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UniProtKB/Swiss-Prot entry O65202


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

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Entry information
Entry name ACOX1_ARATH
Primary accession number O65202
Secondary accession number O23518
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 67)
Name and origin of the protein
Protein name Peroxisomal acyl-coenzyme A oxidase 1
Synonyms AOX 1
EC 1.3.3.6
Long-chain acyl-CoA oxidase
AtCX1
Gene name
Name: ACX1
OrderedLocusNames: At4g16760
ORFNames: dl4405c, FCAALL.119
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND CHARACTERIZATION.
STRAIN=cv. Columbia;
TISSUE=Seedling hypocotyl;
DOI=10.1046/j.1365-313X.1999.00559.x; PubMed=10571860 [NCBI, ExPASy, EBI, Israel, Japan]
Hooks M.A., Kellas F., Graham I.A.;
"Long-chain acyl-CoA oxidases of Arabidopsis.";
Plant J. 20:1-13(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35140; PubMed=9461215 [NCBI, ExPASy, EBI, Israel, Japan]
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana.";
Nature 391:485-488(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
INDUCTION.
DOI=10.1104/pp.104.039925; PubMed=15141068 [NCBI, ExPASy, EBI, Israel, Japan]
Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.;
"Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis.";
Plant Physiol. 135:85-94(2004).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-659 OF MUTANT LEU-155.
DOI=10.1016/j.jmb.2004.10.062; PubMed=15581893 [NCBI, ExPASy, EBI, Israel, Japan]
Pedersen L., Henriksen A.;
"Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism.";
J. Mol. Biol. 345:487-500(2005).
Comments
  • FUNCTION: Catalyzes the desaturation of both long- and medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Most active with C14-CoA. Activity on long-chain mono-unsaturated substrates is 40% higher than with the corresponding saturated substrates. Seems to be an important factor in the general metabolism of root tips. May be involved in the biosynthesis of jasmonic acid.
  • CATALYTIC ACTIVITY: Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.
  • COFACTOR: Binds 1 FAD per subunit.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=5.3 µM for C14-CoA;
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Peroxisome (Probable).
  • TISSUE SPECIFICITY: Expressed mainly in flowers and young seedlings. Lower expression in roots, leaves and bracts.
  • DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak at day 2 and then declines to reach a basal level 4 days after sowing.
  • INDUCTION: Induced by dehydration, abscisic acid (ABA) and jasmonic acid (JA), and localy and systemically by wounding.
  • SIMILARITY: Belongs to the acyl-CoA oxidase family.
  • SEQUENCE CAUTION:
    • Sequence=CAB10450.1; Type=Erroneous gene model prediction;
    • Sequence=CAB78718.1; Type=Erroneous gene model prediction;
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
AF057044; AAC13498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97341; CAB10450.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161544; CAB78718.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY058849; AAL24237.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT001067; AAN46824.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H71434; H71434.
T52121; T52121.
3D structure databases
PDB
1W07; X-ray; 2.00 A; A/B=1-659.[ExPASy / RCSB / EBI]
PDBsum 1W07; -.
ModBase O65202.
Organism-specific databases
TAIR At4g16760; -.
Gene expression databases
GermOnline AT4G16760; Arabidopsis thaliana.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from InterPro).
GO:0003995; Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997; Molecular function: acyl-CoA oxidase activity (inferred from electronic annotation from InterPro).
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:0001676; Biological process: long-chain fatty acid metabolic process (inferred from mutant phenotype from TAIR).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046686; Biological process: response to cadmium ion (inferred from expression pattern from TAIR).
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.
Proteomics databases
PRIDE O65202; -.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G16760.
Other
ProtoNet O65202.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   664  664     Peroxisomal acyl-coenzyme A oxidase 1. PRO_0000204689
NP_BIND   399   404  6     FAD. 
MOTIF   662   664  3     Microbody targeting signal. 
DISULFID   467   576         
HELIX   8    11  4      
HELIX   18    26  9      
HELIX   29    43  15      
HELIX   46    48  3      
TURN   51    54  4      
HELIX   58    78  21      
HELIX   83    93  11      
HELIX   98   104  7      
HELIX   106   113  8      
HELIX   116   127  12      
STRAND   133   136  4      
STRAND   142   144  3      
HELIX   146   148  3      
STRAND   152   155  4      
TURN   157   159  3      
STRAND   160   165  6      
HELIX   169   171  3      
STRAND   172   174  3      
TURN   177   182  6      
STRAND   184   194  11      
STRAND   197   207  11      
TURN   211   213  3      
STRAND   220   224  5      
STRAND   228   232  5      
HELIX   233   236  4      
STRAND   240   250  11      
HELIX   251   253  3      
STRAND   257   261  5      
STRAND   267   269  3      
HELIX   274   276  3      
TURN   278   282  5      
HELIX   283   309  27      
HELIX   324   326  3      
HELIX   328   361  34      
TURN   362   365  4      
HELIX   370   397  28      
HELIX   398   404  7      
HELIX   406   408  3      
HELIX   410   417  8      
HELIX   418   421  4      
TURN   422   424  3      
HELIX   427   442  16      
TURN   443   447  5      
HELIX   453   460  8      
HELIX   461   464  4      
HELIX   474   478  5      
HELIX   480   502  23      
STRAND   505   507  3      
HELIX   508   514  7      
HELIX   516   538  23      
HELIX   548   566  19      
HELIX   568   573  6      
HELIX   579   596  18      
HELIX   597   599  3      
HELIX   600   605  6      
HELIX   611   614  4      
HELIX   626   635  10      
HELIX   637   640  4      
HELIX   647   650  4      
HELIX   652   655  4      
Sequence information
Length: 664 AA [This is the length of the unprocessed precursor] Molecular weight: 74302 Da [This is the MW of the unprocessed precursor] CRC64: 44AFD139D5434636 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEGIDHLADE RNKAEFDVED MKIVWAGSRH AFEVSDRIAR LVASDPVFEK SNRARLSRKE 

