ACDH_ROSCS
ID ACDH_ROSCS Reviewed; 305 AA.
AC A7NLU3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Rcas_2411;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-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; CP000804; ABU58491.1; -; Genomic_DNA.
DR RefSeq; WP_012120915.1; NC_009767.1.
DR AlphaFoldDB; A7NLU3; -.
DR SMR; A7NLU3; -.
DR STRING; 383372.Rcas_2411; -.
DR EnsemblBacteria; ABU58491; ABU58491; Rcas_2411.
DR KEGG; rca:Rcas_2411; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_0; -.
DR OMA; TSAYVHK; -.
DR OrthoDB; 1432332at2; -.
DR Proteomes; UP000000263; 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.
FT CHAIN 1..305
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000387734"
FT ACT_SITE 128
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 13..16
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 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 305 AA; 32687 MW; DFCA758E9E7000E0 CRC64;
MGDETIKVAI LGSGNIGTDL MYKLLDCPAS MELVLLAGID PNSEGLARAR ALGVAASAQG
IDAVLEHPDI QIVFDATSAK AHVRHAKLLR ETGRTAIDLT PAARGPYVVP PVNLRQHLDA
PNVNLITCGG QATIPLVYAV SRVTPVRYAE IVSTVASRSA GPGTRQNIDE FTFTTAHGLE
VIGGAQQGKA IIILNPAEPP ILMRNTVYAL PEDDFDPAQV RDSIEAMVAE VQQYVPGYRL
KNPPVFDMRD TPWGRKSAVT VLLEVEGAGH FLPTYAGNLD IMTASARRVG DVFARHLLSR
REVAV
