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Reviewed, UniProtKB/Swiss-Prot O64894 (ACOX2_CUCMA)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifier3661 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids ICucurbitalesCucurbitaceaeCucurbita

Protein attributes

Sequence length690 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Peroxisome Ref.1
Chain46 – 690645Acyl-coenzyme A oxidase, peroxisomal
PRO_0000000556

Regions

Nucleotide binding448 – 4536FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
O64894-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 430C843A757ABFC2

FASTA69077,319
        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 

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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

AF002016 mRNA. Translation: AAC15870.1.

3D structure databases

HSSPHSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.3.6. 2176.

Family and domain databases

InterProIPR006090. 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]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACOX2_CUCMA
AccessionPrimary (citable) accession number: O64894
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents