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Database: UniProt
Entry: A0A0M4QW78_9MICC
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ID   A0A0M4QW78_9MICC        Unreviewed;       690 AA.
AC   A0A0M4QW78;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=acyl-CoA oxidase {ECO:0000256|ARBA:ARBA00012870};
DE            EC=1.3.3.6 {ECO:0000256|ARBA:ARBA00012870};
GN   ORFNames=AOC05_06810 {ECO:0000313|EMBL:ALE92111.1};
OS   Arthrobacter alpinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE92111.1, ECO:0000313|Proteomes:UP000062833};
RN   [1] {ECO:0000313|Proteomes:UP000062833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA   See-Too W.S., Chan K.G.;
RT   "Complete genome of Arthrobacter alpinus strain R3.8.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; CP012677; ALE92111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4QW78; -.
DR   KEGG; aaq:AOC05_06810; -.
DR   PATRIC; fig|656366.3.peg.1457; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000062833; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
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; PF14749; Acyl-CoA_ox_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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062833}.
FT   DOMAIN          35..142
FT                   /note="Acyl-coenzyme A oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   DOMAIN          145..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          516..649
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   690 AA;  75513 MW;  8732BA9927AFB1FB CRC64;
     MTEVMTSTTA PASDGHTVDV AALGELLLGN WADVRRQARA LAGNPELHKV EGLSHTEHRL
     RAFKQLGILV QQDGVHRAFP SRLGGNDDHG GNVAGFEELV LADPSVQIKA GVQWGLFGSA
     VMHLGSAEHQ DKWLPGIMSL EIPGCFAMTE IGHGSDVASI ATTATYDSST GEFVINTPFR
     AAWKEYIGNA AVDGLAAVVF AQLITRGVNH GVHAFYVQLR DPATKEFFPG IDGLDDSIKG
     GLNGIDNGRL CFNNVRIPRS NLLNRYGDVT ADGVYSSPIA SPGRRFFTML GTLVQGRVSL
     NGAAVAASKV ALKIAIQYAT ERRQFNAASD TEEVVLMDYQ RHQRRLLPLL ATTYAATFAH
     EQLLVKFDGV FSGAHDSDED RQDLETLAAA LKSMTTWHAL DTLQECREAC GGAGFMVENR
     FTSLRADLDV YATFEGDNTV LLQLVAKRLL ADYSKEFRNL DFGVLARFVV GQAADLTLNR
     TGLRQVAQFV ADSGSPQKSA KALKDEDTQH ELLVGRVQTM VADVAGALKE AAKLPKDKAA
     EIFNDNQNEL IEAARAHAEL LQWEAFTEAL HRVEDAGTKK VLTRLRDLFG LGLIEKHLDW
     YLMNGRVSMQ RARTLGPYIN RLLAKLRPHA LDLVDAFGYG PEHLRATIAT GIERERQDEA
     RDYFRIQRAS SDGPVDEKVL IQRAKASAKK
//
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