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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2).
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)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 748	748	Acyl-coenzyme A oxidase
Amino acid modifications
	Modified residue	6	1	Phosphothreonine
	Modified residue	11	1	Phosphoserine
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
EMBLGenBankDDBJ	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
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6592N.
IntAct	P13711.
Proteomic databases
PeptideAtlas	P13711.
Genome annotation databases
Ensembl	YGL205W. Saccharomyces cerevisiae. [Contig view]
GeneID	852667.
GenomeReviews	Gene locus YGL205W in contig Y13135_GR.
KEGG	sce:YGL205W.
NMPDR	fig|4932.3.peg.2413.
Organism-specific databases
CYGD	YGL205w.
SGD	S000003173. POX1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P13711.
Gene expression databases
ArrayExpress	P13711.
GermOnline	YGL205W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006091. Acyl-CoA_DHase/Oxase_M. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl_CoA_ox_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. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProDom	P13711. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P13711.
ProtoNet	Search...

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:	July 22, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)