ID P97091_PSEFL Unreviewed; 306 AA.
AC P97091;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1997, sequence version 1.
DT 13-SEP-2023, entry version 80.
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 Name=cumG {ECO:0000313|EMBL:BAA09693.1};
OS Pseudomonas fluorescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294 {ECO:0000313|EMBL:BAA09693.1};
RN [1] {ECO:0000313|EMBL:BAA09693.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IP01 {ECO:0000313|EMBL:BAA09693.1};
RA Aoki H., Kimura T., Habe H., Yamane H., Kodama T., Omori T.;
RT "Cloning, nucleotide sequence, and characterization of the genes encoding
RT enzymes involved in the degradation of cumene to 2-Hydroxy-6-oxo-7-
RT methylocta-2,4-dienoic acid in Pseudomonas fluorescens IP01.";
RL J. Ferment. Bioeng. 81:187-196(1996).
RN [2] {ECO:0000313|EMBL:BAA09693.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IP01 {ECO:0000313|EMBL:BAA09693.1};
RA Habe H., Kimura T., Nojiri H., Yamane H., Omori T.;
RT "Cloning and nucleotide sequence of the genes involved in the meta-cleavage
RT pathway of cumene degradation in Pseudomonas fluorescens IP01.";
RL J. Ferment. Bioeng. 81:247-254(1996).
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; D63377; BAA09693.1; -; Genomic_DNA.
DR AlphaFoldDB; P97091; -.
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}.
FT DOMAIN 5..120
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 130
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 161..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 306 AA; 32622 MW; 60D71CC3198FC3E4 CRC64;
MNKIKCALIG PGNIGTDLLY KLQRSTVLEP VWMVGVDPTS EGLRRAAAMG LKTTSDGVDG
LLPHIATDGI LIAFDATSAY VHAENSRKLN ELGVMMIDLT PAAIGPFCVP PVNLLKHVGQ
GEMNVNMVTC GGQATIPMVA AVSRVQPVTY GEIVATTASK SIGPGTRANI DEFTRTTGSA
IEIVGGAKKG KAIIIINPAE PPMIMRDTVH CLTETEPDRE RITASVQKMV KEVQKYVPGY
KLVNGPVFDG KRISLFLEVE GLGDYLPKYA GNLDIMTAAA VRTAEMFAEE ISSGKLKLGP
TIETQK
//
