ID ACDH2_NOCSJ Reviewed; 314 AA. AC A1SIM4; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 90. 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=Noca_2150; OS Nocardioides sp. (strain ATCC BAA-499 / JS614). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614; 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 Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., RA Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) 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; CP000509; ABL81659.1; -; Genomic_DNA. DR AlphaFoldDB; A1SIM4; -. DR SMR; A1SIM4; -. DR STRING; 196162.Noca_2150; -. DR KEGG; nca:Noca_2150; -. DR eggNOG; COG4569; Bacteria. DR HOGENOM; CLU_062208_0_0_11; -. DR Proteomes; UP000000640; 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..314 FT /note="Acetaldehyde dehydrogenase 2" FT /id="PRO_0000387699" 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 289 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 314 AA; 32725 MW; F86FEF69218E7E0C CRC64; MTASTIPRQI AIIGSGNIGT DLMIKVLRLS KTLEVGAMVG IDPDSDGLAR ANRLGVPTTS DGVDGLIRMP NFEAIDIVLD ATSARAHAAN YTALRRYRKR MIDLTPAAVG PFVVPAVNMG ASLSADNVNM VTCGGQATIP IVAAISQVTP VAYAEIVASI ASKSAGPGTR QNIDEFTETT AHAIEQVGGA RKGKAIIILN PAEPPLIMRD TVLALIGPSD HDAVKGSIRA MVDAVAEYVP GYRLKQRIEI QPLDGLPVGT LTSEPVTHKV SVFLEVEGAA HYLPAYAGNL DIMTSAALRV AEAMAAQKLS GAVA //