ID   A0A1K1Y432_STRAR        Unreviewed;       618 AA.
AC   A0A1K1Y432;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-coenzyme A oxidase {ECO:0000313|EMBL:SFX56616.1};
GN   ORFNames=SAMN02787144_100493 {ECO:0000313|EMBL:SFX56616.1};
OS   Streptomyces atratus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1893 {ECO:0000313|EMBL:SFX56616.1, ECO:0000313|Proteomes:UP000181909};
RN   [1] {ECO:0000313|EMBL:SFX56616.1, ECO:0000313|Proteomes:UP000181909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK807 {ECO:0000313|EMBL:SFX56616.1,
RC   ECO:0000313|Proteomes:UP000181909};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; FPJO01000004; SFX56616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1Y432; -.
DR   STRING; 1893.SAMN02787144_100493; -.
DR   Proteomes; UP000181909; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
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; 2.
DR   InterPro; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR012258; Acyl-CoA_oxidase.
DR   InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          285..397
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
FT   DOMAIN          482..583
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   618 AA;  66304 MW;  9FCE332A019383C2 CRC64;
     MTATIDSPSA EPSTDLLTGV LLGYNHRREH GFWQRLISTE PFRRPEHRTT EERLDLAYER
     LRVLNDCLDS GARLAADHRA LAALHEWLGP VDPALTTVAG IHYNLFLGSL LDHGDDGHHD
     LSDFLRLRRI GTFLCTEVAH GNDAAAVETT AEYDRERDGF VLRTPHAGAQ KFMPNTSPAG
     GPKTGLVAAR LLVDGADHGV FLFLVPLTDA EQPLPGVRIR RLPTRTGSPV DHCLTSFDRV
     FVGRAALLGG DHGRIGADGE FSSTIDNRRR RFLASIGRVT SGKISMTACA VGCARATLAV
     AVRYGGHRYI SGPRGSRPVP VIAHRSHHGP LASATATVFA MSLLHRRALD RWERGGQPEE
     AERLVAVAKG WITWQARAVI VECRERCGAQ ALLENNGMSE LLTGVEGAIT AEGDNVAIHA
     KAAAEMLFAA APAGPGPSPG GGPGDLDDPG FLGRLLAELE RIWFGRARER IGLAPLGDPL
     ARWNAASGPA LRGVEAHAQR QAAEAYTVAV AELPEGPARE RLDELRRLFA LDRIARNSGD
     LLAAGLLTAD QVNGLPDRVE ALITAVAAHL PGLVESFALP PELLADWPIA GADYVAAYDD
     PDAAWQTDGG RATVPDER
//