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P05335 (ACOX4_CANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acyl-coenzyme A oxidase 4
Short name=AOX 4
Short name=Acyl-CoA oxidase 4
EC=1.3.3.6
Gene names
Name:POX4
OrganismCandida maltosa (Yeast)
Taxonomic identifier5479 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length709 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation

Inferred from electronic annotation. Source: InterPro

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

acyl-CoA oxidase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 709708Acyl-coenzyme A oxidase 4
PRO_0000204694

Sequences

Sequence LengthMass (Da)Tools
P05335 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7772A2E61D772D1A

FASTA70978,374
        10         20         30         40         50         60 
MTFTKKNVSV SQGPDPRTSI QTERANSKFD PVTMNYFLEG SKERSELMKS LAQQIERDPI 

        70         80         90        100        110        120 
LFTDGSYYDL TKDQQRELTV LKINRLSRYR EGDSVDTFNK RLSIMGVVDP QVATRIGVNL 

       130        140        150        160        170        180 
GLFLSCISGN GTAEQFKYWA IDKGTHNIQG LYGCFGMTEL GHGSNVAGVE TTATFDKETD 

       190        200        210        220        230        240 
EFVINTPHIG ATKWWIGGAA HSATHCSVYA RLVVDGKDYG VKTFVVPLRD SNHDLMPGVT 

       250        260        270        280        290        300 
VGDIGAKMGR DGIDNGWIQF SNVRIPRFFM LQKFCKVSAE GEVVLPPLEQ LSYSALLGGR 

       310        320        330        340        350        360 
VMMVLDSYRM LARVSTIALR YAIGRRQFKG DNVDQNDPNA LETQLIDYPL HQKRLFPYLA 

       370        380        390        400        410        420 
AAYVVSTGAL KVEHTIQSTL ATLDAAVENN DTTAIFKSID DMKSLFIDSG SLKATTTWLA 

       430        440        450        460        470        480 
AEAIDQCRQA CGGHGYSSYN GFAKAFNDWV VQCTWEGDNN VLSLSVGKPI IKQIIGIEDN 

       490        500        510        520        530        540 
GKTVRGSTAF LNQVKDFTGS NASKVVLNNT SDLNDINKVI KSIEVAIIRL AHEAAISVRK 

       550        560        570        580        590        600 
ESLDFAGAEL VQISKLKAHH YLLTEFVKRV GEFEHKELVP FLNTIGRLYS ATVVLDKFAG 

       610        620        630        640        650        660 
VFLTFNVASP QAITDLASTQ IPKLCAEVRP NVVAYTDSFQ QSDMVINSAI GKYDGDVYEN 

       670        680        690        700 
YFDLVKQLNP PKNTKAPYTA ALEGMLNRPS LEARERYEKS DETAAILSK

« Hide

References

[1]"Complete nucleotide sequence of the peroxisomal acyl CoA oxidase from the alkane-utilizing yeast Candida maltosa."
Hill D.E., Boulay R., Rogers D.
Nucleic Acids Res. 16:365-366(1988) [PubMed: 3340538] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20184.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X06721 Genomic DNA. Translation: CAA29901.1.
PIROXCKPM. A29441.

3D structure databases

ProteinModelPortalP05335.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006090. 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.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
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.
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNetSearch...

Entry information

Entry nameACOX4_CANMA
AccessionPrimary (citable) accession number: P05335
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: September 21, 2011
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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