ID A0A0Q8Q042_9SPHN Unreviewed; 305 AA.
AC A0A0Q8Q042;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ASE00_21220 {ECO:0000313|EMBL:KRB78898.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB78898.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB78898.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB78898.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB78898.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB78898.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB78898.1}.
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DR EMBL; LMIB01000020; KRB78898.1; -; Genomic_DNA.
DR RefSeq; WP_056384063.1; NZ_LMIB01000020.1.
DR AlphaFoldDB; A0A0Q8Q042; -.
DR STRING; 1736594.ASE00_21220; -.
DR OrthoDB; 9786743at2; -.
DR Proteomes; UP000051854; 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 Reference proteome {ECO:0000313|Proteomes:UP000051854}.
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 11..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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 305 AA; 32262 MW; 08729CD531B62527 CRC64;
MNRVRCAIIG SGNIGTDLIY KLQRSDILDP VWLVGIDPLS DGLARASGMG LKTTAEGVDG
LLPHVKADDI RIAFDATSAY VHAENSAKLT ALGVLMIDLT PAAIGPYCCP PVNLAEVAKS
GVTNVNMISC AGQATIPMVH AVSRIQPVDY AEIVATAASK SIGPGTRANL DEFTYTTSGA
VAEVGGAKRG KALVIVNPAE PPLMMRDTIY CLTQSTPDEA AVRDSVYAMV DEVKQYVPGY
RLVNGPVFDG NKISIFVEVE GLGDYLPKYA GNLDIMTASA VRTAELFAER MIAAVGSERE
KEVAR
//
