ID ACDH2_PSEPW Reviewed; 315 AA. AC B1J6Y2; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 24-JAN-2024, entry version 82. DE RecName: Full=Acetaldehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 2 {ECO:0000255|HAMAP-Rule:MF_01657}; GN OrderedLocusNames=PputW619_2008; OS Pseudomonas putida (strain W619). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=390235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W619; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D., RA Richardson P.; RT "Complete sequence of Pseudomonas putida W619."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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; CP000949; ACA72508.1; -; Genomic_DNA. DR AlphaFoldDB; B1J6Y2; -. DR SMR; B1J6Y2; -. DR STRING; 390235.PputW619_2008; -. DR KEGG; ppw:PputW619_2008; -. DR eggNOG; COG4569; Bacteria. DR HOGENOM; CLU_062208_0_0_6; -. DR OrthoDB; 9786743at2; -. 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..315 FT /note="Acetaldehyde dehydrogenase 2" FT /id="PRO_0000387710" FT ACT_SITE 131 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 13..16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 162..170 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 315 AA; 33227 MW; DA8DC3E8B68FCBD6 CRC64; MSSTRIPVAI IGSGNIGTDL MIKILRCSDT LEVGAMVGID PASDGLARAE RLGVPTTAGG IDGLLALPNF KEIRIAFDAT SAGAHKVHDS KLRAHGVRII DLTPAAVGPY VVPVVNFAEH AHEPNLNMVT CGGQATIPIV HAVAGVAPVH YAEIVAAISS KSAGPGTRAN IDEFTETTSR AIVEVGGAAR GKAIIVLNPA EPPLIMRDTV YCFVPLDADT QAIVDAVEQR VAEVNRYVPG YRLKQHVQFE HFTENNRQNI PGLGWSTGIK VAVYLEVEGA GHYLPAYAGN LDIMTSAALT VAERIAQAQF TDQGL //