[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29; DOI=10.1002/(SICI)1097-0061(199811)14:15<1373::AID-YEA332>3.3.CO;2-T; PubMed=9848229 [NCBI, ExPASy, EBI, Israel, Japan] Wang H., Le Clainche A., le Dall M.-T., Wache Y., Pagot Y., Belin J.M., Gaillardin C., Nicaud J.-M.; "Cloning and characterization of the peroxisomal acyl CoA oxidase ACO3 gene from the alkane-utilizing yeast Yarrowia lipolytica."; Yeast 14:1373-1386(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CLIB 122 / E 150; DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Genome evolution in yeasts."; Nature 430:35-44(2004).
[3]	CHARACTERIZATION. DOI=10.1006/abbi.2000.2079; PubMed=11147819 [NCBI, ExPASy, EBI, Israel, Japan] Luo Y.S., Wang H.J., Gopalan K.V., Srivastava D.K., Nicaud J.-M., Chardot T.; "Purification and characterization of the recombinant form of Acyl CoA oxidase 3 from the yeast Yarrowia lipolytica."; Arch. Biochem. Biophys. 384:1-8(2000).
[4]	SUBUNIT, AND SUBCELLULAR LOCATION. DOI=10.1083/jcb.200111075; PubMed=11815635 [NCBI, ExPASy, EBI, Israel, Japan] Titorenko V.I., Nicaud J.-M., Wang H., Chan H., Rachubinski R.A.; "Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica."; J. Cell Biol. 156:481-494(2002).

Comments

FUNCTION: Oxidizes aliphatic acyl-CoA substrates of different chain lengths such as hexanoyl-CoA, decanoyl-CoA and myristyl-CoA as well as aromatic/heterocyclic ring-substituted chromogenic substrates, such as furylpropionyl-CoA. Of the above substrates, the efficiency of the enzyme, exhibits the following order: decanoyl-CoA > myristyl-CoA > hexanoyl-CoA > furyl-propionyl-CoA.
CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 7.4;
Temperature dependence: Optimum temperature is 23-38 degrees Celsius;
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation .
SUBUNIT: Heteropentamer composed of five different subunits.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the acyl-CoA oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ001301; CAA04661.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382130; CAG81448.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_503244.1; -.

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

ModBase

O74936.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from InterPro).
GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997;	Molecular function: acyl-CoA oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.

PANTHER

PTHR10909:SF11; Acyl-CoA_oxidase; 1.

Pfam

PF01756; ACOX; 1.
PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000168; Acyl-CoA_oxidase; 1.

Genome annotation databases

GeneID

2910308; -.

KEGG

yli:YALI0D24750g; -.

Phylogenomic databases

HOGENOM

O74936; -.

Other

ProtoNet

O74936.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 700`	`700`		`Acyl-coenzyme A oxidase 3.`	`PRO_0000204703`

Sequence information

Length: 700 AA [This is the length of the unprocessed precursor]

Molecular weight: 78010 Da [This is the MW of the unprocessed precursor]

CRC64: 864A89CF48161D5E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MISPNLTANV EIDGKQYNTF TEPPKALAGE RAKVKFPIKD MTEFLHGGEE NVTMIERLMT 

        70         80         90        100        110        120 
ELERDPVLNV SGDYDMPKEQ LRETAVARIA ALSGHWKKDT EKEALLRSQL HGIVDMGTRI 

       130        140        150        160        170        180 
RLGVHTGLFM GAIRGSGTKE QYDYWVRKGA ADVKGFYGCF AMTELGHGSN VAGLETTATY 

       190        200        210        220        230        240 
IQDTDEFIIN TPNTGATKWW IGGAAHSATH TACFARLLVD GKDYGVKIFV VQLRDVSSHS 

       250        260        270        280        290        300 
LMPGIALGDI GKKMGRDAID NGWIQFTNVR IPRQNMLMKY AKVSSTGKVS QPPLAQLTYG 

       310        320        330        340        350        360 
ALIGGRVTMI ADSFFVSQRF ITIALRYACV RRQFGTTPGQ PETKIIDYPY HQRRLLPLLA 

       370        380        390        400        410        420 
FTYAMKMAAD QSQIQYDQTT DLLQTIDPKD KGALGKAIVD LKELFASSAG LKAFTTWTCA 

       430        440        450        460        470        480 
NIIDQCRQAC GGHGYSGYNG FGQAYADWVV QCTWEGDNNV LCLSMGRGLI QSCLGHRKGK 

       490        500        510        520        530        540 
PLGSSVGYLA NKGLEQATLS GRDLKDPKVL IEAWEKVANG AIQRATDKFV ELTKGGLSPD 

       550        560        570        580        590        600 
QAFEELSQQR FQCAKIHTRK HLVTAFYERI NASAKADVKP YLINLANLFT LWSIEEDSGL 

       610        620        630        640        650        660 
FLREGFLQPK DIDQVTELVN HYCKEVRDQV AGYTDAFGLS DWFINAPIGN YDGDVYKHYF 

       670        680        690        700 
AKVNQQNPAQ NPRPPYYEST LRPFLFREDE DDDICELDEE

O74936 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools