ACDH1_CUPMC
ID ACDH1_CUPMC Reviewed; 303 AA.
AC Q1LNS3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Acetaldehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 1 {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=Rmet_1320;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01657};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01657}.
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DR EMBL; CP000352; ABF08203.1; -; Genomic_DNA.
DR RefSeq; WP_011516086.1; NC_007973.1.
DR AlphaFoldDB; Q1LNS3; -.
DR SMR; Q1LNS3; -.
DR STRING; 266264.Rmet_1320; -.
DR EnsemblBacteria; ABF08203; ABF08203; Rmet_1320.
DR KEGG; rme:Rmet_1320; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_4; -.
DR OMA; LMMRDTI; -.
DR OrthoDB; 1432332at2; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01657; Ac_ald_DH_ac; 1.
DR InterPro; IPR003361; Acetaldehyde_dehydrogenase.
DR InterPro; IPR015426; Acetylaldehyde_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR Pfam; PF09290; AcetDehyd-dimer; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR PIRSF; PIRSF015689; Actaldh_dh_actl; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..303
FT /note="Acetaldehyde dehydrogenase 1"
FT /id="PRO_0000387714"
FT ACT_SITE 130
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 161..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 303 AA; 32332 MW; EF590C5280B84A9F CRC64;
MKKIKCALIG PGNIGTDLLA KLKRSSVLEP VWMVGIDPES EGLNRARELG IKTTAEGVDG
LLPHVLADGV QIAFDATSAY VHAENARKLN ALGVMMIDLT PAAIGPYCVP PVNLKEHLGK
REMNVNMVTC GGQATIPMVA AVSRVQPVAY GEIVATVSSR SVGPGTRKNI DEFTRTTAGA
VEKVGGARKG KAIIIINPAE PPLMMRDTIH CLTETEPDQQ RIAESIHAMI EEVQKYVPGY
RLVNGPVFDG KRVTVFMEVA GLGDYLPTYA GNLDIMTAAA ARTAEMFAEE MIAGNLTLEP
VVA
