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P06598 (ACOX4_CANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 91. 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=Acyl-CoA oxidase 4
EC=1.3.3.6
Alternative name(s):
PXP-4
Peroxisomal fatty acyl-CoA oxidase
Gene names
Name:POX4
Synonyms:AOX
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [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 existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subunit structure

Homooctamer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Sequence caution

The sequence CAA68661.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA68662.1 differs from that shown. Reason: Erroneous initiation.

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
Chain2 – 709708Acyl-coenzyme A oxidase 4
PRO_0000204696

Experimental info

Sequence conflict2171Q → E in CAA68660. Ref.4
Sequence conflict2461P → A in AAA34362. Ref.3
Sequence conflict2461P → A in CAA68660. Ref.4
Sequence conflict3361N → K in AAA34362. Ref.3
Sequence conflict359 – 39436FVPPM…TTPRL → LAAAYVISAGALKVEDTIHN TLAELDAAVEKNDTKA in AAA34362. Ref.3
Sequence conflict359 – 39436FVPPM…TTPRL → LAAAYVISAGALKVEDTIHN TLAELDAAVEKNDTKA in CAA68660. Ref.4
Sequence conflict359 – 39436FVPPM…TTPRL → LAAAYVISAGALKVEDTIHN TLAELDAAVEKNDTKA in CAA68661. Ref.4
Sequence conflict4361H → Y in AAA34362. Ref.3
Sequence conflict4631G → A in AAA34362. Ref.3
Sequence conflict4961E → D in AAA34362. Ref.3
Sequence conflict577 – 5793ELA → DLV in AAA34362. Ref.3
Sequence conflict6981Q → E in AAA34362. Ref.3
Sequence conflict6981Q → E in CAA68660. Ref.4
Sequence conflict6981Q → E in CAA68661. Ref.4
Sequence conflict6981Q → E in CAA68662. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P06598 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0D60580353F5D927

FASTA70979,094
        10         20         30         40         50         60 
MTFTKKNVSV SQGPDPRSSI QKERDSSKWN PQQMNYFLEG SVERSELMKA LAQQMERDPI 

        70         80         90        100        110        120 
LFTDGSYYDL TKDQQRELTA VKINRIARYR EQESIDTFNK RLSLIGIFDP QVGTRIGVNL 

       130        140        150        160        170        180 
GLFLSCIRGN GTTSQLNYWA NEKETADVKG IYGCFGMTEL AHGSNVAGLE TTATFDKESD 

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

       250        260        270        280        290        300 
VGDIGPKMGR DGIDNGWIQF SNVRIPRFFM LQKFCKVSAE GEVTLPPLEQ LSYSALLGGR 

       310        320        330        340        350        360 
VMMVLDSYRM LARMSTIALR YAIGRRQFKG DNVDPNDPNA LETQLIDYPL HQKRLFPYFV 

       370        380        390        400        410        420 
PPMSSPSVPS RLNTPSRPPW SNWTSPLKRT TPRLIFKSID DMKSLFVDSG SLKSTATWLG 

       430        440        450        460        470        480 
AEAIDQCRQA CGGHGHSSYN GFGKAYNDWV VQCTWEGDNN VLGMSVGKPI VKQVISIEDA 

       490        500        510        520        530        540 
GKTVRGSTAF LNQLKEYTGS NSSKVVLNTV ADLDDIKTVI KAIEVAIIRL SQEAASIVKK 

       550        560        570        580        590        600 
ESFDYVGAEL VQLSKLKAHH YLLTEYIRRI DTFDQKELAP YLITLGKLYA ATIVLDRFAG 

       610        620        630        640        650        660 
VFLTFNVAST EAITALASVQ IPKLCAEVRP NVVAYTDSFQ QSDMIVNSAI GRYDGDIYEN 

       670        680        690        700 
YFDLVKLQNP PSKTKAPYSD ALEAMLNRPT LDERERFQKS DETAAILSK

« Hide

References

[1]"The primary structure of a peroxisomal fatty acyl-CoA oxidase from the yeast Candida tropicalis pK233."
Murray W.W., Rachubinski R.A.
Gene 51:119-128(1987) [PubMed: 3596241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20336 / pK233 / NCYC 997.
[2]Murray W.W., Rachubinski R.A.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 367; 381 AND 385.
[3]"Two acyl-coenzyme A oxidases in peroxisomes of the yeast Candida tropicalis: primary structures deduced from genomic DNA sequence."
Okazaki K., Takechi T., Kambara N., Fukui S., Kubota I., Kamiryo T.
Proc. Natl. Acad. Sci. U.S.A. 83:1232-1236(1986) [PubMed: 3456583] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20336 / pK233 / NCYC 997.
[4]"Import of the carboxy-terminal portion of acyl-CoA oxidase into peroxisomes of Candida tropicalis."
Small G.M., Lazarow P.B.
J. Cell Biol. 105:247-250(1987) [PubMed: 3611187] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-709.
Strain: RR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M16193 Genomic DNA. Translation: AAA34322.2.
M12160 Genomic DNA. Translation: AAA34362.1.
Y00623 mRNA. Translation: CAA68660.1.
Y00623 mRNA. Translation: CAA68661.1. Different initiation.
Y00623 mRNA. Translation: CAA68662.1. Different initiation.
PIROXCKX4. A25123.
OXCKAX. A28584.
OXCKX. A29047.

3D structure databases

ProteinModelPortalP06598.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
[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. 3 hits.
PfamPF01756. ACOX. 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_CANTR
AccessionPrimary (citable) accession number: P06598
Secondary accession number(s): P11355
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 21, 2011
This is version 91 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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