[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29; Le Clainche A., Nicaud J.-M.; Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[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]	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

CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD (By similarity).
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

AJ001299; CAA04659.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382131; CAG80307.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_504703.1; -.

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

ModBase

O74934.

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

2912003; -.

KEGG

yli:YALI0E32835g; -.

Phylogenomic databases

HOGENOM

O74934; -.

Other

ProtoNet

O74934.

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`	`1 689`	`689`		`Acyl-coenzyme A oxidase 1.`	`PRO_0000204701`

Sequence information

Length: 689 AA [This is the length of the unprocessed precursor]

Molecular weight: 77282 Da [This is the MW of the unprocessed precursor]

CRC64: 843D99D6DCEB4150 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTNTFTDPP VEMAKERGKT QFTVRDVTNF LNGGEEETQI VEKIMSSIER DPVLSVTADY 

        70         80         90        100        110        120 
DCNLQQARKQ TMERVAALSP YLVTDTEKLS LWRAQLHGMV DMSTRTRLSI HNNLFIGSIR 

       130        140        150        160        170        180 
GSGTPEQFKY WVKKGAVAVK QFYGCFAMTE LGHGSNLKGL ETTATYDQDS DQFIINTPHI 

       190        200        210        220        230        240 
GATKWWIGGA AHTSTHCVCF AKLIVHGKDY GTRNFVVPLR NVHDHSLKVG VSIGDIGKKM 

       250        260        270        280        290        300 
GRDGVDNGWI QFTNVRIPRQ NMLMRYAKVS DTGVVTKPAL DQLTYGALIR GRVSMIADSF 

       310        320        330        340        350        360 
HVSKRFLTIA LRYACVRRQF GTSGDTKETK IIDYPYHQRR LLPLLAYCYA MKMGADEAQK 

       370        380        390        400        410        420 
TWIETTDRIL ALNPNDPAQK NDLEKAVTDT KELFAASAGM KAFTTWGCAK IIDECRQACG 

       430        440        450        460        470        480 
GHGYSGYNGF GQGYADWVVQ CTWEGDNNVL CLSMGRGLVQ SALQILAGKH VGASIQYVGD 

       490        500        510        520        530        540 
KSKISQNGQG TPREQLLSPE FLVEAFRTAS RNNILRTTDK YQELVKTLNP DQAFEELSQQ 

       550        560        570        580        590        600 
RFQCARIHTR QHLISSFYAR IATAKDDIKP HLLKLANLFA LWSIEEDTGI FLRENILTPG 

       610        620        630        640        650        660 
DIDLINSLVD ELCVAVRDQV IGLTDAFGLS DFFINAPIGS YDGNVYEKYF AKVNQQNPAT 

       670        680 
NPRPPYYEST LKPFLFREEE DDEICDLDE

O74934 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