ID ACOX2_CUCMA Reviewed; 690 AA. AC O64894; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=Acyl-coenzyme A oxidase, peroxisomal; DE Short=AOX; DE EC=1.3.3.6; DE AltName: Full=Long-chain acyl-CoA oxidase; DE Flags: Precursor; GN Name=Acx; OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-81, FUNCTION, RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RC STRAIN=cv. Kurokawa Amakuri Nankin; TISSUE=Cotyledon; RX MEDLINE=98192624; PubMed=9525937; DOI=10.1074/jbc.273.14.8301; RA Hayashi H., De Bellis L., Yamaguchi K., Kato A., Hayashi M., RA Nishimura M.; RT "Molecular characterization of a glyoxysomal long chain acyl-CoA RT oxidase that is synthesized as a precursor of higher molecular mass in RT pumpkin."; RL J. Biol. Chem. 273:8301-8307(1998). CC -!- FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2- CC trans-enoyl-CoAs. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + CC H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: Peroxisome. Glyoxysome. CC -!- DEVELOPMENTAL STAGE: Induced one day after germination with a peak CC at day 5 and then declines steadily until day 8. 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; AF002016; AAC15870.1; -; mRNA. DR HSSP; P07872; 1IS2. DR BRENDA; 1.3.3.6; 2176. DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell. 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; IPR006090; Acyl-CoA_Oxase/DH_1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_M. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. 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:1.20.140.10; AcylCoA_DH_1/2_C; 2. DR PANTHER; PTHR10909:SF11; Acyl-CoA_oxidase; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein; KW Glyoxysome; Lipid metabolism; Oxidoreductase; Peroxisome; KW Transit peptide. FT TRANSIT 1 45 Peroxisome. FT CHAIN 46 690 Acyl-coenzyme A oxidase, peroxisomal. FT /FTId=PRO_0000000556. FT NP_BIND 448 453 FAD (By similarity). SQ SEQUENCE 690 AA; 77319 MW; 430C843A757ABFC2 CRC64; MASPGEPNRT AEDESQAAAR RIERLSLHLT PIPLDDSQGV EMETCAAGKA KAKIEVDMGS LSLYMRGKHR EIQERVFEYF NSRPELQTPV GISMADHREL CMKQLVGLVR EAGIRPFRFV NEDPAKYFAI MEAVGSVDVS LAIKMGVQFS LWGGSVINLG TKKHRDRFFD GIDNVDYPGC FAMTELHHGS NVQGLQTTAT FDPITDEFII NTPNDGAIKW WIGNAAVHGK FATVFAKLVL PTHDSRKTAD MGVHAFIVPI RDLKSHKTLP GIEIHDCGHK VGLNGVDNGA LRFRSVRIPR DNLLNRFGEV SRDGKYKSSL PSINKRFAAT LGELVGGRVG LAYSSASVLK IASTIAIRYS LLRQQFGPPK QPEVSILDYQ SQQHKLMPML ASTYAFHFST MQLVEKYAQM KKTHDEELVG DVHALSAGLK AYVTSYTAKS LSTCREACGG HGYAVVNRFG TLRNDHDIFQ TFEGDNTVLL QQVAAYLLKQ YQEKFQGGTL AVTWNYLRES MNTYLSQPNP VTARWESADH LRDPKFQLDA FQYRTSRLLQ SVAVRLRKHT KNLGSFGAWN RCLNHLLTLA ESHIESVILA QFIESVQRCP NANTQATLKL VCDLYALDRI WNDIGTYRNV DYVAPNKAKA IHKLTEYLCF QVRNIAQELV DAFDLPDHVT RAPIAMKSNA YSQYTQYIGF //