Reviewed, UniProtKB/Swiss-Prot O65201 (ACOX2_ARATH)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A oxidase 2, peroxisomal
      Short name=AOX 2
    EC=1.3.3.6
Alternative name(s):
    Long-chain acyl-CoA oxidase
      Short name=AtCX2

Gene names

Name:	ACX2
Ordered Locus Names:	At5g65110
ORF Names:	MQN23.4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Subunit structure	Homodimer.
Subcellular location	Peroxisome Probable.
Tissue specificity	Expressed mainly in flowers and young seedlings. Lower expression in roots, leaves and bracts. Ref.1
Developmental stage	Induced by seed imbibition with a peak at day 2 and then declines steadily until day 8. Ref.1
Induction	Induced by dehydration and abscisic acid (ABA). Ref.3
Sequence similarities	Belongs to the acyl-CoA oxidase family.
Biophysicochemical properties	Kinetic parameters: KM=4.4 µM for C18:1-CoA

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.1 Inferred from direct assay. Source: TAIR long-chain fatty acid metabolic process Ref.1 Inferred from direct assay. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro acyl-CoA oxidase activity Ref.1 Inferred from direct assay. Source: TAIR electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O65201-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 49	49	Peroxisome By similarity
	Chain	50 – 692	643	Acyl-coenzyme A oxidase 2, peroxisomal		PRO_0000000555
Regions
	Nucleotide binding	450 – 455	6	FAD
Experimental info
	Sequence conflict	37	1	P → L in AAC13497. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 43B29F0E8D3176D7	FASTA	692	77,480
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Long-chain acyl-CoA oxidases of Arabidopsis." Hooks M.A., Kellas F., Graham I.A. Plant J. 20:1-13(1999) [PubMed: 10571860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, CHARACTERIZATION. Strain: cv. Columbia. Tissue: Seedling hypocotyl.
[2]	"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." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed: 9734815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis." Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J. Plant Physiol. 135:85-94(2004) [PubMed: 15141068] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF057043 mRNA. Translation: AAC13497.1. AB013395 Genomic DNA. Translation: BAB11647.1.
IPI	IPI00542372.
PIR	T52120.
RefSeq	NP_201316.1.
UniGene	At.49226
3D structure databases
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Proteomic databases
PRIDE	O65201.
Genome annotation databases
GeneID	836635.
GenomeReviews	Gene locus AT5G65110 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.28589.
Organism-specific databases
GeneFarm	4886.
TAIR	At5g65110.
Phylogenomic databases
OMA	O65201. RIWKDIG.
Enzyme and pathway databases
BRENDA	1.3.3.6. 302.
Family and domain databases
InterPro	IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHER	PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
Pfam	PF01756. ACOX. 1 hit. PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACOX2_ARATH

Accession

Primary (citable) accession number: O65201
Secondary accession number(s): Q9FJQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)