ID Q84DI0_9ACTN Unreviewed; 296 AA. AC Q84DI0; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 02-OCT-2024, entry version 66. DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000256|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000256|HAMAP-Rule:MF_01657}; GN Name=sanN {ECO:0000313|EMBL:AAO73547.1}; OS Streptomyces ansochromogenes. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=115647 {ECO:0000313|EMBL:AAO73547.1}; RN [1] {ECO:0000313|EMBL:AAO73547.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17659257; DOI=10.1016/j.bbrc.2007.07.016; RA Ling H., Wang G., Tian Y., Liu G., Tan H.; RT "SanM catalyzes the formation of 4-pyridyl-2-oxo-4-hydroxyisovalerate in RT nikkomycin biosynthesis by interacting with SanN."; RL Biochem. Biophys. Res. Commun. 361:196-201(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:0000256|HAMAP- CC Rule:MF_01657}; CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009244, ECO:0000256|HAMAP-Rule:MF_01657}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; AY188795; AAO73547.1; -; Genomic_DNA. DR AlphaFoldDB; Q84DI0; -. 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:0009056; P:catabolic process; IEA:UniProtKB-KW. 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 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 {ECO:0000256|HAMAP-Rule:MF_01657}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01657}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01657}. FT DOMAIN 8..120 FT /note="Semialdehyde dehydrogenase NAD-binding" FT /evidence="ECO:0000259|SMART:SM00859" FT ACT_SITE 128 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657" FT BINDING 268 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657" SQ SEQUENCE 296 AA; 31414 MW; 04C88B6A3485F79C CRC64; MQATGRLSVS VLGAGLIGMD LATKIMRSDC LDLRLVAGRH DAAELRRAAR RGMPVATGGI QSLVDAEEDF DVVFDATNAS FHAEHAEKLA ASGAMIVDLT PSRVGQMIVP GVNREDIGSH RDISMVTCGG QACVPILHAI ARAHEIDCVE VVTTAATLSV GRASRLNLDE YVQTTQDAIR WFTGVEDVKA LVNISPARPA ATFRVAMYLR GRDLTTDSVR ALVTRAADEI RTYVKGFGVS VCTVNDSTAF VSVEVTSSGE RLPHYAGNLD IINSAAIQAA ECYAAGRLAL AGRETA //