ACDH6_RHOOB
ID ACDH6_RHOOB Reviewed; 327 AA.
AC C1BE29;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Acetaldehyde dehydrogenase 6 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 6 {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=ROP_pROB02-02250;
OS Rhodococcus opacus (strain B4).
OG Plasmid pROB02.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011117; BAH47232.1; -; Genomic_DNA.
DR RefSeq; WP_012687258.1; NC_012521.1.
DR AlphaFoldDB; C1BE29; -.
DR SMR; C1BE29; -.
DR EnsemblBacteria; BAH47232; BAH47232; ROP_pROB02-02250.
DR KEGG; rop:ROP_pROB02-02250; -.
DR PATRIC; fig|632772.20.peg.8609; -.
DR HOGENOM; CLU_062208_0_0_11; -.
DR OMA; MIKVIRH; -.
DR OrthoDB; 1432332at2; -.
DR Proteomes; UP000002212; Plasmid pROB02.
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.
FT CHAIN 1..327
FT /note="Acetaldehyde dehydrogenase 6"
FT /id="PRO_0000387725"
FT ACT_SITE 133
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 15..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 164..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 327 AA; 34054 MW; F0DAF5DDEA10DE2C CRC64;
MSENTRKVTV AVIGSGNIGT DLMIKVIRHS DVLQMGAMVG IDPDSDGLAR ARRLGVPTTA
VGVHGLLELP NFDEIDVVFD ATSAKAHAAN AALLEPLGKR LIDLTPAALG PFVVPAVNLD
EHRHAANVNM VTCGGQATIP IVAAVSRVTP VAYAEIVASI ASKSAGPGTR ANIDEFTETT
SHAIETVGGA RRGKAIIVLN PADPPLIMRD TVLCLISARD PATHDAIRNS IQAMVEHVAT
YVPGYRLKQQ VQITPVPDGQ PVHTLLASGD TAAPTHQVSV FLEVEGAAHY LPAYAGNLDI
MTSAAVRYAE SVADTIAAPA ATQGATR