ACDH1_MYCUA
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 03-AUG-2022, entry version 77.
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; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
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};
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DR EMBL; CP000325; ABL04788.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_071498395.1; NC_008611.1.
DR AlphaFoldDB; A0PR19; -.
DR SMR; A0PR19; -.
DR STRING; 362242.MUL_2436; -.
DR EnsemblBacteria; ABL04788; ABL04788; MUL_2436.
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 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 SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03215; ac_ald_DH_ac; 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
