ID V9V0K3_9PSED Unreviewed; 316 AA.
AC V9V0K3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=X970_10620 {ECO:0000313|EMBL:AHC87843.1};
OS Pseudomonas monteilii SB3101.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC87843.1, ECO:0000313|Proteomes:UP000018660};
RN [1] {ECO:0000313|EMBL:AHC87843.1, ECO:0000313|Proteomes:UP000018660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3101 {ECO:0000313|EMBL:AHC87843.1,
RC ECO:0000313|Proteomes:UP000018660};
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA Nielsen J.L.;
RT "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL Submitted (DEC-2013) 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: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; CP006979; AHC87843.1; -; Genomic_DNA.
DR RefSeq; WP_012052594.1; NC_023076.1.
DR AlphaFoldDB; V9V0K3; -.
DR SMR; V9V0K3; -.
DR KEGG; pmot:X970_10620; -.
DR PATRIC; fig|1435058.3.peg.2076; -.
DR HOGENOM; CLU_062208_0_0_6; -.
DR Proteomes; UP000018660; 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 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|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|HAMAP-Rule:MF_01657,
KW ECO:0000313|EMBL:AHC87843.1}.
FT DOMAIN 6..124
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 132
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 12..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 163..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 316 AA; 33685 MW; 8EC4DB2D9A44D19B CRC64;
MTRKVKAAII GSGNIGTDLM IKILRHGQHI EMGAMVGIDP ASDGLARAQR MGVAITHEGV
EGLTRLPVFN EIDVVFDATS AGAHVKNEAL LRERKPGLRM IDLTPAAIGP YCIPVVNGDD
HLDATNVNMV TCGGQATIPM VAAVSRVAKV HYAEIIASIS SKSAGPGTRA NIDEFTETTS
KAIEVVGGAA KGKAIIVLNP AEPPLMMRDT VYTLSDFADI DQIEESVQRM ADAVQAYVPG
YRLKQRVQFD RIEADCPIRI PGVGDRMNGL KTSIFLEVEG AAHYLPAYAG NLDIMTSAAL
RTAEKLAERL LASLVA
//
