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Database: UniProt
Entry: A0A0U4CJR2_9ACTN
LinkDB: A0A0U4CJR2_9ACTN
Original site: A0A0U4CJR2_9ACTN 
ID   A0A0U4CJR2_9ACTN        Unreviewed;       633 AA.
AC   A0A0U4CJR2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:ALX03430.1};
GN   ORFNames=AERYTH_01300 {ECO:0000313|EMBL:ALX03430.1};
OS   Aeromicrobium erythreum.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX03430.1, ECO:0000313|Proteomes:UP000067689};
RN   [1] {ECO:0000313|EMBL:ALX03430.1, ECO:0000313|Proteomes:UP000067689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR18 {ECO:0000313|EMBL:ALX03430.1,
RC   ECO:0000313|Proteomes:UP000067689};
RX   PubMed=1883712;
RA   Miller E.S., Woese C.R., Brenner S.;
RT   "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT   strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL   Int. J. Syst. Bacteriol. 41:363-368(1991).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; CP011502; ALX03430.1; -; Genomic_DNA.
DR   RefSeq; WP_067853624.1; NZ_CP011502.1.
DR   AlphaFoldDB; A0A0U4CJR2; -.
DR   STRING; 2041.AERYTH_01300; -.
DR   KEGG; aer:AERYTH_01300; -.
DR   PATRIC; fig|2041.4.peg.273; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000067689; Chromosome.
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; 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; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067689}.
FT   DOMAIN          128..237
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          271..430
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          490..628
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   633 AA;  69652 MW;  29F47B4BEA7ECF13 CRC64;
     MTLSDEVRIA LDGKWRHVRE QSRTELAAME LAYDLDLDID AARERTLRQL HGLVPTGVPA
     AGFRTEHGGG GDPGMAVTGI EMLAQFDLSL MVKAGVQWGL FGGAVENLGT ERHRDLIPRL
     IELDLVGCYA MTEIGHGSNV QHLETTATYD AETQEFVVDS PTPSATKDYI GNAAAHATVA
     AVYAQLVTRG ENHGVHCFLV PIRDDQGQVL EGVEVGDDRH KGGLGGVDNG RLAFHQVRIP
     RVNLLNKYGD VAEDGTYSSP IDDVNRRFFS MLGTLVRGRI SVGGSALAAA EVALSIAGRY
     ALQRRQFGQE GEPEVLLADY RLHQRRLLPL LARSYAYRFA QNQQVSRMDR LQRATEPDAQ
     QQRELEGRAA GLKAIMTWHA SRAINESREM CGGAGYLAEN RLTVLRGDID VFTTFEGDNH
     VMLQLLSKEL LTSYAKEVGG LDPFGMVRFV AETVADTVRE RTAASQLIQR LIDAAPAGGD
     AHDLLDRGTQ LSLFEDREQH LIETAARRLQ RAAKAKGEEA FRIFNDAQDH LIRCGRAHVD
     RVVLEAFTAG IARCEDEEAA DLLRQVCTVY ALSVIEDDLA WFMAHNRISD QRAKAVTQLL
     NEQLAELRPH LLTLVEGLGV PEETLGAAML LKQ
//
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