ACDH2_BURVG
ID ACDH2_BURVG Reviewed; 303 AA.
AC A4JW24;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Acetaldehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 2 {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=Bcep1808_7604;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OG Plasmid pBVIE04.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of plasmid pBVIE04 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000620; ABO60477.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JW24; -.
DR SMR; A4JW24; -.
DR STRING; 269482.Bcep1808_7604; -.
DR EnsemblBacteria; ABO60477; ABO60477; Bcep1808_7604.
DR KEGG; bvi:Bcep1808_7604; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_4; -.
DR OMA; LMMRDTI; -.
DR Proteomes; UP000002287; Plasmid pBVIE04.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..303
FT /note="Acetaldehyde dehydrogenase 2"
FT /id="PRO_0000387643"
FT ACT_SITE 130
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 161..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 303 AA; 32376 MW; 95FA82383D1AFCFC CRC64;
MKKIKCALIG PGNIGTDLLA KLKRSSVLEP VWMVGIDPES EGLKRARELG VKTTAEGVDG
LLPHVLADGV QIAFDATSAY VHAENARKLN ALGVMMIDLT PAAIGPYCVP PVNLKEHLGK
REMNVNMVTC GGQATIPMVA AVSRVQPVAY AEIVATVSSR SVGPGTRKNI DEFTRTTAGA
VEKVGGARKG KAIIIINPAE PPLMMRDTIH CLTETEPDQQ RITESIHAMI EEVQKYVPGY
RLVNGPVFDG KRVTVFMEVA GLGDYLPTYA GNLDIMTAAA ARTAEMFAEE MIAGNLTLEP
VVA
