ID   ACOX_ASHGO              Reviewed;         733 AA.
AC   Q756A9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Acyl-coenzyme A oxidase;
DE            Short=Acyl-CoA oxidase;
DE            EC=1.3.3.6;
GN   Name=POX1; OrderedLocusNames=AER358C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO C-TERMINUS.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS53038.2; -; Genomic_DNA.
DR   RefSeq; NP_985214.2; NM_210568.2.
DR   AlphaFoldDB; Q756A9; -.
DR   SMR; Q756A9; -.
DR   STRING; 33169.AAS53038; -.
DR   PRIDE; Q756A9; -.
DR   EnsemblFungi; AAS53038; AAS53038; AGOS_AER358C.
DR   GeneID; 4621430; -.
DR   KEGG; ago:AGOS_AER358C; -.
DR   eggNOG; KOG0136; Eukaryota.
DR   HOGENOM; CLU_014629_3_1_1; -.
DR   InParanoid; Q756A9; -.
DR   OMA; PMMRGKL; -.
DR   UniPathway; UPA00661; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR   GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..733
FT                   /note="Acyl-coenzyme A oxidase"
FT                   /id="PRO_0000204691"
SQ   SEQUENCE   733 AA;  81863 MW;  DD31D4E0419304C0 CRC64;
     MTKASVVDQS APAYAPKRLL AEARAASKVN IEQVFAFLEG SPEKAALTNE LLAEFAADPA
     ITQGPEYYDL TKAEQREQTV KKIARLALYL ENDIKLARKQ HHKDVVRDLQ SPDAPMVTMS
     DMERFEKRST LVALIDPQLA TRLGVNLSLF GNAVRGNGTD EQIKYWLQER GLIFVKGIYG
     CFAMTELGHG SNVANLQTRA TYDPASDSFV IQTPDLVATK WWIGGAAHSA THSTVYARLI
     VEGKDYGVKV FVVPLRNPKT MELLAGISIG DIGSKMGRDG IDNGWIQFNN VRIPREYMLS
     RFTKVIPGNP PKVEMEPLLD SISGYAALLS GRVSMVLDSY RFGARFSTIA TRYAFGRQQF
     GDPTNETQLI EYPLHQFRVL PQLAIIYMMA PGAMKLMDTY NSCLGELYGA GDDKKKLTTV
     SARMKDLFVE SASLKATCTW LTSTLIDELR QTCGGHGYSS YNGFGKAYND WVVQCTWEGD
     NNVLCLTSGK SLLKKFAGIV RGKKVTICDT SMDYLRMDYI QKVVMGGTKK VSNLSTLPDY
     YQIWSVILVK YLKRCAETVR DNNDPESVSK LLVSIAKFHA FYSMLQEFHR KLASDQSHVG
     DAATKEVLWK VYKLSSLYFI DKFSGEFQQL KVMSPDQMTN VQEQMLAILP EIKTHAIRLT
     DAFHLPDAVI NSSIGNYDGD IYHNYFNDVT RVAAKDKAPG VPPYADMLVN FLARGDQFDN
     LNISETSFKN LGK