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UniProtKB/Swiss-Prot entry Q7KML2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACOX1_DROME
Primary accession number Q7KML2
Secondary accession number Q95ST5
Integrated into Swiss-Prot on September 2, 2008
Sequence was last modified on October 3, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 30)
Name and origin of the protein
Protein name Probable peroxisomal acyl-coenzyme A oxidase 1
Synonym EC 1.3.3.6
Gene name
ORFNames: CG5009
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
DOI=10.1126/science.287.5461.2222; PubMed=10731138 [NCBI, ExPASy, EBI, Israel, Japan]
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.;
"A Drosophila complementary DNA resource.";
Science 287:2222-2224(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-544 AND SER-551, AND MASS SPECTROMETRY.
DOI=10.1039/b617545g; PubMed=17372656 [NCBI, ExPASy, EBI, Israel, Japan]
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE013599; AAF57794.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF145642; AAD38617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY060596; AAL28144.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_611264.2; -.
UniGene Dm.3153
3D structure databases
HSSP P07872; 1IS2. [HSSP ENTRY / PDB]
ModBase Q7KML2.
Protein-protein interaction databases
IntAct Q7KML2; -.
Organism-specific databases
FlyBase FBgn0027572; CG5009.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from sequence or structural similarity from UniProtKB).
GO:0003995; Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997; Molecular function: acyl-CoA oxidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635; Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0006091; Biological process: generation of precursor metabolites and energy (inferred from sequence or structural similarity from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006693; Biological process: prostaglandin metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.
PANTHER PTHR10909:SF11; Acyl-CoA_oxidase; 1.
Pfam PF01756; ACOX; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000168; Acyl-CoA_oxidase; 1.
ProtoNet Q7KML2.
Genome annotation databases
GeneID 37028; -.
KEGG dme:Dmel_CG5009; -.
NMPDR fig|7227.3.peg.6033; -.
Other
NextBio 801574; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   669  669     Probable peroxisomal acyl-coenzyme A oxidase 1. PRO_0000348222
MOTIF   667   669  3     Microbody targeting signal (Potential). 
MOD_RES   544   544        Phosphotyrosine. 
MOD_RES   551   551        Phosphoserine. 
CONFLICT   191   191        G -> C (in Ref. 4; AAL28144). 
Sequence information
Length: 669 AA [This is the length of the unprocessed precursor] Molecular weight: 74287 Da [This is the MW of the unprocessed precursor] CRC64: 10DEE761437E92FE [This is a checksum on the sequence]
        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 

Q7KML2 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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