ID ACOX5_CANTR Reviewed; 662 AA. AC P08790; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 68. DE RecName: Full=Acyl-coenzyme A oxidase 5; DE Short=Acyl-CoA oxidase 5; DE EC=1.3.3.6; DE AltName: Full=PXP-5; GN Name=POX5; OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=5482; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86149279; PubMed=3456583; DOI=10.1073/pnas.83.5.1232; RA Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.; RT "Two acyl-coenzyme A oxidases in peroxisomes of the yeast Candida RT tropicalis: primary structures deduced from genomic DNA sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1232-1236(1986). RN [2] RP SEQUENCE REVISION TO 265. RA Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + CC H(2)O(2). CC -!- COFACTOR: FAD. CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M12161; AAA34363.2; -; Genomic_DNA. DR PIR; B25123; OXCKX5. DR HSSP; P07872; 1IS2. DR BRENDA; 1.3.3.6; 1242. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_M. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR013764; AcylCoA_oxidase/DH_1/2_C. DR Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1. DR Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1. DR Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2. DR PANTHER; PTHR10909:SF11; Acyl-CoA_oxidase; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. PE 3: Inferred from homology; KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; KW Oxidoreductase; Peroxisome. FT INIT_MET 1 1 Removed. FT CHAIN 2 662 Acyl-coenzyme A oxidase 5. FT /FTId=PRO_0000204697. SQ SEQUENCE 662 AA; 74238 MW; 6746A72B6AD1986C CRC64; MPTELQKERE LTKFNPKELN YFLEGSQERS EIISNMVEQM QKDPILKVDA SYYNLTKDQQ REVTAKKIAR LSRYFEHEYP DQQAQRLSIL GVFDPQVFTR IGVNLGLFVS CVRGNGTNSQ FFYWTINKGI DKLRGIYGCF GMTELAHGSN VQGIETTATF DEDTDEFVIN TPHIGATKWW IGGAAHSATH CSVYARLKVK GKDYGVKTFV VPLRDSNHDL EPGVTVGDIG AKMGRDGIDN GWIQFSNVRI PRFFMLQKYC KVSRSGEVTM PPSEQLSYSA LIGGRVTMMM DSYRMTSRFI TIALRYAIHR RQFKKKDTDT IETKLIDYPL HQKRLFPFLA AAYLFSQGAL YLEQTMNATN DKLDEAVSAG EKEAIDAAIV ESKKLFVASG CLKSTCTWLT AEAIDEARQA CGGHGYSSYN GFGKAYSDWV VQCTWEGDNN ILAMNVAKPM VRDLLKEPEQ KGLVLSSVAD LDDPAKLVKA FDHALSGLAR DIGAVAEDKG FDITGPSLVL VSKLNAHRFL IDGFFKRITP EWSEVLRPLG FLYADWILTN FGATFLQYGI ITPDVSRKIS SEHFPALCAK VRPNVVGLTD GFNLTDMMTN AAIGRYDGNV YEHYFETVKA LNPPENTKAP YSKALEDMLN RPDLEVRERG EKSEEAAEIL SS //