Reviewed, UniProtKB/Swiss-Prot P13711 (ACOX_YEAST)

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
Synonyms:	FOX1
Ordered Locus Names:	YGL205W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
Cofactor	FAD.
Pathway	Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subunit structure	Homooctamer.
Subcellular location	Peroxisome.
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
PTM	Phosphoprotein
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38800	1	EBI-3999,EBI-24597
RPN3	P40016	1	EBI-3999,EBI-15927
TAF2	P23255	1	EBI-3999,EBI-18862

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 748	748	Acyl-coenzyme A oxidase		PRO_0000204704
Amino acid modifications
	Modified residue	6	1	Phosphothreonine Ref.4
	Modified residue	11	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	443	1	S → T in AAA34891. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13711-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 5C0664455A050BDA	FASTA	748	84,042
	10 20 30 40 50 60 MTRRTTINPD SVVLNPQKFI QKERADSKIK VDQVNTFLES SPERRTLTHA LIDQIVNDPI 70 80 90 100 110 120 LKTDTDYYDA KKMQEREITA KKIARLASYM EHDIKTVRKH FRDTDLMKEL QANDPDKASP 130 140 150 160 170 180 LTNKDLFIFD KRLSLVANID PQLGTRVGVH LGLFGNCIKG NGTDEQIRYW LQERGATLMK 190 200 210 220 230 240 GIYGCFAMTE LGHGSNVAQL QTRAVYDKQN DTFVIDTPDL TATKWWIGGA AHSATHAAVY 250 260 270 280 290 300 ARLIVEGKDY GVKTFVVPLR DPSTFQLLAG VSIGDIGAKM GRDGIDNGWI QFRNVVIPRE 310 320 330 340 350 360 FMLSRFTKVV RSPDGSVTVK TEPQLDQISG YSALLSGRVN MVMDSFRFGS KFATIAVRYA 370 380 390 400 410 420 VGRQQFAPRK GLSETQLIDY PLHQYRVLPQ LCVPYLVSPV AFKLMDNYYS TLDELYNASS 430 440 450 460 470 480 SAYKAALVTV SKKLKNLFID SASLKATNTW LIATLIDELR QTCGGHGYSQ YNGFGKGYDD 490 500 510 520 530 540 WVVQCTWEGD NNVLSLTSAK SILKKFIDSA TKGRFDNTLD VDSFSYLKPQ YIGSVVSGEI 550 560 570 580 590 600 KSGLKELGDY TEIWSITLIK LLAHIGTLVE KSRSIDSVSK LLVLVSKFHA LRCMLKTYYD 610 620 630 640 650 660 KLNSRDSHIS DEITKESMWN VYKLFSLYFI DKHSGEFQQF KIFTPDQISK VVQPQLLALL 670 680 690 700 710 720 PIVRKDCIGL TDSFELPDAM LNSPIGYFDG DIYHNYFNEV CRNNPVEADG AGKPSYHALL 730 740 SSMLGRGFEF DQKLGGAANA EILSKINK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and transcriptional control of the Saccharomyces cerevisiae POX1 gene encoding acyl-coenzyme A oxidase." Dmochowska A., Dignard D., Maleszka R., Thomas D.Y. Gene 88:247-252(1990) [PubMed: 2189786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII reveals 11 open reading frames: two correspond to new genes." Feuermann M., Simeonava L., Souciet J.-L., Potier S. Yeast 13:475-477(1997) [PubMed: 9153757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-327.
[4]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND SER-11, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27515 Genomic DNA. Translation: AAA34891.1. Z72727 Genomic DNA. Translation: CAA96918.1. Z72726 Genomic DNA. Translation: CAA96917.1.
PIR	S64224.
RefSeq	NP_011310.1.
3D structure databases
SMR	P13711. Positions 15-720.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6592N.
IntAct	P13711. 6 interactions.
STRING	P13711.
Proteomic databases
PeptideAtlas	P13711.
Genome annotation databases
Ensembl	YGL205W; YGL205W; YGL205W; Saccharomyces cerevisiae. [Genome view]
GeneID	852667.
KEGG	sce:YGL205W.
NMPDR	fig|4932.3.peg.2413.
Organism-specific databases
CYGD	YGL205w.
SGD	S000003173. POX1.
Phylogenomic databases
eggNOG	fuNOG06313.
HOGENOM	HBG737904.
OMA	ISGYSAL.
OrthoDB	EOG9908S4.
PhylomeDB	P13711.
Enzyme and pathway databases
BRENDA	1.3.3.6. 250.
Gene expression databases
ArrayExpress	P13711.
Genevestigator	P13711.
GermOnline	YGL205W. Saccharomyces cerevisiae.
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...
Other Resources
NextBio	971963.

Entry information

Entry name

ACOX_YEAST

Accession

Primary (citable) accession number: P13711

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 1, 1996
Last modified:	January 19, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)