ACDH1_RHIWR
ID ACDH1_RHIWR Reviewed; 314 AA.
AC A5V6T7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Acetaldehyde dehydrogenase 1/2 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 1/2 {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=Swit_1640;
GN and
GN OrderedLocusNames=Swit_2112;
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-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; CP000699; ABQ68003.1; -; Genomic_DNA.
DR EMBL; CP000699; ABQ68471.1; -; Genomic_DNA.
DR RefSeq; WP_011952481.1; NC_009511.1.
DR AlphaFoldDB; A5V6T7; -.
DR SMR; A5V6T7; -.
DR STRING; 392499.Swit_1640; -.
DR PRIDE; A5V6T7; -.
DR EnsemblBacteria; ABQ68003; ABQ68003; Swit_1640.
DR EnsemblBacteria; ABQ68471; ABQ68471; Swit_2112.
DR KEGG; swi:Swit_1640; -.
DR KEGG; swi:Swit_2112; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_5; -.
DR OMA; NVNMISC; -.
DR OrthoDB; 1432332at2; -.
DR Proteomes; UP000001989; 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..314
FT /note="Acetaldehyde dehydrogenase 1/2"
FT /id="PRO_0000387743"
FT ACT_SITE 130
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 12..15
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 314 AA; 33111 MW; 096763373CD7890D CRC64;
MSQKVKAAII GSGNIGTDLM IKMIKYPQNM ELAAVVGIDP ASEGLAMARE RGIATTHEGI
EGLKKLPDYA EIGVVFDATS AYAHKVHDEA LRADGKLVVD LTPAAIGPFT IPPVNMDEHL
DATNVNMVTC GGQATIPIVA AVSQVATVHY AEIVASVSSR SAGPGTRANI DEFTRTTASA
IEKVGGAAQG KAIIILNPAE PPMIMRDTVF TLSEGADEEA IRASVAAMVA KVQAYVPGYR
LKQEVQFERF GDNNKLKIPG RGEFTGIKTS VFLEVEGAGD YLPSYSGNLD IMTAAAKATG
ELLAQRIIER RAAA