Reviewed, UniProtKB/Swiss-Prot O74936 (ACOX3_YARLI)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A oxidase 3
      Short name=Acyl-CoA oxidase 3
    EC=1.3.3.6

Gene names

Name:	POX3
Synonyms:	ACO3
Ordered Locus Names:	YALI0D24750g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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.
Pathway	Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subunit structure	Heteropentamer composed of five different subunits. Ref.4
Subcellular location	Peroxisome. Ref.4
Sequence similarities	Belongs to the acyl-CoA oxidase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.4. Temperature dependence: Optimum temperature is 23-38 degrees Celsius.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD 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 electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	Acyl-coenzyme A oxidase 3		PRO_0000204703

Sequences

	Sequence		Length	Mass (Da)
	O74936-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 864A89CF48161D5E	FASTA	700	78,010
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the peroxisomal acyl CoA oxidase ACO3 gene from the alkane-utilizing yeast Yarrowia lipolytica." Wang H., Le Clainche A., le Dall M.-T., Wache Y., Pagot Y., Belin J.M., Gaillardin C., Nicaud J.-M. Yeast 14:1373-1386(1998) [PubMed: 9848229] [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. , 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: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.
[3]	"Purification and characterization of the recombinant form of Acyl CoA oxidase 3 from the yeast Yarrowia lipolytica." Luo Y.S., Wang H.J., Gopalan K.V., Srivastava D.K., Nicaud J.-M., Chardot T. Arch. Biochem. Biophys. 384:1-8(2000) [PubMed: 11147819] [Abstract] Cited for: CHARACTERIZATION.
[4]	"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: 11815635] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ001301 Genomic DNA. Translation: CAA04661.1. CR382130 Genomic DNA. Translation: CAG81448.1.
RefSeq	XP_503244.1.
3D structure databases
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Genome annotation databases
GeneID	2910308.
KEGG	yli:YALI0D24750g.
Phylogenomic databases
HOGENOM	O74936.
OMA	O74936. EYERANT.
Enzyme and pathway databases
BRENDA	1.3.3.6. 3602.
Family and domain databases
InterPro	IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA: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.
PANTHER	PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
Pfam	PF01756. ACOX. 1 hit. PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACOX3_YARLI

Accession

Primary (citable) accession number: O74936
Secondary accession number(s): Q6C7W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)