NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-81, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Kurokawa Amakuri Nankin;
TISSUE=Cotyledon;
DOI=10.1074/jbc.273.14.8301; PubMed=9525937 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi H., De Bellis L., Yamaguchi K., Kato A., Hayashi M., Nishimura M.;
"Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin.";
J. Biol. Chem. 273:8301-8307(1998).

Comments

FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2-trans-enoyl-CoAs.
CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD.
SUBCELLULAR LOCATION: Peroxisome. Glyoxysome.
DEVELOPMENTAL STAGE: Induced one day after germination with a peak at day 5 and then declines steadily until day 8.
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

AF002016; AAC15870.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

ModBase

O64894.

Ontologies

GO:0009514;	Cellular component: glyoxysome (inferred from electronic annotation from UniProtKB-KW).
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: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.

Other

ProtoNet

O64894.

UniRef

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

Keywords

Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein; Glyoxysome; Lipid metabolism; Oxidoreductase; Peroxisome; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 45`	`45`	`Peroxisome.`
`CHAIN`	`46 690`	`645`	`Acyl-coenzyme A oxidase, peroxisomal.`	`PRO_0000000556`
`NP_BIND`	`448 453`	`6`	`FAD (By similarity).`

Sequence information

Length: 690 AA [This is the length of the unprocessed precursor]

Molecular weight: 77319 Da [This is the MW of the unprocessed precursor]

CRC64: 430C843A757ABFC2 [This is a checksum on the sequence]

        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

O64894 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