ID ACDH2_PSEP1 Reviewed; 314 AA. AC A5W4F9; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 89. 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=Pput_2889; OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.; RT "Complete sequence of Pseudomonas putida F1."; RL Submitted (MAY-2007) 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; CP000712; ABQ79019.1; -; Genomic_DNA. DR AlphaFoldDB; A5W4F9; -. DR SMR; A5W4F9; -. DR KEGG; ppf:Pput_2889; -. DR eggNOG; COG4569; Bacteria. DR HOGENOM; CLU_062208_0_0_6; -. 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..314 FT /note="Acetaldehyde dehydrogenase 2" FT /id="PRO_0000387708" FT ACT_SITE 133 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 15..18 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 164..172 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 291 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 314 AA; 33141 MW; 8493107A6E2138DD CRC64; MQTHDGKTAV AIIGSGNIGT DLMVKILRHG KHLRMGAFVG IDPESDGLKR AERMGVPTVS TGIEGLLSHP DFGSIGFVFD ATSAGAHARH EQLLRPHGVR VIDLTPAAIG PFVVPAVNIE QHLDAPNVNM VTCGGQATIP MVAAVSRVVP VEYAEIVASI SSRSAGPGTR ANIDEFTETT SNAIVRVGGA QRGKAIIILN PAEPPLIMRD TVYCLVPGHA DRQAIVESVE RMASAVAAYV PGYRLKQTVQ FDEFKGRMPQ ETGSAQAPRL KVSVFLEVEG AGHYLPSYAG NLDIMTSAAL ATAERIAARQ PVAA //