ID ACDH_METSB Reviewed; 313 AA. AC B8ESV1; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657}; GN OrderedLocusNames=Msil_1478; OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB OS 13906 / BL2). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Beijerinckiaceae; Methylocella. OX NCBI_TaxID=395965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2; RX PubMed=20472789; DOI=10.1128/jb.00506-10; RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B., RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.; RT "Complete genome sequence of the aerobic facultative methanotroph RT Methylocella silvestris BL2."; RL J. Bacteriol. 192:3840-3841(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001280; ACK50436.1; -; Genomic_DNA. DR RefSeq; WP_012590506.1; NC_011666.1. DR AlphaFoldDB; B8ESV1; -. DR SMR; B8ESV1; -. DR STRING; 395965.Msil_1478; -. DR KEGG; msl:Msil_1478; -. DR eggNOG; COG4569; Bacteria. DR HOGENOM; CLU_062208_0_0_5; -. DR OrthoDB; 9786743at2; -. DR Proteomes; UP000002257; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR03215; ac_ald_DH_ac; 1. 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..313 FT /note="Acetaldehyde dehydrogenase" FT /id="PRO_0000387668" FT ACT_SITE 129 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 11..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" 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 288 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 313 AA; 33150 MW; F584D180AB1C417D CRC64; MEKIPCAIIG SGNIGTDLMI KIMRMSKHLE MGAMVGIDPK SDGLARAARL GVPVTHEGID GLRKLPNYGD IQIVFDATSA GAHVHNNAIL QKDGKKVIDL TPAAIGPFTI PAINGDANID EPNINMVTCG GQATIPMVRA VRRATDRVIW GEIVASISSK SAGPGTRANI DEFTETTSKA IEILGGAEHG KAIIILNPAE PPLIMRDTVF TLSQGGSRES IEQSILDMVA AVQKYVPGYR LKQKVQFENI GDNAPVRIPG VGLCSGLKTT IMLEVEGAAH YLPAYAGNLD IMTSAALVSA DHWAAKQLQK EAA //