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Database: UniProt
Entry: A0A194QVT5_PAPMA
LinkDB: A0A194QVT5_PAPMA
Original site: A0A194QVT5_PAPMA 
ID   A0A194QVT5_PAPMA        Unreviewed;       627 AA.
AC   A0A194QVT5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   ORFNames=RR48_08880 {ECO:0000313|EMBL:KPJ09429.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ09429.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ09429.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09429.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ09429.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00004846}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR   EMBL; KQ461103; KPJ09429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194QVT5; -.
DR   STRING; 76193.A0A194QVT5; -.
DR   InParanoid; A0A194QVT5; -.
DR   Proteomes; UP000053240; Unassembled WGS sequence.
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:0009058; P:biosynthetic process; IEA:UniProt.
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; 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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR10909:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 1.
DR   Pfam; PF01756; ACOX; 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|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000168};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053240}.
FT   DOMAIN          12..107
FT                   /note="Acyl-coenzyme A oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   DOMAIN          443..623
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        395
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         113
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         152
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ   SEQUENCE   627 AA;  70531 MW;  6ACC54D0F5F852A4 CRC64;
     MDEQKVLSIK GLLDDTPEEY LSHKEKYENS IRKSVLFYKT LHSTEDENMS VDEKTKLNFR
     NIVTSAIFKD NSPFMLHNSM FIPTIMGQGT DEQREYWMKR AKNMEIIGTY AQTELGHGTF
     IRGLETQATY DPDTEEFVLH SPVLSSYKWW PGGLAHTANY CIVMARLYIK GKSHGIHPFM
     VQIRDEETHM PLPGIKLGEI GAKLGFNTVN NGFLGFENHR ISRDRMLMKN AQVLKDGTFV
     AGSNSKLTYG TMVYVRVLIV SNMANMLAKA VTIALRYSAI RRQSQPKPDE PEPQILDYVT
     QQHKLFIAIA SSHAFYMNAM WLWEIYYSVS LQLASGKLDN LPELHALACC LKPLSTIDAT
     AMIEKCRLAC GGHGYMLSAN LAQTYGLATA AYTYEGENTV LLLQAARSLV KAWVGHVKGR
     PLKGTMAYLA GDSTVKAWDG SIDGIIQSFK VVAIRKISSV VKILQDYEKS GLSPEDAWNK
     ASVFLTAASE AHGRAVLLSV YKSEMDKRAA VLSPPLRKVL LQLVDLYVTY WALEKVGDML
     LYASITDKDV DELQRRYIEL LAAIRPNAVG LVDAFDFRDE ILNSTLGAYD GRAYERLMEE
     AMKSPLNAEP VNQTFHKYLK PFMRGKL
//
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