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Database: UniProt
Entry: A0A0N0AQL5_9ACTN
LinkDB: A0A0N0AQL5_9ACTN
Original site: A0A0N0AQL5_9ACTN 
ID   A0A0N0AQL5_9ACTN        Unreviewed;       653 AA.
AC   A0A0N0AQL5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:KOX19844.1};
GN   ORFNames=ADL06_28330 {ECO:0000313|EMBL:KOX19844.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX19844.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX19844.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX19844.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOX19844.1}.
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DR   EMBL; LGEE01000251; KOX19844.1; -; Genomic_DNA.
DR   RefSeq; WP_053647798.1; NZ_LGEE01000251.1.
DR   AlphaFoldDB; A0A0N0AQL5; -.
DR   PATRIC; fig|1519495.3.peg.6046; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000037743; 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; 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; 2.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
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; IPR009075; AcylCo_DH/oxidase_C.
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; PTHR10909:SF382; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 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;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          35..142
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          147..255
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          289..450
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          508..649
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   653 AA;  71178 MW;  A5839BC808B190CE CRC64;
     MATDNAFTTG SGYAQPEIDV RALAGVLDGE YAGIRDLVRT NLATYASVLE EADELDIDAF
     RERVREIVVG MAATGQTGMG FPAEYGGGGD VGASIAAFET LAFGDLSVLV KTGVQFGLFG
     GAILHLGTER HHEAYLPDLI AGRLMGSFAM TESGHGSNVQ ALGTVARYDA GSREFVITTP
     GDRERKDYIG NAARHAELAV VFAQLEVDGT SEGVHAFVVP VRVGGETAPG VRIEDDGRKM
     GLNGVDNGRI WFDGVRVPRE ALLDRFAAVS PEGVYTSPIE NPNRRFFTML GTLVQGRVSV
     GGAGVNVAKV ALAIAVKYSV RRRQFEASPG TEEQLLLDYG LHQRRLLPLV ARTYALHFAQ
     DVVRTQLHEV FSGTEDDPPA RRRLESRAAG TKALGTWHAT RTVQECREAC GGAGYLAVNR
     FAALKSDSDV FTTFEGDNHV LLQLVAKGLL TDHASEFEDL DQLGMVRYVT GLAVETVMER
     TSAHKLLERV RDLLPGGDEW DREAGLLDPE YQLAMVRYRE EHMLAGVARR LKRGIDQKRD
     PGAVFSHVQD HVIALAHAHV ERLVLESFVD RVRAMPEGGN KEALALLCDL FALSTIEADR
     AWFMEHGRLT VQRSKAITRE VNDLCRKVRP LAVDLVDAWG VPPEMLRAPD LVG
//
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