Skip Header

Contribute Send feedback
Read comments (?) or add your own

O74935 (ACOX2_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A oxidase 2
Short name=Acyl-CoA oxidase 2
EC=1.3.3.6
Gene names
Name:POX2
Synonyms:ACO2
Ordered Locus Names:YALI0F10857g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia ›

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidizes strain chain acyl-CoAs with a chain length of 10 to 14 carbons. Also active toward the 2S isomers of acyl-CoA-esters containing a 2-methyl group.

Catalytic activity

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

Cofactor

FAD.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subunit structure

Heteropentamer composed of five different subunits. Ref.3

Subcellular location

Peroxisome Ref.3.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation using acyl-CoA oxidase

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 700700Acyl-coenzyme A oxidase 2
PRO_0000204702

Sequences

Sequence LengthMass (Da)Tools
O74935 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 434C97B8A7D71E3E

FASTA70078,691
        10         20         30         40         50         60 
MNPNNTGTIE INGKEYNTFT EPPVAMAQER AKTSFPVREM TYFLDGGEKN TLKNEQIMEE 

        70         80         90        100        110        120 
IERDPLFNND NYYDLNKEQI RELTMERVAK LSLFVRDQPE DDIKKRFALI GIADMGTYTR 

       130        140        150        160        170        180 
LGVHYGLFFG AVRGTGTAEQ FGHWISKGAG DLRKFYGCFS MTELGHGSNL AGLETTAIYD 

       190        200        210        220        230        240 
EETDEFIINT PHIAATKWWI GGAAHTATHT VVFARLIVKG KDYGVKTFVV QLRNINDHSL 

       250        260        270        280        290        300 
KVGISIGDIG KKMGRDGIDN GWIQFTNVRI PRQNLLMKYT KVDREGNVTQ PPLAQLTYGS 

       310        320        330        340        350        360 
LITGRVSMAS DSHQVGKRFI TIALRYACIR RQFSTTPGQP ETKIIDYPYH QRRLLPLLAY 

       370        380        390        400        410        420 
VYALKMTADE VGALFSRTML KMDDLKPDDK AGLNEVVSDV KELFSVSAGL KAFSTWACAD 

       430        440        450        460        470        480 
VIDKTRQACG GHGYSGYNGF GQAYADWVVQ CTWEGDNNIL TLSAGRALIQ SAVALRKGEP 

       490        500        510        520        530        540 
VGNAVSYLKR YKDLANAKLN GRSLTDPKVL VEAWEVAAGN IINRATDQYE KLIGEGLNAD 

       550        560        570        580        590        600 
QAFEVLSQQR FQAAKVHTRR HLIAAFFSRI DTEAGEAIKQ PLLNLALLFA LWSIEEDSGL 

       610        620        630        640        650        660 
FLREGFLEPK DIDTVTELVN KYCTTVREEV IGYTDAFNLS DYFINAPIGC YDGDAYRHYF 

       670        680        690        700 
QKVNEQNPAR DPRPPYYAST LKPFLFREEE DDDICELDEE

« Hide

References

« Hide 'large scale' references
[1]"The acyl-CoA oxidases from the yeast Yarrowia lipolytica: characterization of Aox2p."
Luo Y.S., Nicaud J.-M., Van Veldhoven P.P., Chardot T.
Arch. Biochem. Biophys. 407:32-38(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 20460 / W29 / CBS 7504 / IFP29.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIB 122 / E 150.
[3]"Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica."
Titorenko V.I., Nicaud J.-M., Wang H., Chan H., Rachubinski R.A.
J. Cell Biol. 156:481-494(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ001300 Genomic DNA. Translation: CAA04660.1.
CR382132 Genomic DNA. Translation: CAG78071.1.
RefSeqXP_505264.1. XM_505264.1.

3D structure databases

ProteinModelPortalO74935.
ModBaseSearch...

Protein-protein interaction databases

STRING4952.O74935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2907872.
KEGGyli:YALI0F10857g.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000181256.
KOK00232.
OMASARFITI.
OrthoDBEOG490BJ9.

Enzyme and pathway databases

UniPathwayUPA00661.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
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]
PANTHERPTHR10909:SF11. PTHR10909:SF11. 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.
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNetSearch...

Entry information

Entry nameACOX2_YARLI
AccessionPrimary (citable) accession number: O74935
Secondary accession number(s): Q6C248
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 82 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents