ID ACDH1_MYCUA Reviewed; 336 AA. AC A0PR19; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 03-NOV-2009, sequence version 2. DT 24-JAN-2024, entry version 83. DE RecName: Full=Acetaldehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 1 {ECO:0000255|HAMAP-Rule:MF_01657}; GN Name=mhpF; OrderedLocusNames=MUL_2436; OS Mycobacterium ulcerans (strain Agy99). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=362242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Agy99; RX PubMed=17210928; DOI=10.1101/gr.5942807; RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M., RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.; RT "Reductive evolution and niche adaptation inferred from the genome of RT Mycobacterium ulcerans, the causative agent of Buruli ulcer."; RL Genome Res. 17:192-200(2007). 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 -!- SEQUENCE CAUTION: CC Sequence=ABL04788.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000325; ABL04788.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_071498395.1; NC_008611.1. DR AlphaFoldDB; A0PR19; -. DR SMR; A0PR19; -. DR KEGG; mul:MUL_2436; -. DR eggNOG; COG4569; Bacteria. DR HOGENOM; CLU_062208_0_0_11; -. DR Proteomes; UP000000765; 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 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..336 FT /note="Acetaldehyde dehydrogenase 1" FT /id="PRO_0000387690" FT ACT_SITE 150 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 32..35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 309 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 336 AA; 34358 MW; 176DCC1008DA9038 CRC64; MSLGAADVGA GAGPPGQHAG AVDNWPVAII GSGVVGTDLM SRIGNGDGRL RVSAMVGTNP HCDGLARAAA AGISTSPGGV DGLLSMPEFA NIRLVFDTTN PGAHQSNWAR LADTGVRMLD LTASAIGPCC VPAVNLDAQL DAPNLSMATC SAQAAVPIVA AVRRHGVVRY AEVVSAIASQ ALGPAERVTL DEFAELTTTA VQELGGARRA KTLTIVNPAD PPMPMRTTVF CLVDQADEVA RNEADVLAVV DGVQALLPGY RLKHRVQFER LGSGNTLYIP GTGEFGGTRI TVLLEITAAG GYLPACAGNV AIVTSAAKAT AEAIVERHAQ TLKAKI //