ID   DHA2_CUPNH              Reviewed;         506 AA.
AC   P46368; Q0JZT2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Acetaldehyde dehydrogenase 2;
DE            EC=1.2.1.3;
DE   AltName: Full=Acetaldehyde dehydrogenase II;
DE            Short=ACDH-II;
GN   Name=acoD; OrderedLocusNames=H16_B1960;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RX   PubMed=1732222; DOI=10.1128/jb.174.3.899-907.1992;
RA   Priefert H., Krueger N., Jendrossek D., Schmidt B., Steinbuechel A.;
RT   "Identification and molecular characterization of the gene coding for
RT   acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus.";
RL   J. Bacteriol. 174:899-907(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   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).
CC   -!- FUNCTION: Involved in the catabolism of acetoin and ethanol.
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   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2.
CC   -!- PATHWAY: Ketone degradation; acetoin degradation.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M74003; AAA21943.1; -; Genomic_DNA.
DR   EMBL; AM260480; CAJ96742.1; -; Genomic_DNA.
DR   PIR; A42597; A42597.
DR   RefSeq; WP_010812798.1; NZ_CP039288.1.
DR   AlphaFoldDB; P46368; -.
DR   SMR; P46368; -.
DR   STRING; 381666.H16_B1960; -.
DR   GeneID; 57647862; -.
DR   KEGG; reh:H16_B1960; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_4; -.
DR   OrthoDB; 6187633at2; -.
DR   UniPathway; UPA00040; -.
DR   UniPathway; UPA00780; UER00768.
DR   Proteomes; UP000008210; Chromosome 2.
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:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07116; ALDH_ACDHII-AcoD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Acetoin catabolism; Direct protein sequencing; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..506
FT                   /note="Acetaldehyde dehydrogenase 2"
FT                   /id="PRO_0000056566"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000250"
FT   BINDING         240..245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  54882 MW;  A8715BD93B126D4D CRC64;
     MNMAEIAQLG VSNPYKQQYE NYIGGAWVPP AGGEYFESTT PITGKPFTRV PRSGQQDVDA
     ALDAAHAAKA AWARTSTTER ANILNRIADR IEANLKLLAV AESIDNGKPV RETTAADLPL
     AVDHFRYFAG CIRAQEGGIS EIDADTIAYH FHEPLGVVGQ IIPWNFPLLM ATWKLAPALA
     AGNCVVLKPA EQTPASILVL MEVIGDLLPP GVVNVINGFG LEAGKPLASS PRISKVAFTG
     ETTTGRLIMQ YASQNLIPVT LELGGKSPNI FFEDVLAADD AFFDKALEGF AMFALNQGEV
     CTCPSRALIQ ESIYDRFMER ALKRVAAIRQ GHPLDTGTMI GAQASAEQLE KILSYIDLGR
     KEGAQCLTGG ERNVLDGDLA GGYYVKPTVF AGHNKMRIFQ EEIFGPVVSV TTFKDEEEAL
     AIANDTLYGL GAGVWTRDGA RAFRMGRGIQ AGRVWTNCYH AYPAHAAFGG YKQSGIGREN
     HRMMLDHYQQ TKNLLVSYSP NALGFF
//