ID   ACDH1_MYCMM             Reviewed;         336 AA.
AC   B2HGH0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   28-JAN-2026, entry version 86.
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=MMAR_1505;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + NAD(+) + CoA = acetyl-CoA + NADH + H(+);
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}.
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DR   EMBL; CP000854; ACC39956.1; -; Genomic_DNA.
DR   RefSeq; WP_012393348.1; NC_010612.1.
DR   AlphaFoldDB; B2HGH0; -.
DR   SMR; B2HGH0; -.
DR   STRING; 216594.MMAR_1505; -.
DR   KEGG; mmi:MMAR_1505; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_11; -.
DR   OrthoDB; 9786743at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   CDD; cd23933; ALDH_C; 1.
DR   Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
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   NCBIfam; NF006157; PRK08300.1; 1.
DR   Pfam; PF09290; AcetDehyd-dimer; 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..336
FT                   /note="Acetaldehyde dehydrogenase 1"
FT                   /id="PRO_0000387677"
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;  34340 MW;  BF143065EFA89B7E CRC64;
     MSLGAADVGA GAGPPGQHAG AVDNWPVAII GSGVVGADLM SRIGNGDGRL RVSAMVGTNP
     HCDGLARAAA AGISTSPGGV DGLLIMPEFA NIRLVFDTTN PGARQSNWAR LADTGVRMLD
     LTASAIGPCC VPAVNLDAQL DAPNLSMATC SAQAAVPIVA AVRRHGVVRY AEVVSAIASQ
     ALGPAERVTL DEFAELTTTA VQELGGARRA KTLTIVNPAD PPMPMRTTVF CLVDQADEVA
     RIEADVLAVV DGVQALLPGY RLKHRVQFER LGSGNTLYIP GTGEFGGTRI TVLLEITAAG
     GYLPACAGNV AIVTSAAKAT AEAIVEHHAQ TVKAEL
//