ID   ACOX2_ARATH             Reviewed;         692 AA.
AC   O65201; Q9FJQ4;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Acyl-coenzyme A oxidase 2, peroxisomal;
DE            Short=AOX 2;
DE            EC=1.3.3.6;
DE   AltName: Full=Long-chain acyl-CoA oxidase;
DE            Short=AtCX2;
DE   Flags: Precursor;
GN   Name=ACX2; OrderedLocusNames=At5g65110; ORFNames=MQN23.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP   AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX   MEDLINE=20040045; PubMed=10571860;
RX   DOI=10.1046/j.1365-313X.1999.00559.x;
RA   Hooks M.A., Kellas F., Graham I.A.;
RT   "Long-chain acyl-CoA oxidases of Arabidopsis.";
RL   Plant J. 20:1-13(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98403884; PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI.
RT   Sequence features of the regions of 1,367,185 bp covered by 19
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
RP   INDUCTION.
RX   PubMed=15141068; DOI=10.1104/pp.104.039925;
RA   Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.;
RT   "Gene-specific involvement of beta-oxidation in wound-activated
RT   responses in Arabidopsis.";
RL   Plant Physiol. 135:85-94(2004).
CC   -!- FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2-
CC       trans-enoyl-CoAs. Active on substrates longer than C14 and mostly
CC       with C18-CoA. Activity on long-chain mono-unsaturated substrates
CC       is double than with the corresponding saturated substrates.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA +
CC       H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.4 uM for C18:1-CoA;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences;
CC       Name=1;
CC         IsoId=O65201-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in flowers and young
CC       seedlings. Lower expression in roots, leaves and bracts.
CC   -!- DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day
CC       2 and then declines steadily until day 8.
CC   -!- INDUCTION: Induced by dehydration and abscisic acid (ABA).
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
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DR   EMBL; AF057043; AAC13497.1; -; mRNA.
DR   EMBL; AB013395; BAB11647.1; -; Genomic_DNA.
DR   IPI; IPI00542372; -.
DR   PIR; T52120; T52120.
DR   RefSeq; NP_201316.1; -.
DR   UniGene; At.49226; -.
DR   HSSP; P07872; 1IS2.
DR   PRIDE; O65201; -.
DR   GeneID; 836635; -.
DR   GenomeReviews; BA000015_GR; AT5G65110.
DR   NMPDR; fig|3702.1.peg.28589; -.
DR   GeneFarm; 4886; -.
DR   TAIR; At5g65110; -.
DR   OMA; O65201; RIWKDIG.
DR   BRENDA; 1.3.3.6; 302.
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; IDA:TAIR.
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; IDA:TAIR.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:TAIR.
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   Alternative splicing; Complete proteome; FAD; Fatty acid metabolism;
KW   Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome;
KW   Transit peptide.
FT   TRANSIT       1     49       Peroxisome (By similarity).
FT   CHAIN        50    692       Acyl-coenzyme A oxidase 2, peroxisomal.
FT                                /FTId=PRO_0000000555.
FT   NP_BIND     450    455       FAD.
FT   CONFLICT     37     37       P -> L (in Ref. 1; AAC13497).
SQ   SEQUENCE   692 AA;  77480 MW;  43B29F0E8D3176D7 CRC64;
     MESRREKNPM TEEESDGLIA ARRIQRLSLH LSPSLTPSPS LPLVQTETCS ARSKKLDVNG
     EALSLYMRGK HIDIQEKIFD FFNSRPDLQT PIEISKDDHR ELCMNQLIGL VREAGVRPFR
     YVADDPEKYF AIMEAVGSVD MSLGIKMGVQ YSLWGGSVIN LGTKKHRDKY FDGIDNLDYT
     GCFAMTELHH GSNVQGLQTT ATFDPLKDEF VIDTPNDGAI KWWIGNAAVH GKFATVFARL
     ILPTHDSKGV SDMGVHAFIV PIRDMKTHQT LPGVEIQDCG HKVGLNGVDN GALRFRSVRI
     PRDNLLNRFG DVSRDGTYTS SLPTINKRFG ATLGELVGGR VGLAYASVGV LKISATIAIR
     YSLLRQQFGP PKQPEVSILD YQSQQHKLMP MLASTYAYHF ATVYLVEKYS EMKKTHDEQL
     VADVHALSAG LKSYVTSYTA KALSVCREAC GGHGYAAVNR FGSLRNDHDI FQTFEGDNTV
     LLQQVAADLL KRYKEKFQGG TLTVTWSYLR ESMNTYLSQP NPVTARWEGE DHLRDPKFQL
     DAFRYRTSRL LQNVAARLQK HSKTLGGFGA WNRCLNHLLT LAESHIETVI LAKFIEAVKN
     CPDPSAKAAL KLACDLYALD RIWKDIGTYR NVDYVAPNKA KAIHKLTEYL SFQVRNVAKE
     LVDAFELPDH VTRAPIAMQS DAYSQYTQVV GF
//