ID K6GHW3_9GAMM Unreviewed; 307 AA.
AC K6GHW3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 13-SEP-2023, entry version 42.
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=B273_0470 {ECO:0000313|EMBL:EKO36611.1};
OS SAR86 cluster bacterium SAR86E.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1208365 {ECO:0000313|EMBL:EKO36611.1, ECO:0000313|Proteomes:UP000010310};
RN [1] {ECO:0000313|EMBL:EKO36611.1, ECO:0000313|Proteomes:UP000010310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAR86E {ECO:0000313|EMBL:EKO36611.1};
RA Dupont C.L., Rusch D.B., Lombardo M.-J., Novotny M., Yee-Greenbaum J.,
RA Laskin R.;
RL Submitted (SEP-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKO36611.1}.
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DR EMBL; AMWX01000005; EKO36611.1; -; Genomic_DNA.
DR AlphaFoldDB; K6GHW3; -.
DR STRING; 1208365.B273_0470; -.
DR PATRIC; fig|1208365.4.peg.724; -.
DR Proteomes; UP000010310; Unassembled WGS sequence.
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:EKO36611.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010310}.
FT DOMAIN 5..121
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 129
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 11..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 160..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 307 AA; 32798 MW; 8AF41D713F8AE01B CRC64;
MSKVKCAIIG SGNIGTDLML KIIKTSQSLS LNGVIGIDPE SEGLAMAKSH NIAISSTGLQ
GFMEMDEYQD TEIFFDATSA GAHKNHHDLI INDGKQMIDL TPAAIGPYCV PVVNLTEHLK
EKNVNMVTCG GQATIPMVAA VNQVSSVKYA EIVASVSSKS AGPGTRANID EFTQTTKLGL
EKVGGADRAK AIIVLNPAEP PLLMRNTVFT LCDPVDQQLV KDSIEAMVGR VQSYVPGYRL
KQEVQFERFG SNNPCLIPGY GEFEGLKASI FLEVEGAGHY LPTYAGNLDI MTSAAMGTAQ
ELIKLNS
//
