[1]	NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND CHARACTERIZATION. STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl; DOI=10.1046/j.1365-313X.1999.00559.x; PubMed=10571860 [NCBI, ExPASy, EBI, Israel, Japan] Hooks M.A., Kellas F., Graham I.A.; "Long-chain acyl-CoA oxidases of Arabidopsis."; Plant J. 20:1-13(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/5.3.203; PubMed=9734815 [NCBI, ExPASy, EBI, Israel, Japan] Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."; DNA Res. 5:203-216(1998).
[3]	INDUCTION. DOI=10.1104/pp.104.039925; PubMed=15141068 [NCBI, ExPASy, EBI, Israel, Japan] Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.; "Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis."; Plant Physiol. 135:85-94(2004).

Comments

FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on substrates longer than C14 and mostly with C18-CoA. Activity on long-chain mono-unsaturated substrates is double than with the corresponding saturated substrates.
CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=4.4 µM for C18:1-CoA;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Peroxisome (Probable).
ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. A number of isoforms are produced. According to EST sequences.

Name 1

Isoform ID O65201-1

This is the isoform sequence displayed in this entry.
TISSUE SPECIFICITY: Expressed mainly in flowers and young seedlings. Lower expression in roots, leaves and bracts.
DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day 2 and then declines steadily until day 8.
INDUCTION: Induced by dehydration and abscisic acid (ABA).
SIMILARITY: Belongs to the acyl-CoA oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF057043; AAC13497.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB013395; BAB11647.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T52120; T52120.

NP_201316.1; -.

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

ModBase

O65201.

Organism-specific databases

GeneFarm

4886; -.

TAIR

At5g65110; -.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from InterPro).
GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997;	Molecular function: acyl-CoA oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0001676;	Biological process: long-chain fatty acid metabolic process (inferred from direct assay from TAIR).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.

PANTHER

PTHR10909:SF11; Acyl-CoA_oxidase; 1.

Pfam

PF01756; ACOX; 1.
PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000168; Acyl-CoA_oxidase; 1.

Proteomics databases

PRIDE

O65201; -.

Genome annotation databases

GeneID

836635; -.

GenomeReviews

BA000015_GR; AT5G65110.

NMPDR

fig|3702.1.peg.28589; -.

Other

ProtoNet

O65201.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 49`	`49`	`Peroxisome (By similarity).`
`CHAIN`	`50 692`	`643`	`Acyl-coenzyme A oxidase 2, peroxisomal.`	`PRO_0000000555`
`NP_BIND`	`450 455`	`6`	`FAD.`
`CONFLICT`	`37 37`		`P -> L (in Ref. 1; AAC13497).`

Sequence information

Length: 692 AA [This is the length of the unprocessed precursor]

Molecular weight: 77480 Da [This is the MW of the unprocessed precursor]

CRC64: 43B29F0E8D3176D7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MESRREKNPM TEEESDGLIA ARRIQRLSLH LSPSLTPSPS LPLVQTETCS ARSKKLDVNG 

        70         80         90        100        110        120 
EALSLYMRGK HIDIQEKIFD FFNSRPDLQT PIEISKDDHR ELCMNQLIGL VREAGVRPFR 

       130        140        150        160        170        180 
YVADDPEKYF AIMEAVGSVD MSLGIKMGVQ YSLWGGSVIN LGTKKHRDKY FDGIDNLDYT 

       190        200        210        220        230        240 
GCFAMTELHH GSNVQGLQTT ATFDPLKDEF VIDTPNDGAI KWWIGNAAVH GKFATVFARL 

       250        260        270        280        290        300 
ILPTHDSKGV SDMGVHAFIV PIRDMKTHQT LPGVEIQDCG HKVGLNGVDN GALRFRSVRI 

       310        320        330        340        350        360 
PRDNLLNRFG DVSRDGTYTS SLPTINKRFG ATLGELVGGR VGLAYASVGV LKISATIAIR 

       370        380        390        400        410        420 
YSLLRQQFGP PKQPEVSILD YQSQQHKLMP MLASTYAYHF ATVYLVEKYS EMKKTHDEQL 

       430        440        450        460        470        480 
VADVHALSAG LKSYVTSYTA KALSVCREAC GGHGYAAVNR FGSLRNDHDI FQTFEGDNTV 

       490        500        510        520        530        540 
LLQQVAADLL KRYKEKFQGG TLTVTWSYLR ESMNTYLSQP NPVTARWEGE DHLRDPKFQL 

       550        560        570        580        590        600 
DAFRYRTSRL LQNVAARLQK HSKTLGGFGA WNRCLNHLLT LAESHIETVI LAKFIEAVKN 

       610        620        630        640        650        660 
CPDPSAKAAL KLACDLYALD RIWKDIGTYR NVDYVAPNKA KAIHKLTEYL SFQVRNVAKE 

       670        680        690 
LVDAFELPDH VTRAPIAMQS DAYSQYTQVV GF

O65201 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools