ID ACDH4_AZOVD Reviewed; 312 AA. AC C1DF11; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Acetaldehyde dehydrogenase 4 {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 4 {ECO:0000255|HAMAP-Rule:MF_01657}; GN OrderedLocusNames=Avin_42130; 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; ACO80340.1; -; Genomic_DNA. DR RefSeq; WP_012702708.1; NC_012560.1. DR AlphaFoldDB; C1DF11; -. DR SMR; C1DF11; -. DR STRING; 322710.Avin_42130; -. DR EnsemblBacteria; ACO80340; ACO80340; Avin_42130. DR KEGG; avn:Avin_42130; -. 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..312 FT /note="Acetaldehyde dehydrogenase 4" FT /id="PRO_0000387622" FT ACT_SITE 132 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 12..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 163..171 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 290 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 312 AA; 32771 MW; 0E27C1810950BD4D CRC64; MTKKLKVAIV GSGNIGTDLM IKILRHGQHL EMGALVGIDP NSDGLARAAR LGVATTAEGV EGLARLPGFG EIDFVFDATS AGAHVRNEAF LRALKPGLRL IDLTPAAIGP YCVPVVNLEQ NLHETNVNMV TCGGQATIPM VAAVSRVARV HYAEIVASIA SRSAGPGTRA NIDEFTETTS KAIEAIGGAR KGKAIIVLNP AEPPLIMRDT VYVLSAPADR ARVEASLAEM AQAVQGYVPG YRLKQRVQFD EIPDAAPLNI PGLGRLSGLK TSVFLEVEGA AHYLPAYAGN LDIMTSAALA TAERMAQSML NA //