ID   A0A1H1Y130_9MICO        Unreviewed;       688 AA.
AC   A0A1H1Y130;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acyl-coenzyme A oxidase {ECO:0000313|EMBL:SDT14849.1};
GN   ORFNames=SAMN04489751_3912 {ECO:0000313|EMBL:SDT14849.1};
OS   Brevibacterium sandarakinum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=629680 {ECO:0000313|EMBL:SDT14849.1, ECO:0000313|Proteomes:UP000199700};
RN   [1] {ECO:0000313|EMBL:SDT14849.1, ECO:0000313|Proteomes:UP000199700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22082 {ECO:0000313|EMBL:SDT14849.1,
RC   ECO:0000313|Proteomes:UP000199700};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT629739; SDT14849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1Y130; -.
DR   STRING; 629680.SAMN04489751_3912; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000199700; Chromosome i.
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:SF378; ACYL-COENZYME A OXIDASE-LIKE PROTEIN; 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          53..128
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          132..241
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          275..436
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          500..629
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   REGION          651..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  74849 MW;  BA57F118D76A6454 CRC64;
     MKLSLDPQAI NTVLDGRWAA ARRQGRSLAL DETTHEDPAD DLETARAKTL TSVGLMADTG
     LPKLSLPESL GGRNEHAANI AAFEETVTAS PSLQVKAGVQ FGLFGGAILH LGNPEQHDAW
     LLAAQSGELL GSFAMTEIGH GSDVAAVGTT ATYVAEDEEF VIDTPFRAAT KEFIGSAARD
     ARAAVVFAQL ITGGVNHGVH AFFVPIRDED GQTLPGISTE DDGYKGGLKG VDNGRIAFDQ
     VHIPRFNLLD RYGAVTAAGE YSSPIDSPGR RFFTMLGTLV QGRVSLDGAA IVASKLALDI
     AVRYGLERKQ FTTVDDINET TLLDYQQHQR RLMPAIASVY ASAFAHDKLL TSFEEVFSGA
     DGSEENRALL ETRAAAFKAD TTWMALDVIQ ECREACGGAG YMAENRLVGL RADLDIYATF
     EGDNTVLLQL AAKRLLGDYA KEFANIDVGG AARYIGTQAA EHTLYRTGLA NAGLAISDVF
     TPNLGEKRIR SGRLQRSLLE TRLEVMVSGL AQALRPAMKM SAADAADLFN SNQHEFIEMA
     RAYVELEKWK ALDEAMKDQT DPDQNKLFRR LRDTYGLSLI EKHVGWHLMY GRLPMLRARQ
     LNETLNRLCA KLSANAVDLV DAFGYGDDHR RATIATGVEA ERQTEAADYY RHSRAQEDYA
     VPEKQLRKAA KAARKAAEKD GRKAKSGS
//