ID   ACOX2_YARLI             Reviewed;         700 AA.
AC   O74935; Q6C248;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Acyl-coenzyme A oxidase 2;
DE            Short=Acyl-CoA oxidase 2;
DE            EC=1.3.3.6;
GN   Name=POX2; Synonyms=ACO2; OrderedLocusNames=YALI0F10857g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX   PubMed=12392712; DOI=10.1016/s0003-9861(02)00466-6;
RA   Luo Y.S., Nicaud J.-M., Van Veldhoven P.P., Chardot T.;
RT   "The acyl-CoA oxidases from the yeast Yarrowia lipolytica: characterization
RT   of Aox2p.";
RL   Arch. Biochem. Biophys. 407:32-38(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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).
RN   [3]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11815635; DOI=10.1083/jcb.200111075;
RA   Titorenko V.I., Nicaud J.-M., Wang H., Chan H., Rachubinski R.A.;
RT   "Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing
RT   complex into peroxisomes of Yarrowia lipolytica.";
RL   J. Cell Biol. 156:481-494(2002).
CC   -!- FUNCTION: Oxidizes strain chain acyl-CoAs with a chain length of 10 to
CC       14 carbons. Also active toward the 2S isomers of acyl-CoA-esters
CC       containing a 2-methyl group.
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: Heteropentamer composed of five different subunits.
CC       {ECO:0000269|PubMed:11815635}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11815635}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; AJ001300; CAA04660.1; -; Genomic_DNA.
DR   EMBL; CR382132; CAG78071.1; -; Genomic_DNA.
DR   RefSeq; XP_505264.1; XM_505264.1.
DR   AlphaFoldDB; O74935; -.
DR   SMR; O74935; -.
DR   STRING; 284591.O74935; -.
DR   EnsemblFungi; CAG78071; CAG78071; YALI0_F10857g.
DR   GeneID; 2907872; -.
DR   KEGG; yli:YALI0F10857g; -.
DR   VEuPathDB; FungiDB:YALI0_F10857g; -.
DR   HOGENOM; CLU_014629_3_1_1; -.
DR   InParanoid; O74935; -.
DR   OMA; VMPNIQI; -.
DR   OrthoDB; 5777at2759; -.
DR   BRENDA; 1.3.3.6; 1122.
DR   UniPathway; UPA00661; -.
DR   Proteomes; UP000001300; Chromosome F.
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; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
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_sf.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 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; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   1: Evidence at protein level;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW   Peroxisome; Reference proteome.
FT   CHAIN           1..700
FT                   /note="Acyl-coenzyme A oxidase 2"
FT                   /id="PRO_0000204702"
SQ   SEQUENCE   700 AA;  78691 MW;  434C97B8A7D71E3E CRC64;
     MNPNNTGTIE INGKEYNTFT EPPVAMAQER AKTSFPVREM TYFLDGGEKN TLKNEQIMEE
     IERDPLFNND NYYDLNKEQI RELTMERVAK LSLFVRDQPE DDIKKRFALI GIADMGTYTR
     LGVHYGLFFG AVRGTGTAEQ FGHWISKGAG DLRKFYGCFS MTELGHGSNL AGLETTAIYD
     EETDEFIINT PHIAATKWWI GGAAHTATHT VVFARLIVKG KDYGVKTFVV QLRNINDHSL
     KVGISIGDIG KKMGRDGIDN GWIQFTNVRI PRQNLLMKYT KVDREGNVTQ PPLAQLTYGS
     LITGRVSMAS DSHQVGKRFI TIALRYACIR RQFSTTPGQP ETKIIDYPYH QRRLLPLLAY
     VYALKMTADE VGALFSRTML KMDDLKPDDK AGLNEVVSDV KELFSVSAGL KAFSTWACAD
     VIDKTRQACG GHGYSGYNGF GQAYADWVVQ CTWEGDNNIL TLSAGRALIQ SAVALRKGEP
     VGNAVSYLKR YKDLANAKLN GRSLTDPKVL VEAWEVAAGN IINRATDQYE KLIGEGLNAD
     QAFEVLSQQR FQAAKVHTRR HLIAAFFSRI DTEAGEAIKQ PLLNLALLFA LWSIEEDSGL
     FLREGFLEPK DIDTVTELVN KYCTTVREEV IGYTDAFNLS DYFINAPIGC YDGDAYRHYF
     QKVNEQNPAR DPRPPYYAST LKPFLFREEE DDDICELDEE
//