ACDH_MYCBP
ID ACDH_MYCBP Reviewed; 303 AA.
AC A1KPM0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Propanal dehydrogenase (CoA-propanoylating) {ECO:0000250|UniProtKB:P9WQH3};
DE EC=1.2.1.87 {ECO:0000250|UniProtKB:P9WQH3};
DE AltName: 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=hsaG {ECO:0000250|UniProtKB:P9WQH3}; OrderedLocusNames=BCG_3599c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC -!- FUNCTION: Involved in cholesterol degradation. Catalyzes the conversion
CC of propanal to propanoyl-CoA, using NAD(+) and coenzyme A.
CC {ECO:0000250|UniProtKB:P9WQH3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA;
CC Xref=Rhea:RHEA:36027, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.87;
CC Evidence={ECO:0000250|UniProtKB:P9WQH3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36028;
CC Evidence={ECO:0000250|UniProtKB:P9WQH3};
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;
CC Evidence={ECO:0000250|UniProtKB:P9WQH3, ECO:0000255|HAMAP-
CC Rule:MF_01657};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23289;
CC Evidence={ECO:0000250|UniProtKB:P9WQH3};
CC -!- SUBUNIT: Monomer. Forms an heterotetramer composed of two aldolase
CC (HsaF) and two dehydrogenase (HsaG) subunits.
CC {ECO:0000250|UniProtKB:P9WQH3}.
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01657}.
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DR EMBL; AM408590; CAL73588.1; -; Genomic_DNA.
DR RefSeq; WP_003419251.1; NC_008769.1.
DR AlphaFoldDB; A1KPM0; -.
DR SMR; A1KPM0; -.
DR GeneID; 45427519; -.
DR KEGG; mbb:BCG_3599c; -.
DR HOGENOM; CLU_062208_0_0_11; -.
DR OMA; TSAYVHK; -.
DR Proteomes; UP000001472; 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 PIRSF; PIRSF015689; Actaldh_dh_actl; 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..303
FT /note="Propanal dehydrogenase (CoA-propanoylating)"
FT /id="PRO_0000387674"
FT ACT_SITE 127
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 12..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 158..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 303 AA; 32009 MW; D52F1BEA88A56827 CRC64;
MPSKAKVAIV GSGNISTDLL YKLLRSEWLE PRWMVGIDPE SDGLARAAKL GLETTHEGVD
WLLAQPDKPD LVFEATSAYV HRDAAPKYAE AGIRAIDLTP AAVGPAVIPP ANLREHLDAP
NVNMITCGGQ ATIPIVYAVS RIVEVPYAEI VASVASVSAG PGTRANIDEF TKTTARGVQT
IGGAARGKAI IILNPADPPM IMRDTIFCAI PTDADREAIA ASIHDVVKEV QTYVPGYRLL
NEPQFDEPSI NSGGQALVTT FVEVEGAGDY LPPYAGNLDI MTAAATKVGE EIAKETLVVG
GAR
