ID   ACOX5_CANTR             Reviewed;         662 AA.
AC   P08790;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Acyl-coenzyme A oxidase 5;
DE            Short=Acyl-CoA oxidase 5;
DE            EC=1.3.3.6;
DE   AltName: Full=PXP-5;
GN   Name=POX5;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=3456583; DOI=10.1073/pnas.83.5.1232;
RA   Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.;
RT   "Two acyl-coenzyme A oxidases in peroxisomes of the yeast Candida
RT   tropicalis: primary structures deduced from genomic DNA sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:1232-1236(1986).
RN   [2]
RP   SEQUENCE REVISION TO 265.
RA   Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC   -!- SUBUNIT: Homooctamer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; M12161; AAA34363.2; -; Genomic_DNA.
DR   PIR; B25123; OXCKX5.
DR   AlphaFoldDB; P08790; -.
DR   SMR; P08790; -.
DR   PRIDE; P08790; -.
DR   VEuPathDB; FungiDB:CTMYA2_045920; -.
DR   VEuPathDB; FungiDB:CTRG_02721; -.
DR   SABIO-RK; P08790; -.
DR   UniPathway; UPA00661; -.
DR   GO; GO:0005777; C:peroxisome; 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:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
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   Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR   PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF47203; SSF47203; 2.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW   Peroxisome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..662
FT                   /note="Acyl-coenzyme A oxidase 5"
FT                   /id="PRO_0000204697"
FT   REGION          642..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   662 AA;  74238 MW;  6746A72B6AD1986C CRC64;
     MPTELQKERE LTKFNPKELN YFLEGSQERS EIISNMVEQM QKDPILKVDA SYYNLTKDQQ
     REVTAKKIAR LSRYFEHEYP DQQAQRLSIL GVFDPQVFTR IGVNLGLFVS CVRGNGTNSQ
     FFYWTINKGI DKLRGIYGCF GMTELAHGSN VQGIETTATF DEDTDEFVIN TPHIGATKWW
     IGGAAHSATH CSVYARLKVK GKDYGVKTFV VPLRDSNHDL EPGVTVGDIG AKMGRDGIDN
     GWIQFSNVRI PRFFMLQKYC KVSRSGEVTM PPSEQLSYSA LIGGRVTMMM DSYRMTSRFI
     TIALRYAIHR RQFKKKDTDT IETKLIDYPL HQKRLFPFLA AAYLFSQGAL YLEQTMNATN
     DKLDEAVSAG EKEAIDAAIV ESKKLFVASG CLKSTCTWLT AEAIDEARQA CGGHGYSSYN
     GFGKAYSDWV VQCTWEGDNN ILAMNVAKPM VRDLLKEPEQ KGLVLSSVAD LDDPAKLVKA
     FDHALSGLAR DIGAVAEDKG FDITGPSLVL VSKLNAHRFL IDGFFKRITP EWSEVLRPLG
     FLYADWILTN FGATFLQYGI ITPDVSRKIS SEHFPALCAK VRPNVVGLTD GFNLTDMMTN
     AAIGRYDGNV YEHYFETVKA LNPPENTKAP YSKALEDMLN RPDLEVRERG EKSEEAAEIL
     SS