ID C6KWI9_9BACT Unreviewed; 325 AA.
AC C6KWI9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000256|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000256|HAMAP-Rule:MF_01657};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:BAH90336.1};
RN [1] {ECO:0000313|EMBL:BAH90336.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Ohnuki T., Miyazaki K.;
RT "Functional screening of a metagenomic library for genes involved in
RT microbial degradation of aromatic compounds.";
RL Environ. Microbiol. 9:2289-2297(2007).
RN [2] {ECO:0000313|EMBL:BAH90336.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Koyama Y., Miyakoshi M., Miyazaki R., Yano H., Sota M.,
RA Ohtsubo Y., Tsuda M., Miyazaki K.;
RT "Novel organization of aromatic degradation pathway genes in a microbial
RT community as revealed by metagenomic analysis.";
RL ISME J. 0:0-0(2009).
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:0000256|HAMAP-
CC Rule:MF_01657};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009244, ECO:0000256|HAMAP-Rule:MF_01657}.
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DR EMBL; AB266148; BAH90336.1; -; Genomic_DNA.
DR AlphaFoldDB; C6KWI9; -.
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 {ECO:0000256|HAMAP-Rule:MF_01657};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01657};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01657}.
FT DOMAIN 17..133
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 141
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 23..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 173..181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 325 AA; 34429 MW; FDF296F64343695E CRC64;
MQAGCGGERG NANMKRKVAI IGSGNIGTDL MMKILKGSDE LEIAAMVGID PDSDGLRRAR
DLGVATTHEG LEGLRAMAVY PEVSIVMDAT SAHAHERHHP VLVADGKQII DLTPAAIGPF
VIPPVNLDEN KSSEALNMVT CGGQATIPMV YAVRRAVDRL IYGEIVASVS SRSAGPGTRA
NIDEFTQTTS LGIEKVGGAE RGKAIIILNP ADPPMLMRDT VFTLSQGGSE EAIRESVAEM
VREVQSYVPG YRLKQEIQFE RIGDNAPLNV PGIGRVSGLK TSIFIEVEGN GDYFPSYAGN
LDIMTSAAKA AAESWARAHD SGKAA
//
