ID A0A1G5Q8B2_9MICC Unreviewed; 700 AA.
AC A0A1G5Q8B2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl-coenzyme A oxidase {ECO:0000313|EMBL:SCZ57917.1};
GN ORFNames=SAMN02799638_02327 {ECO:0000313|EMBL:SCZ57917.1};
OS Arthrobacter sp. UNCCL28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1502752 {ECO:0000313|EMBL:SCZ57917.1, ECO:0000313|Proteomes:UP000199526};
RN [1] {ECO:0000313|EMBL:SCZ57917.1, ECO:0000313|Proteomes:UP000199526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCCL28 {ECO:0000313|EMBL:SCZ57917.1,
RC ECO:0000313|Proteomes:UP000199526};
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}.
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DR EMBL; FMWE01000003; SCZ57917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5Q8B2; -.
DR STRING; 1502752.SAMN02799638_02327; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000199526; 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; 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 45..151
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 156..266
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 300..461
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 524..660
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 76410 MW; 4D05DF041F1BE3BF CRC64;
MTEVVDRNAS VQHTAGSKGA AAAGPEPVVD VAALGEQLLG KWAHIRHEAR KVAGNPVVQK
IEGLHHTEHR ARVFEQLKFL VDNNTVHRAF PTRLGGSDDH GGNIAGFEEI VTADPSLQIK
AGVQWGLFGS AVMHLGTVEH QDKWLPGIMS LEIPGCFAMT ETGHGSDVAS IATTATYDDA
SQEFVINTPF RAAWKDYIGN AANDGLAAVV FAQLITRNVN HGVHAFYVEL RDPATKEFLP
GIGGEDDGIK GGLNGIDNGR LHFTNVRIPR TNLLNRYGDV AVDGTYSSPI ESPGRRFFTM
LGTLVQGRVS LDGAAVAASK VALKTAIQYA TERRQFNASS ATDEEVLLDY QRHQRRLFSR
LATTYAASFA HEQLLQKFDD VFSGAHDTDA DRQDLETLAA ALKPLSTWHA LDTLQECREA
CGGAGFLIEN RFASLRADLD VYVTFEGDNT VLLQLVAKRL LADYAKEFRS ADFGVLARYV
VDQAAGVALH RTGLRQVAQF VADTGSVQKA ALALRDEEGQ RTLLADRVQS MVAEVGAALK
GANKLPQHQA AALFNQHQHE LIEAAQAHAE LLQWEAFTEG LNQVTDEGTK RVLTWLRDLF
GLSLIEKHLS WYLMNGRLSM QRGRTVGTYI NRLLVKIRPH AVDLVDAFGY GPEHLRASIA
TGAEAERQDA ARKHFREQRA SGSAPADEKT LLALKASKAR
//
