Reviewed, UniProtKB/Swiss-Prot Q7KML2 (ACOX1_DROME)

Names and origin

Protein names

Recommended name:
    Probable peroxisomal acyl-coenzyme A oxidase 1
    EC=1.3.3.6

Gene names

ORF Names:

CG5009

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	669 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 + 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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro generation of precursor metabolites and energy Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW prostaglandin metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	peroxisome Inferred from sequence or structural similarity. Source: UniProtKB
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 sequence or structural similarity. Source: UniProtKB 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 – 669	669	Probable peroxisomal acyl-coenzyme A oxidase 1		PRO_0000348222
Regions
	Motif	667 – 669	3	Microbody targeting signal Potential
Sites
	Active site	434	1	Proton acceptor By similarity
	Binding site	152	1	FAD By similarity
	Binding site	191	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	544	1	Phosphotyrosine Ref.5
	Modified residue	551	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	191	1	G → C in AAL28144. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q7KML2-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 10DEE761437E92FE	FASTA	669	74,287
	10 20 30 40 50 60 MPAKPVNPDL QKERSTATFN PREFSVLWAG GEERFKEKKA LEKLFLEDPA LQDDLPISYL 70 80 90 100 110 120 SHKELYEHSL RKACIIGEKI RKLRADGEDG VDTYNALLGG SLGSAILKEG NPLALHYVMF 130 140 150 160 170 180 VPTIMGQGTM DQQVEWLSKA WDCEIIGTYA QTELGHGTFL RGLETRADYD ASTQEFVINT 190 200 210 220 230 240 PSLSAYKWWP GGLGHTANHA VVVAQLYTKG EFRGLAPFIV QLRDSDTHRP MPGIDIGDIG 250 260 270 280 290 300 TKLGMKGVNN GYLGLKNVRV PLNNMLMKNQ QVLPDGTYVA PKNSVLTYGT MMFVRCALIR 310 320 330 340 350 360 DTAQSLAKAS TIATRYSAVR RQSPIDPNQP EPQIMDHTTQ QLKLFPQIAK AIVFKTTGDG 370 380 390 400 410 420 IWNMYNVISG EIEQGNLDRL PEMHALSCCL KAICSADAAA GVETCRLSCG GHGYMDCSNF 430 440 450 460 470 480 PTIYGMTTAV CTYEGENTVM LLQTARYLVK VYGQALNGEK LVPTVSYISD AINQTKFVNF 490 500 510 520 530 540 DGSLRSIVKA FQFVAANKTR IAYEQIELRR KQGYGTEVAA NLCGTFLTAA ADLHGRAFLA 550 560 570 580 590 600 QTAYTELLAL SREVSPELAE VLKVVLELYL VDACLNRIGD FLRFIDLTDQ DVTKLEVRLE 610 620 630 640 650 660 NCLKRFRPNA VSLVDSFDLH DRVLDSALGA YDGNVYEHIF ESTKKNPLNK EPVNGAFHKY LKPFMKAHL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila complementary DNA resource." Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A. Science 287:2222-2224(2000) [PubMed: 10731138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-544 AND SER-551, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF57794.1. AF145642 mRNA. Translation: AAD38617.1. AY060596 mRNA. Translation: AAL28144.1.
RefSeq	NP_611264.2.
UniGene	Dm.3153
3D structure databases
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7KML2. 1 interaction.
Proteomic databases
PRIDE	Q7KML2.
Genome annotation databases
Ensembl	FBgn0027572. Drosophila melanogaster. [Contig view]
GeneID	37028.
KEGG	dme:Dmel_CG5009.
NMPDR	fig|7227.3.peg.6033.
Organism-specific databases
FlyBase	FBgn0027572. CG5009.
Phylogenomic databases
OMA	Q7KML2. VDITNER.
Family and domain databases
InterPro	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. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	801574.

Entry information

Entry name

ACOX1_DROME

Accession

Primary (citable) accession number: Q7KML2
Secondary accession number(s): Q95ST5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	October 3, 2006
Last modified:	June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project