ID   ACDH1_NOVAD             Reviewed;         311 AA.
AC   A4XF36;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Acetaldehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] 1 {ECO:0000255|HAMAP-Rule:MF_01657};
GN   OrderedLocusNames=Saro_3688;
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OG   Plasmid pNL2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC   F199;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT   "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT   12444.";
RL   Submitted (APR-2007) 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:0000255|HAMAP-
CC         Rule:MF_01657};
CC   -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01657}.
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DR   EMBL; CP000677; ABP64547.1; -; Genomic_DNA.
DR   RefSeq; WP_011906931.1; NC_009427.1.
DR   AlphaFoldDB; A4XF36; -.
DR   SMR; A4XF36; -.
DR   STRING; 279238.Saro_3688; -.
DR   EnsemblBacteria; ABP64547; ABP64547; Saro_3688.
DR   KEGG; nar:Saro_3688; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_5; -.
DR   OMA; NVNMISC; -.
DR   OrthoDB; 1432332at2; -.
DR   Proteomes; UP000009134; Plasmid pNL2.
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   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   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; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..311
FT                   /note="Acetaldehyde dehydrogenase 1"
FT                   /id="PRO_0000387700"
FT   ACT_SITE        129
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         11..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         161..169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   311 AA;  33365 MW;  75D1AD29DD55CCF8 CRC64;
     MTRVKAAIIG SGNIGTDLMM KMIKYPQNME LAIVVGIDEK SEGLAMAREH GIATTHEGLE
     GLRRHPLYKE IGIAFDATSA YAHKVHDEAL RADGIQVVDL TPAAIGPFTV PPVNMSQHLD
     QPNVNMVTCG GQATIPMVAA VARVSDKVHY AEIVASVSSR SAGPGTRANI DEFTRTTARA
     IEVVGGATRG KAIIILNPAE PPMIMRDTVF TLSEGADEDQ IRRSVADMVA EVQKYVPGYR
     LKQEVQFERF GDNNKLKIPG QGEFTGIKSM IMLEVEGAGD YLPSYSGNLD IMTAAAKATG
     ELLAARRMAA A