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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //