ACDH7_RHOJR
ID ACDH7_RHOJR Reviewed; 262 AA.
AC Q0RWM7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Acetaldehyde dehydrogenase 7 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 7 {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=RHA1_ro10116;
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL2.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
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}.
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DR EMBL; CP000433; ABH00309.1; -; Genomic_DNA.
DR RefSeq; WP_011599978.1; NC_008270.1.
DR AlphaFoldDB; Q0RWM7; -.
DR SMR; Q0RWM7; -.
DR EnsemblBacteria; ABH00309; ABH00309; RHA1_ro10116.
DR KEGG; rha:RHA1_ro10116; -.
DR PATRIC; fig|101510.16.peg.8524; -.
DR HOGENOM; CLU_062208_0_0_11; -.
DR OMA; TESIHRM; -.
DR Proteomes; UP000008710; Plasmid pRHL2.
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..262
FT /note="Acetaldehyde dehydrogenase 7"
FT /id="PRO_0000387732"
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"
SQ SEQUENCE 262 AA; 27348 MW; EC351AE6B1A07D09 CRC64;
MTTKVAIIGS GNIGTDLMFK IQRLSQTLEV AALVGIDPES DGLQRAGRLG IPITADGVAG
LLDIPGFDQI SIVFDATSAR AHVANAAALE PFGKQLVDLT PAAIGPYVVP AVNLEENLAA
RNVNMVTCGG QATIPMVAAV SHVAPVAYAE IVASIASRSA GPGTRANIDE FTETTSKAIE
VVGGAHRGKA IIVLNPADPP LIMRDTILCL IGDADHDAIR DSVHRRVAEV SEYVPGYRLK
QDVQITTVTD DVPLSTLGRV SQ
