ID ACDH7_RHOJR Reviewed; 262 AA. AC Q0RWM7; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Acetaldehyde dehydrogenase 7 {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 7 {ECO:0000255|HAMAP-Rule:MF_01657}; GN OrderedLocusNames=RHA1_ro10116; OS Rhodococcus jostii (strain RHA1). OG Plasmid pRHL2. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=101510; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RHA1; RX PubMed=17030794; DOI=10.1073/pnas.0607048103; RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H., RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., RA Eltis L.D.; RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a RT catabolic powerhouse."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006). 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; CP000433; ABH00309.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RWM7; -. DR SMR; Q0RWM7; -. DR KEGG; rha:RHA1_ro10116; -. DR PATRIC; fig|101510.16.peg.8524; -. DR HOGENOM; CLU_062208_0_0_11; -. DR OrthoDB; 9786743at2; -. DR Proteomes; UP000008710; Plasmid pRHL2. 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; Plasmid; KW Reference proteome. FT CHAIN 1..262 FT /note="Acetaldehyde dehydrogenase 7" FT /id="PRO_0000387732" FT ACT_SITE 128 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 10..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 159..167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 262 AA; 27348 MW; EC351AE6B1A07D09 CRC64; MTTKVAIIGS GNIGTDLMFK IQRLSQTLEV AALVGIDPES DGLQRAGRLG IPITADGVAG LLDIPGFDQI SIVFDATSAR AHVANAAALE PFGKQLVDLT PAAIGPYVVP AVNLEENLAA RNVNMVTCGG QATIPMVAAV SHVAPVAYAE IVASIASRSA GPGTRANIDE FTETTSKAIE VVGGAHRGKA IIVLNPADPP LIMRDTILCL IGDADHDAIR DSVHRRVAEV SEYVPGYRLK QDVQITTVTD DVPLSTLGRV SQ //