ID A0A2S0WF43_9CORY Unreviewed; 679 AA.
AC A0A2S0WF43;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:AWB84391.1};
GN ORFNames=C3E79_07765 {ECO:0000313|EMBL:AWB84391.1}, DF219_04360
GN {ECO:0000313|EMBL:PWB99881.1};
OS Corynebacterium liangguodongii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2079535 {ECO:0000313|EMBL:AWB84391.1, ECO:0000313|Proteomes:UP000244754};
RN [1] {ECO:0000313|EMBL:AWB84391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2184 {ECO:0000313|EMBL:AWB84391.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWB99881.1, ECO:0000313|Proteomes:UP000245180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2185 {ECO:0000313|EMBL:PWB99881.1,
RC ECO:0000313|Proteomes:UP000245180};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-2018) 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 oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288}.
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DR EMBL; CP026948; AWB84391.1; -; Genomic_DNA.
DR EMBL; QEEY01000003; PWB99881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WF43; -.
DR KEGG; clia:C3E79_07765; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000244754; Chromosome.
DR Proteomes; UP000245180; 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; 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}.
FT DOMAIN 157..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 404..473
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 528..667
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 73694 MW; 65D9E8B8006F9C27 CRC64;
MSQPTTTQAD RKQAKPEKNR PATLPVPGDS AVAGVLADVL DGPYAEAKNK LRPLLNDASF
LPPVEGSLDE LRAANLEKVK AVAASGEIQP SFSPLNGGEG KVTAGVTSLE LIAQVNNSVC
IKSGVQFGLW GGAIDALGTE RHVKFAQGAM DLSMLGCFAM TEMGHGSNVQ HVETTATFDP
ETQEFIINSP TPSSKKAYIG NAARDGRWAA VFAQLYTPDS EESRGVHCFI VRIREEDGTD
APGVTTSDHG HKGGLLGVDN GMIMFDHVRI PRENLLNRFA DVTEDGTYVS PIENPNRRFF
TMLGTLVRGR MGVGASAAGA TRAGLALAVK YANVRRQFEA GDESKEARLI DYRQHRRRLL
IPLAKSYALM TFQNAILQRF QNQIDAQFAG DWDPARPTKE QDRAGREMET LAAIFKATAS
THANSTLQTC REACGGAGYM SENLLTTFRA DVDIFTTFEG DDTILRQLAG KNLLTAYGWE
AASWSPFDIA KHVASNVGDI LARRSGIAAG IETISDRVTG TGSLFEADTQ LRILQYREEQ
VLESLVRRVQ SARKMDRAEA AKVIDRAQDH LLAMADAYGD RMLLQSMIEA EGQLEEGSTA
RAVFEQVRDL FALNAIVEHA DWYQEHGALS AGRSKAAKAA VNDLVDSLGP WSETLVDAFK
IPQVVLDRPM MTNGGTDLS
//
