Reviewed, UniProtKB/Swiss-Prot Q6FY63 (ACOX_CANGA)

Names and origin

Protein names

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

Gene names

Name:	POX1
Ordered Locus Names:	CAGL0A03740g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	FAD By similarity.
Pathway	Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subcellular location	Peroxisome By similarity.
Sequence similarities	Belongs to the acyl-CoA oxidase family.

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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 748	748	Acyl-coenzyme A oxidase		PRO_0000204692

Sequences

	Sequence		Length	Mass (Da)
	Q6FY63-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 0955D23455BFF665	FASTA	748	84,417
	10 20 30 40 50 60 MTKLSTVDPN ASVLNPQRFI QRERENCSID IDQVNTFLES DPRSRDLTHL IVDQLVNDPI 70 80 90 100 110 120 IKADSATYDQ TKLTQREVTV KKIARMALYM EQDIKTVRKH FRDTDLLKSL QDFGDTTTPP 130 140 150 160 170 180 LTNKDLAIFD KRLSLVANMD PQLSTRIGVH LGLFGNCIKG NGTDEQIKYW LQTRGAILIK 190 200 210 220 230 240 GIYGCFAMTE LGHGSNVAQL QTTATYDQES DTFIINTPDL AATKWWIGGA AHSATHTACY 250 260 270 280 290 300 ARLLVNGKDY GVKTFVVPLR DPSSLQLMPG IAIGDIGAKM GRDGIDNGWI QFRNVVIPRE 310 320 330 340 350 360 FMLSRFTKVH RNPGATPTVE VDPQLDQISG YSALLSGRVN MVMDSFRFGS KFATIATRYA 370 380 390 400 410 420 VGRQQFADKP GQPEKQLIDY PLHQYRVLPQ IVIPYIISPA AFSLLNFYYS TLDELYAASS 430 440 450 460 470 480 KNDKRALVVV SQKLKNLFID SASLKATNTW LVAQLIDELR QTCGGHGYSG YNAFGKGYND 490 500 510 520 530 540 WVVQCTWEGD NNILSLTSAK SILKKFVDSA TKGKYNKELD KRSFRYLDPQ FIRKVFTSSS 550 560 570 580 590 600 ENKLDDLYDY TNIWAVALLK LLRHIAKQVD STKDLDGASK LLVLVSKFHA LYVMLNTYYE 610 620 630 640 650 660 KLNSPTDSYV TCPKTKEQLW NVYKLFSLYF IDKHAGEFQQ FKILSPDQIS QVVQPRLLKL 670 680 690 700 710 720 LPEIRKECIS LTDSFKWPDG MLNAPIGYYD GDIYHNYFNE VVKNNPVEKD GAGIPPYHEL 730 740 LANMLTRGDE FARLGGANNA EILSKLTK

References

[1]

"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: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380947 Genomic DNA. Translation: CAG57823.1.
RefSeq	XP_444930.1.
3D structure databases
SMR	Q6FY63. Positions 14-721.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FY63.
Genome annotation databases
GeneID	2886280.
GenomeReviews	Gene locus CAGL0A03740g in contig CR380947_GR.
KEGG	cgr:CAGL0A03740g.
Phylogenomic databases
eggNOG	fuNOG06313.
HOGENOM	HBG737904.
OMA	ISGYSAL.
OrthoDB	EOG9908S4.
PhylomeDB	Q6FY63.
Enzyme and pathway databases
BRENDA	1.3.3.6. 189220.
Family and domain databases
InterPro	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. 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. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACOX_CANGA

Accession

Primary (citable) accession number: Q6FY63

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 19, 2004
Last modified:	January 19, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)