ID ACDH_MOOTA Reviewed; 291 AA.
AC Q2RHL2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 OrderedLocusNames=Moth_1776;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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}.
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DR EMBL; CP000232; ABC20077.1; -; Genomic_DNA.
DR RefSeq; YP_430620.1; NC_007644.1.
DR AlphaFoldDB; Q2RHL2; -.
DR SMR; Q2RHL2; -.
DR STRING; 264732.Moth_1776; -.
DR EnsemblBacteria; ABC20077; ABC20077; Moth_1776.
DR KEGG; mta:Moth_1776; -.
DR PATRIC; fig|264732.11.peg.1927; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_9; -.
DR OrthoDB; 9783105at2; -.
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.
FT CHAIN 1..291
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000387669"
FT ACT_SITE 124
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 155..163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 291 AA; 30795 MW; 8AA1B3C4474AA82F CRC64;
MDKVKVAVIG PGNIGSDLMY KILRSRHLEM ALMTGIIESE GIKRARKLGI KTSIEGVKAV
LAEDDIKIVF DATGAKPHLQ HAPLLKEAGK IAIDLTPAAV GPYVVPCVNL DQVKAEPNLN
MVTCGGQATV PIVYAINRVA GARYAEIVAC IASKSAGPGT RQNIDEFTQT TAKALEVVGG
AKKGKAIIIL NPAEPPIMMH NTIYVEVEKP DIEAIRASVE AMVKEIQSYV PGYRLVVPPI
LDGNKVTAAV EVEGAGDFLP KYSGNLDIIT SAAVAVAEKL AQELQVKEGV A
//
