ID Q0S1Y0_RHOJR Unreviewed; 365 AA.
AC Q0S1Y0;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Probable acyl-CoA dehydrogenase {ECO:0000313|EMBL:ABG98456.1};
GN OrderedLocusNames=RHA1_ro06683 {ECO:0000313|EMBL:ABG98456.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG98456.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
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).
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DR EMBL; CP000431; ABG98456.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0S1Y0; -.
DR KEGG; rha:RHA1_ro06683; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_1_11; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 3..112
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 117..199
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
SQ SEQUENCE 365 AA; 40033 MW; BEC6A97FDF6859D3 CRC64;
MDDLRTEVRE FLAEQLSEGK IGRQIDSWLT GWDEDFTRAL AARGWLGMTV PAEYGGHDRR
HLERFVVTEE LLAAGAPVAA HWIADRQIVP SLLKYGTEVQ KHKFLPAITR GECYFGIGMS
EPDSGSDLAS VRTKATRVDG GWSITGAKVW TSGAHRADAF ICLARTAQLD PAHRHDGLSQ
FIVDLHAPGV DIRPIVSMNG QHHFNEVLLD EVLVEDEMVF GTIDNGWQQV TSELSFERSG
PERFLSTFVL LAKTAEQMKQ GTLPRHSNLG RYFGRIAGLH QMSTAVAGAL ERHEPADTAA
AVVKVLGTST EGDIADFADL LTDESSATHY TSMLEDAIVQ RPGFTLRGGT NEVLRGVIAR
GLGMR
//
