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Database: UniProt
Entry: R0GMU0_9BRAS
LinkDB: R0GMU0_9BRAS
Original site: R0GMU0_9BRAS 
ID   R0GMU0_9BRAS            Unreviewed;       692 AA.
AC   R0GMU0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   ORFNames=CARUB_v10025999mg {ECO:0000313|EMBL:EOA12483.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA12483.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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, ECO:0000256|PIRNR:PIRNR000168}.
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DR   EMBL; KB870812; EOA12483.1; -; Genomic_DNA.
DR   RefSeq; XP_006279585.1; XM_006279523.1.
DR   AlphaFoldDB; R0GMU0; -.
DR   STRING; 81985.R0GMU0; -.
DR   GeneID; 17874753; -.
DR   KEGG; crb:17874753; -.
DR   eggNOG; KOG0135; Eukaryota.
DR   OrthoDB; 5473219at2759; -.
DR   Proteomes; UP000029121; 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:0005504; F:fatty acid binding; IEA:InterPro.
DR   GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:InterPro.
DR   CDD; cd01150; AXO; 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; IPR034171; ACO.
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, ECO:0000256|PIRNR:PIRNR000168};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT   DOMAIN          182..298
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          332..489
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          535..679
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        475
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         186
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ   SEQUENCE   692 AA;  77533 MW;  87037BB10C29C04E CRC64;
     MESRRGMNPM TEEESSELAA MRRIQRLSSH ISPAMTAPPS LPLVQAETCS SRAKKLEVNG
     QALSLYMKGK HMDIQEKVYE FFNSRPDLQT PIEISKDDHR ELCMNQLLGL VREAGIRPFK
     YVADDPEKYF AIMEAVGSVD MSLGIKMGVQ YSLWGGSVIN LGTKKHRDKY FDGIDNLDYT
     GCFAMTELHH GSNVQGLQTT ATFDPLKDEF VIDTPHDGAI KWWIGNAAVH GKFATVFARL
     ILPTHDSKGV SDMGVHAFIV PIRDMKTHQT LPGVEIQDCG HKVGLNGVDN GALRFRSVRI
     PRDNLLNRFG DVSRDGKYTS SLPTINKRFG ATLGELVGGR VGLAYASVGV LKISATIAIR
     YSLLRQQFGP PKQPEVSILD YQSQQHKLMP MLASTYAYHF ATVYLVEKYS EMKKTHDEQL
     VADVHALSAG LKSYVTSYTA KSLSVCREAC GGHGYAAVNR FGSLRNDHDI FQTFEGDNTV
     LLQQVAADLL KRYKEKFQGG TLTVTWSYLR ESMNTYLSQP NPVTARWEGE DHLRDPKFQL
     DAFRYRTSRL LQNVAARLQK HSKTLGGFGA WNRCLNHLLT LAESHIETVI LAKFIEAVKN
     CPEPSARAAL KLACDLYALD RIWKDIGTYR NVDYVAPNKA KAIHKLTEYL CFQVRNVAKE
     LVDAFELPDH VTRAPIAMQS DAYSQYTQVV GF
//
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