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Reviewed, UniProtKB/Swiss-Prot P11356 (ACOX2_CANTR)

Last modified January 19, 2010. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2
      Short name=Acyl-CoA oxidase 2
    EC=1.3.3.6
Alternative name(s):
    PXP-2
Gene names
Name: POX2
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length724 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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 724723Acyl-coenzyme A oxidase 2
PRO_0000204695

Sequences

Sequence LengthMass (Da)Tools
P11356-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B2A145C5DDAF7379

FASTA72481,936
        10         20         30         40         50         60 
MAMLSQPNDG HDHPEKKDPD TTPKQVAGVI SSQDPPHPAK DVAEERARTD WDLKEMHEFL 

        70         80         90        100        110        120 
EGDEAKSEQI LRLYQSIERD PILQTRPEQF DYTQKQEREL VANRINQMTK FLETEPYGKF 

       130        140        150        160        170        180 
RRRLQLMTVI DPSLGIRMLV NIGLFLNCVR GNGTQKQFDF WSNKKEAGIV KQLYGCFGMT 

       190        200        210        220        230        240 
ELGHGSNVAG CETTATFDEK TDEFIIDTPH IGATKWWIGG AAHSATHTVC YARLIVKDVD 

       250        260        270        280        290        300 
YGVKTFIVPL RDSRHSLLPG IAIGDIGAKM GRQGVDNGWI QFTEVRVPRF FMLQRWCKVD 

       310        320        330        340        350        360 
RQGNVTLPPL EQLSYISLLE GRVGMATDSY RIGARYTTIA LRYAVGRRQF SKKAGEPETK 

       370        380        390        400        410        420 
LIDYTLHQRR LLPYLALTYA AAVGTDRLER QHEELLANLD IALAKKDKLL LKNTITGTKS 

       430        440        450        460        470        480 
MFVDSGSLKS TLTWLAADLI NETRQACGGH GYSSYNGFGK TYDDWVVQCT WEGDNNVLAM 

       490        500        510        520        530        540 
SAGKTIIKTV QQVLNGKELK DSTLEFLNAA PELSKAKKAV IRIRDHVDDV DRVLKAIAGL 

       550        560        570        580        590        600 
ISKFSKDLIP ISYQSWDSIG AQRVILSKLR CHYYLLETFN ERLNDKIKAK SPARPHLENI 

       610        620        630        640        650        660 
IKLYYVTNIL GPFIDEFLRF GVISPQVAKY ITYEYPQKLC ANIRPYVIGL TDSFQQPDNF 

       670        680        690        700        710        720 
INSLIGKYDG NIYTNYLESV KDVNDPSNYK APYSEALEAM LNRSALENRE RSERGKAAAD 


ILSK 

« Hide

References

[1]"Peroxisomal acyl-coenzyme A oxidase multigene family of the yeast Candida tropicalis; nucleotide sequence of a third gene and its protein product."
Okazaki K., Tan H., Fukui S., Kubota I., Kamiryo T.
Gene 58:37-44(1987) [PubMed: 3692174] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18259 Genomic DNA. Translation: AAA34361.1.
PIROXCKP2. A27331.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.3.6. 1242.

Family and domain databases

InterProIPR006091. 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.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[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.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACOX2_CANTR
AccessionPrimary (citable) accession number: P11356
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 63 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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