ID K0DX29_9BURK Unreviewed; 350 AA.
AC K0DX29;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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};
GN ORFNames=BUPH_00406 {ECO:0000313|EMBL:AFT87874.1};
OS Paraburkholderia phenoliruptrix BR3459a.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT87874.1, ECO:0000313|Proteomes:UP000010105};
RN [1] {ECO:0000313|EMBL:AFT87874.1, ECO:0000313|Proteomes:UP000010105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3459a {ECO:0000313|EMBL:AFT87874.1,
RC ECO:0000313|Proteomes:UP000010105};
RX PubMed=23144415; DOI=10.1128/JB.01821-12;
RA de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA Ribeiro de Vasconcelos A.T.;
RT "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL J. Bacteriol. 194:6675-6676(2012).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01657}.
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DR EMBL; CP003864; AFT87874.1; -; Genomic_DNA.
DR AlphaFoldDB; K0DX29; -.
DR STRING; 1229205.BUPH_00406; -.
DR KEGG; bpx:BUPH_00406; -.
DR PATRIC; fig|1229205.11.peg.4259; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_791489_0_0_4; -.
DR Proteomes; UP000010105; Chromosome 2.
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 Pfam; PF09290; AcetDehyd-dimer; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01657};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01657};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01657}.
FT DOMAIN 8..126
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT REGION 238..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 165..173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 350 AA; 37230 MW; C2200FB9D19977D9 CRC64;
MKTKARLDVA IIGPGNIGTD LMIKTLRYAK YLRMEAMVGV DPASDGLARA RRLGVATTHE
GVQGLARLPM FEDIDIVFDA TSASAHVKND AFLHAAKPGL QMIDLTPAAI GPFVVPVVNA
FEHVGAANLN MVTCGGQATI PIVHAVSRIA PVHYAEIVAS ISSRSAGPGT RANIDEAAGL
EPWLQCQATD RRGRRHRAPA AGKTRAGGPR NACTWLRWRV FELSAAYRSG RGEVRAVRIR
HHGRARAPPD GGRPGRHDRG RRPGYGANAA ATASASREGK RMIDYDELAA RVDAAACKAT
PVPRLTGTPG FTLDAACEIQ RAAHALAHGV HVQCLINGLG VTEFTTYQPS
//
