ID   ACOX2_CUCMA             Reviewed;         690 AA.
AC   O64894;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Acyl-coenzyme A oxidase, peroxisomal;
DE            Short=AOX;
DE            EC=1.3.3.6;
DE   AltName: Full=Long-chain acyl-CoA oxidase;
DE   Flags: Precursor;
GN   Name=Acx;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-81, FUNCTION,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Kurokawa Amakuri Nankin; TISSUE=Cotyledon;
RX   PubMed=9525937; DOI=10.1074/jbc.273.14.8301;
RA   Hayashi H., De Bellis L., Yamaguchi K., Kato A., Hayashi M., Nishimura M.;
RT   "Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase
RT   that is synthesized as a precursor of higher molecular mass in pumpkin.";
RL   J. Biol. Chem. 273:8301-8307(1998).
CC   -!- FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2-
CC       trans-enoyl-CoAs. {ECO:0000269|PubMed:9525937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC         Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9525937}.
CC       Glyoxysome {ECO:0000269|PubMed:9525937}.
CC   -!- DEVELOPMENTAL STAGE: Induced one day after germination with a peak at
CC       day 5 and then declines steadily until day 8.
CC       {ECO:0000269|PubMed:9525937}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; AF002016; AAC15870.1; -; mRNA.
DR   AlphaFoldDB; O64894; -.
DR   SMR; O64894; -.
DR   PRIDE; O64894; -.
DR   OrthoDB; 226134at2759; -.
DR   Proteomes; UP000504608; Unplaced.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC.
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; -; 1.
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.
DR   PANTHER; PTHR10909; PTHR10909; 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; SSF47203; 2.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein;
KW   Glyoxysome; Lipid metabolism; Oxidoreductase; Peroxisome;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Peroxisome"
FT                   /evidence="ECO:0000269|PubMed:9525937"
FT   CHAIN           46..690
FT                   /note="Acyl-coenzyme A oxidase, peroxisomal"
FT                   /id="PRO_0000000556"
FT   BINDING         448..453
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   690 AA;  77319 MW;  430C843A757ABFC2 CRC64;
     MASPGEPNRT AEDESQAAAR RIERLSLHLT PIPLDDSQGV EMETCAAGKA KAKIEVDMGS
     LSLYMRGKHR EIQERVFEYF NSRPELQTPV GISMADHREL CMKQLVGLVR EAGIRPFRFV
     NEDPAKYFAI MEAVGSVDVS LAIKMGVQFS LWGGSVINLG TKKHRDRFFD GIDNVDYPGC
     FAMTELHHGS NVQGLQTTAT FDPITDEFII NTPNDGAIKW WIGNAAVHGK FATVFAKLVL
     PTHDSRKTAD MGVHAFIVPI RDLKSHKTLP GIEIHDCGHK VGLNGVDNGA LRFRSVRIPR
     DNLLNRFGEV SRDGKYKSSL PSINKRFAAT LGELVGGRVG LAYSSASVLK IASTIAIRYS
     LLRQQFGPPK QPEVSILDYQ SQQHKLMPML ASTYAFHFST MQLVEKYAQM KKTHDEELVG
     DVHALSAGLK AYVTSYTAKS LSTCREACGG HGYAVVNRFG TLRNDHDIFQ TFEGDNTVLL
     QQVAAYLLKQ YQEKFQGGTL AVTWNYLRES MNTYLSQPNP VTARWESADH LRDPKFQLDA
     FQYRTSRLLQ SVAVRLRKHT KNLGSFGAWN RCLNHLLTLA ESHIESVILA QFIESVQRCP
     NANTQATLKL VCDLYALDRI WNDIGTYRNV DYVAPNKAKA IHKLTEYLCF QVRNIAQELV
     DAFDLPDHVT RAPIAMKSNA YSQYTQYIGF