Reviewed, UniProtKB/Swiss-Prot O64894 (ACOX2_CUCMA)

Names and origin

Protein names

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

Gene names

Name:

Acx

Organism

Cucurbita maxima (Pumpkin) (Winter squash)

Taxonomic identifier

3661 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucurbita

Protein attributes

Sequence length	690 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. Ref.1
Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	FAD.
Subcellular location	Peroxisome. Glyoxysome Ref.1.
Developmental stage	Induced one day after germination with a peak at day 5 and then declines steadily until day 8. Ref.1
Sequence similarities	Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Glyoxysome Peroxisome
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glyoxysome 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 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 45	45	Peroxisome Ref.1
	Chain	46 – 690	645	Acyl-coenzyme A oxidase, peroxisomal		PRO_0000000556
Regions
	Nucleotide binding	448 – 453	6	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O64894-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 430C843A757ABFC2	FASTA	690	77,319
	10 20 30 40 50 60 MASPGEPNRT AEDESQAAAR RIERLSLHLT PIPLDDSQGV EMETCAAGKA KAKIEVDMGS 70 80 90 100 110 120 LSLYMRGKHR EIQERVFEYF NSRPELQTPV GISMADHREL CMKQLVGLVR EAGIRPFRFV 130 140 150 160 170 180 NEDPAKYFAI MEAVGSVDVS LAIKMGVQFS LWGGSVINLG TKKHRDRFFD GIDNVDYPGC 190 200 210 220 230 240 FAMTELHHGS NVQGLQTTAT FDPITDEFII NTPNDGAIKW WIGNAAVHGK FATVFAKLVL 250 260 270 280 290 300 PTHDSRKTAD MGVHAFIVPI RDLKSHKTLP GIEIHDCGHK VGLNGVDNGA LRFRSVRIPR 310 320 330 340 350 360 DNLLNRFGEV SRDGKYKSSL PSINKRFAAT LGELVGGRVG LAYSSASVLK IASTIAIRYS 370 380 390 400 410 420 LLRQQFGPPK QPEVSILDYQ SQQHKLMPML ASTYAFHFST MQLVEKYAQM KKTHDEELVG 430 440 450 460 470 480 DVHALSAGLK AYVTSYTAKS LSTCREACGG HGYAVVNRFG TLRNDHDIFQ TFEGDNTVLL 490 500 510 520 530 540 QQVAAYLLKQ YQEKFQGGTL AVTWNYLRES MNTYLSQPNP VTARWESADH LRDPKFQLDA 550 560 570 580 590 600 FQYRTSRLLQ SVAVRLRKHT KNLGSFGAWN RCLNHLLTLA ESHIESVILA QFIESVQRCP 610 620 630 640 650 660 NANTQATLKL VCDLYALDRI WNDIGTYRNV DYVAPNKAKA IHKLTEYLCF QVRNIAQELV 670 680 690 DAFDLPDHVT RAPIAMKSNA YSQYTQYIGF

References

[1]

"Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin." Hayashi H., De Bellis L., Yamaguchi K., Kato A., Hayashi M., Nishimura M. J. Biol. Chem. 273:8301-8307(1998) [PubMed: 9525937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-81, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Strain: cv. Kurokawa Amakuri Nankin. Tissue: Cotyledon.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF002016 mRNA. Translation: AAC15870.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.3.6. 2176.
Family and domain databases
InterPro	IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR009075. AcylCo_DH/oxidase_C. IPR009100. AcylCoA_DH/oxidase. 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_CUCMA

Accession

Primary (citable) accession number: O64894

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	August 1, 1998
Last modified:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)