ID ACDH3_AZOVD Reviewed; 304 AA. AC C1DN56; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Acetaldehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 3 {ECO:0000255|HAMAP-Rule:MF_01657}; GN Name=lapF; OrderedLocusNames=Avin_30580; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303; RX PubMed=19429624; DOI=10.1128/jb.00504-09; RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A., RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S., RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I., RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L., RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., RA Dean D.R., Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized RT to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). 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; CP001157; ACO79223.1; -; Genomic_DNA. DR RefSeq; WP_012701609.1; NC_012560.1. DR AlphaFoldDB; C1DN56; -. DR SMR; C1DN56; -. DR STRING; 322710.Avin_30580; -. DR EnsemblBacteria; ACO79223; ACO79223; Avin_30580. DR KEGG; avn:Avin_30580; -. DR eggNOG; COG4569; Bacteria. DR HOGENOM; CLU_062208_0_0_6; -. DR OrthoDB; 9786743at2; -. DR Proteomes; UP000002424; 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. FT CHAIN 1..304 FT /note="Acetaldehyde dehydrogenase 3" FT /id="PRO_0000387621" FT ACT_SITE 130 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 272 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 304 AA; 32308 MW; 1D4C6F8C9D041824 CRC64; MKKIRCALIG SGNIGTDLIY KIRRSALLEP VWMVGIDPAS EGLARARELG LKTTAEGVDG LLPHVQEDDI QIAFDATSAY VHAENSRKLN ALGVLVIDLT PAAIGPLCVP PVNLREHAAR LEMNVNMISC AGQATIPVVH AVSRIQSVAY AEIVASLASK SIGPGTRANL DEFTYTTSGA LEKVGGARRG KALAIINPAE PPMIMRNTIS CLTDAEPDQE RLSASILQMV GEVQKYVPGY RLVNGPLYDG NGVSVFMEVA GLGDYLPTYA GNLDIMTAAA TRTAEMFAEE ILAGKIRLPT PEVA //