ID ACDH_BURPS Reviewed; 297 AA. AC Q63JB0; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657}; DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657}; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657}; GN Name=mhpF; OrderedLocusNames=BPSS1808; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A., RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia RT pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). 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; BX571966; CAH39284.1; -; Genomic_DNA. DR RefSeq; WP_004552044.1; NZ_CP009537.1. DR RefSeq; YP_111812.1; NC_006351.1. DR AlphaFoldDB; Q63JB0; -. DR SMR; Q63JB0; -. DR STRING; 272560.BPSS1808; -. DR KEGG; bps:BPSS1808; -. DR PATRIC; fig|272560.51.peg.5251; -. DR eggNOG; COG4569; Bacteria. DR Proteomes; UP000000605; Chromosome 2. 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..297 FT /note="Acetaldehyde dehydrogenase" FT /id="PRO_0000387634" FT ACT_SITE 130 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 162..170 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" FT BINDING 272 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657" SQ SEQUENCE 297 AA; 32346 MW; 03A1F8782B7CA1CB CRC64; MKSKSSRTRV AILGSGSIGL DLMFKVKASE QFDLKFVVGR NANSDGLRLA RSCNVETSSD GLDFLKAHED AYDLVFDATS AAAHKVNNRF FSDAGKFVID LTPAKVGRLC VPCINLDDMG AEQNVNLITC GGQASLPLAY ALKQAVDEID YLEVVSAIAS RSAGIATREN IDEYMTTTEY ALAKFSDAKK TKAILNINPA EPGVRMQTTL YAYARYRDFD RVRASVADMV EKVREYVPGY RLVVEPLESQ GRITIGLTVR GRGDYLPEYA GNLDIINCAA LAVASHRHAT ARLGATQ //