ACDH_SALTO
ID ACDH_SALTO Reviewed; 308 AA.
AC A4XAK8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=Strop_3526;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP55957.1; -; Genomic_DNA.
DR RefSeq; WP_012014732.1; NC_009380.1.
DR AlphaFoldDB; A4XAK8; -.
DR SMR; A4XAK8; -.
DR STRING; 369723.Strop_3526; -.
DR EnsemblBacteria; ABP55957; ABP55957; Strop_3526.
DR KEGG; stp:Strop_3526; -.
DR PATRIC; fig|369723.5.peg.3640; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_11; -.
DR OMA; NVNMISC; -.
DR Proteomes; UP000000235; Chromosome.
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; Reference proteome.
FT CHAIN 1..308
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000387738"
FT ACT_SITE 128
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 10..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 159..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 308 AA; 32155 MW; BAEF104DA56F0635 CRC64;
MSVGVAVLGS GNIGTDLMIK VLRLSDSLRM VAMAGIDPDS DGLARARRLG VTTTAEGVAG
LVALPEFADV ALVFDATSAG AHRHHDAVLR AHGRTVVDLT PAAVGPYVVP PVNLDEHLRE
TNVNMVTCGG QATVPIVAAV GRVTPVTYGE IVASIAAKSA GPGTRANIDE FTETTARAIE
VVGGAELGKA IIVLNPADPP LLMRDTVYCL CPDTDADRSA IAAAIADMVR AVQEYVPGYC
LKQDVQFDRV DSYLPALGRR LTGLQVSTFL EVSGAGHYLP TYAGNLDIMT SAALRTAERL
IARRAVTA
