydrogenase from the strict
RT aerobe Alcaligenes eutrophus: purification and properties.";
RL Eur. J. Biochem. 141:555-564(1984).
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:0000269|PubMed:2144274,
CC ECO:0000269|PubMed:6378632}.
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:0000269|PubMed:2144274, ECO:0000269|PubMed:6378632};
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:0000269|PubMed:2144274, ECO:0000269|PubMed:6378632};
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:0000269|PubMed:2144274, ECO:0000269|PubMed:6378632};
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; Evidence={ECO:0000269|PubMed:2144274,
CC ECO:0000269|PubMed:6378632};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.67 mM for acetaldehyde (with NADH as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.69 mM for acetaldehyde (with NADPH as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.56 mM for acetoin (with NADH as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=1.42 mM for acetoin (with NADPH as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.56 mM for diacetyl (with NADH as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=1.10 mM for diacetyl (with NADPH as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=18.2 mM for erythro-2,3-butanediol (with NAD as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=5.00 mM for ethanol (with NAD as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=22.2 mM for threo-2,3-butanediol(with NAD as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.011 mM for NADH (with acetaldehyde as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.012 mM for NADH (with acetoin as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.011 mM for NADH (with diacetyl as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.009 mM for NAD (with ethanol as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.138 mM for NAD (with erythro-2,3-butanediol as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.145 mM for NAD (with threo-2,3-butanediol as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.053 mM for NADPH (with acetaldehyde as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.047 mM for NADPH (with acetoin as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC KM=0.050 mM for NADPH (with diacetyl as cosubstrate)
CC {ECO:0000269|PubMed:6378632};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:6378632}.
CC -!- INDUCTION: By limited oxygen supply. {ECO:0000269|PubMed:6378632}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AM260479; CAJ91905.1; -; Genomic_DNA.
DR RefSeq; WP_010812995.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0KDL6; -.
DR SMR; Q0KDL6; -.
DR STRING; 381666.H16_A0757; -.
DR EnsemblBacteria; CAJ91905; CAJ91905; H16_A0757.
DR GeneID; 57642855; -.
DR KEGG; reh:H16_A0757; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_4; -.
DR OMA; CENCEKG; -.
DR OrthoDB; 787596at2; -.
DR SABIO-RK; Q0KDL6; -.
DR Proteomes; UP000008210; Chromosome 1.
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 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2144274"
FT CHAIN 2..366
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000429032"
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; 38544 MW; F414508D73EFAAF8 CRC64;
MTAMMKAAVF VEPGRIELAD KPIPDIGPND ALVRITTTTI CGTDVHILKG EYPVAKGLTV
GHEPVGIIEK LGSAVTGYRE GQRVIAGAIC PNFNSYAAQD GVASQDGSYL MASGQCGCHG
YKATAGWRFG NMIDGTQAEY VLVPDAQANL TPIPDGLTDE QVLMCPDIMS TGFKGAENAN
IRIGDTVAVF AQGPIGLCAT AGARLCGATT IIAIDGNDHR LEIARKMGAD VVLNFRNCDV
VDEVMKLTGG RGVDASIEAL GTQATFEQSL RVLKPGGTLS SLGVYSSDLT IPLSAFAAGL
GDHKINTALC PGGKERMRRL INVIESGRVD LGALVTHQYR LDDIVAAYDL FANQRDGVLK
IAIKPH
