ACDH5_RHOJR
ID ACDH5_RHOJR Reviewed; 327 AA.
AC Q0S005;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acetaldehyde dehydrogenase 5 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 5 {ECO:0000255|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=RHA1_ro08084;
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1.
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; CP000432; ABG99131.1; -; Genomic_DNA.
DR RefSeq; WP_011599026.1; NC_008269.1.
DR AlphaFoldDB; Q0S005; -.
DR SMR; Q0S005; -.
DR EnsemblBacteria; ABG99131; ABG99131; RHA1_ro08084.
DR KEGG; rha:RHA1_ro08084; -.
DR PATRIC; fig|101510.16.peg.7426; -.
DR HOGENOM; CLU_062208_0_0_11; -.
DR OMA; MIKVIRH; -.
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..327
FT /note="Acetaldehyde dehydrogenase 5"
FT /id="PRO_0000387730"
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; 34131 MW; F6E755D4DC6726B5 CRC64;
MSENTRKVTV AVIGSGNIGT DLMIKVIRHS EVLQMGAMVG IDPDSDGLAR ARRLGVPTTS
DGVQGLLQLP NFDEIDVIFD ATSAKAHEAN AALLEPLGKR LIDLTPAALG PFVVPAVNLD
EHRDAANVNM VTCGGQATIP IVAAVSRVTP VAYAEIVASI ASKSAGPGTR ANIDEFTETT
SHAIETVGGA RRGKAIIILN PADPPLIMRD TVLCLISAPD PATHDAIRDS IQTMVDHVAT
YVPGYRLKQQ VQITPVPDGQ PVRTLLASGD AATPTHQVSV FLEVEGAAHY LPAYAGNLDI
MTSAAVRYAE SVADTIAAPT AAQGATR
