ACDH_MYCBO
ID ACDH_MYCBO Reviewed; 303 AA.
AC Q7TTR4; A0A1R3Y4I3; X2BP90;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=BQ2027_MB3565C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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}.
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; LT708304; SIU02192.1; -; Genomic_DNA.
DR RefSeq; NP_857204.1; NC_002945.3.
DR RefSeq; WP_003419251.1; NC_002945.4.
DR AlphaFoldDB; Q7TTR4; -.
DR SMR; Q7TTR4; -.
DR EnsemblBacteria; SIU02192; SIU02192; BQ2027_MB3565C.
DR GeneID; 45427519; -.
DR PATRIC; fig|233413.5.peg.3908; -.
DR OMA; TSAYVHK; -.
DR Proteomes; UP000001419; 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_0000387673"
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
