ID   ACOX_CANGA              Reviewed;         748 AA.
AC   Q6FY63;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Acyl-coenzyme A oxidase;
DE            Short=Acyl-CoA oxidase;
DE            EC=1.3.3.6;
GN   Name=POX1; OrderedLocusNames=CAGL0A03740g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; CR380947; CAG57823.1; -; Genomic_DNA.
DR   RefSeq; XP_444930.1; XM_444930.1.
DR   AlphaFoldDB; Q6FY63; -.
DR   SMR; Q6FY63; -.
DR   STRING; 5478.XP_444930.1; -.
DR   EnsemblFungi; CAG57823; CAG57823; CAGL0A03740g.
DR   GeneID; 2886280; -.
DR   KEGG; cgr:CAGL0A03740g; -.
DR   CGD; CAL0126919; CAGL0A03740g.
DR   VEuPathDB; FungiDB:CAGL0A03740g; -.
DR   eggNOG; KOG0136; Eukaryota.
DR   HOGENOM; CLU_014629_3_1_1; -.
DR   InParanoid; Q6FY63; -.
DR   OMA; PMMRGKL; -.
DR   UniPathway; UPA00661; -.
DR   Proteomes; UP000002428; Chromosome A.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
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; 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; 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; Reference proteome.
FT   CHAIN           1..748
FT                   /note="Acyl-coenzyme A oxidase"
FT                   /id="PRO_0000204692"
SQ   SEQUENCE   748 AA;  84417 MW;  0955D23455BFF665 CRC64;
     MTKLSTVDPN ASVLNPQRFI QRERENCSID IDQVNTFLES DPRSRDLTHL IVDQLVNDPI
     IKADSATYDQ TKLTQREVTV KKIARMALYM EQDIKTVRKH FRDTDLLKSL QDFGDTTTPP
     LTNKDLAIFD KRLSLVANMD PQLSTRIGVH LGLFGNCIKG NGTDEQIKYW LQTRGAILIK
     GIYGCFAMTE LGHGSNVAQL QTTATYDQES DTFIINTPDL AATKWWIGGA AHSATHTACY
     ARLLVNGKDY GVKTFVVPLR DPSSLQLMPG IAIGDIGAKM GRDGIDNGWI QFRNVVIPRE
     FMLSRFTKVH RNPGATPTVE VDPQLDQISG YSALLSGRVN MVMDSFRFGS KFATIATRYA
     VGRQQFADKP GQPEKQLIDY PLHQYRVLPQ IVIPYIISPA AFSLLNFYYS TLDELYAASS
     KNDKRALVVV SQKLKNLFID SASLKATNTW LVAQLIDELR QTCGGHGYSG YNAFGKGYND
     WVVQCTWEGD NNILSLTSAK SILKKFVDSA TKGKYNKELD KRSFRYLDPQ FIRKVFTSSS
     ENKLDDLYDY TNIWAVALLK LLRHIAKQVD STKDLDGASK LLVLVSKFHA LYVMLNTYYE
     KLNSPTDSYV TCPKTKEQLW NVYKLFSLYF IDKHAGEFQQ FKILSPDQIS QVVQPRLLKL
     LPEIRKECIS LTDSFKWPDG MLNAPIGYYD GDIYHNYFNE VVKNNPVEKD GAGIPPYHEL
     LANMLTRGDE FARLGGANNA EILSKLTK