ID   A0A0W1DXB7_9SPHN        Unreviewed;       311 AA.
AC   A0A0W1DXB7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=ATE67_02215 {ECO:0000313|EMBL:KTE22759.1};
OS   Sphingopyxis sp. H050.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE22759.1, ECO:0000313|Proteomes:UP000053439};
RN   [1] {ECO:0000313|Proteomes:UP000053439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA   Gomez-Alvarez V., Revetta R.P.;
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:KTE22759.1}.
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DR   EMBL; LNRZ01000001; KTE22759.1; -; Genomic_DNA.
DR   RefSeq; WP_058815040.1; NZ_LNRZ01000001.1.
DR   AlphaFoldDB; A0A0W1DXB7; -.
DR   STRING; 1759072.ATE67_02215; -.
DR   OrthoDB; 9786743at2; -.
DR   Proteomes; UP000053439; 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}.
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   311 AA;  32517 MW;  19E770050586054F CRC64;
     MQKTKCAIIG SGNIGTDLMI KILKGSSELE LSAMIGIDPA SEGLAMARER GVTTTHEGMA
     GLQALDVYGE IGLVFDATSA YAHIEHAKAL AEDGKLVVDL TPAALGPFTV PPVNASVSSG
     ARNINMVTCG GQATIPIVAA VSRVAPVHYA EIVASVSSRS AGPGTRANID EFTRTTAKGL
     EVVGGAAKGR AIIILNPAEP PMIMRDTVFT LTDIVDEGLV RSAVEEMVAQ VQRYVPGYRL
     KQDVQFERFG SNRPLRIPGY GEFEGLKTSV FLEVEGAGDY LPKYAGNLDI MTSAAKAAAE
     VMVQHAGSAA A
//