ACDH6_RHOJR
ID ACDH6_RHOJR Reviewed; 299 AA.
AC Q0RXC4; Q8KZT1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
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 Name=hpdG; OrderedLocusNames=RHA1_ro09018;
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12514024; DOI=10.1128/aem.69.1.427-433.2003;
RA Sakai M., Miyauchi K., Kato N., Masai E., Fukuda M.;
RT "2-Hydroxypenta-2,4-dienoate metabolic pathway genes in a strong
RT polychlorinated biphenyl degrader, Rhodococcus sp. strain RHA1.";
RL Appl. Environ. Microbiol. 69:427-433(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABH00062.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AB085906; BAB97164.1; -; Genomic_DNA.
DR EMBL; CP000432; ABH00062.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041813279.1; NC_008269.1.
DR AlphaFoldDB; Q0RXC4; -.
DR SMR; Q0RXC4; -.
DR EnsemblBacteria; ABH00062; ABH00062; RHA1_ro09018.
DR KEGG; rha:RHA1_ro09018; -.
DR PATRIC; fig|101510.16.peg.8301; -.
DR HOGENOM; CLU_062208_0_0_11; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
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..299
FT /note="Acetaldehyde dehydrogenase 6"
FT /id="PRO_0000387731"
FT ACT_SITE 125
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 156..164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 299 AA; 31708 MW; E0F9484669CC9144 CRC64;
MEPINAAIVG PGNIGTDLLA KLERVDSIAV QYVVGVVESD GLERARAKGI SASAGGVDWL
LEQDPLPEIV FEATSAKAHQ LNAPRYHELN IQAVDLTPAH IGPMVCPPVN LTHHIDAPNV
SMITCGGQAT IPMVHAVSRV SAVPYAEIVA SVASRGAGPG TRANIDEFTQ TTGQAVSEVG
GAARGRAIII LNPMEPPMIM RDTVYCMIDA DADRDAISES VHRMVTEVQA YVPGYRLRAD
PQFDDPKDGW DGHGRVAIFL EVEGNGDYLP KYAGNLDIMT AAAARVGDSI ARNRMGVPA