ID   ACOX_PICPA              Reviewed;         719 AA.
AC   Q9Y7B1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Acyl-coenzyme A oxidase;
DE            Short=Acyl-CoA oxidase;
DE            EC=1.3.3.6;
GN   Name=POX1;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TARGETING
RP   SIGNAL.
RX   PubMed=10455228;
RX   DOI=10.1002/(sici)1097-0061(199908)15:11<1035::aid-yea432>3.0.co;2-1;
RA   Koller A., Spong A.P., Luers G.H., Subramani S.;
RT   "Analysis of the peroxisomal acyl-CoA oxidase gene product from Pichia
RT   pastoris and determination of its targeting signal.";
RL   Yeast 15:1035-1044(1999).
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:0000269|PubMed:10455228}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; AF133102; AAD31029.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y7B1; -.
DR   SMR; Q9Y7B1; -.
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   CHAIN           1..719
FT                   /note="Acyl-coenzyme A oxidase"
FT                   /id="PRO_0000204700"
FT   MOTIF           716..719
FT                   /note="Microbody targeting signal"
SQ   SEQUENCE   719 AA;  80519 MW;  252DC1E03BD978F0 CRC64;
     MFKIESIKSQ SPQVAIDKER KATKFDINKM FEFLESGKDE AALTKSLMQQ IERDTILKTN
     ASYYDLTKDQ HRELTAQKIA RLASYIEKDA PFFENFQKRL NLIAIVDPQL GTRVGVHLGL
     FLSAIRGNGT EEQFKYWAFE RGAAYLKDVY GCFGMTELAH GSNVAGLETT ATFDQKTKEF
     EINTPHLGAT KWWIGGAAHS ANHCVVYARL IVSGKDYGVK TFVVPIRDRN HNLHSGVAIG
     DIGAKMGRDG IDNGWIQLTN VRIPMNYMRS KFTKVTQRQE IVEVPPLEQL AYGALLGGRV
     TMVTDSFRMA QRFITIALRY SVGRRQFGAK NSSEELKLID YPLHQRRLLP YLALTYALSI
     SSFDLSQTYD SVLSNLDAAG KSQDFSKLGQ AIAGLKNLFC ASASLKSTAT WYVAQLIDEC
     RQACGGHGYS SYSGFGKAYN DWVVQCTWEG DNNILASNAG RLLCNLLSSC KKKEKKIKGD
     LSYLNGISNI DKEAICWNKQ SMTNLSNSNI DKELFCFNKQ VCTVKLINAI QGTIIRLGVR
     VPNIGSKKST WDDIAAQRVV LSKLNAVLYM LQHLVLKIKQ LGDEEAHKQY LVQIAALFAT
     SQIEMNFASY FLQFKAIDSL EPVADVVSEL CLSVRDQVIG LTDSFQFSDY FINSALGSHS
     GDIYNTYFDT VNNLNNPQVR DGKAAYSEAL EAMLRRDPLE VRECFEKSDK VLKKLAPKI