        70         80         90        100        110        120 
LFKSTLRKCA HAFKRIIELR LNEEEAGRLR HFIDQPAYVD LHWGMFVPAI KGQGTEEQQK 

       130        140        150        160        170        180 
KWLSLANKMQ IIGCYAQTEL GHGSNVQGLE TTATFDPKTD EFVIHTPTQT ASKWWPGGLG 

       190        200        210        220        230        240 
KVSTHAVVYA RLITNGKDYG IHGFIVQLRS LEDHSPLPNI TVGDIGTKMG NGAYNSMDNG 

       250        260        270        280        290        300 
FLMFDHVRIP RDQMLMRLSK VTREGEYVPS DVPKQLVYGT MVYVRQTIVA DASNALSRAV 

       310        320        330        340        350        360 
CIATRYSAVR RQFGAHNGGI ETQVIDYKTQ QNRLFPLLAS AYAFRFVGEW LKWLYTDVTE 

       370        380        390        400        410        420 
RLAASDFATL PEAHACTAGL KSLTTTATAD GIEECRKLCG GHGYLWCSGL PELFAVYVPA 

       430        440        450        460        470        480 
CTYEGDNVVL QLQVARFLMK TVAQLGSGKV PVGTTAYMGR AAHLLQCRSG VQKAEDWLNP 

       490        500        510        520        530        540 
DVVLEAFEAR ALRMAVTCAK NLSKFENQEQ GFQELLADLV EAAIAHCQLI VVSKFIAKLE 

       550        560        570        580        590        600 
QDIGGKGVKK QLNNLCYIYA LYLLHKHLGD FLSTNCITPK QASLANDQLR SLYTQVRPNA 

       610        620        630        640        650        660 
VALVDAFNYT DHYLNSVLGR YDGNVYPKLF EEALKDPLND SVVPDGYQEY LRPVLQQQLR 


TARL 

O65202 in FASTA format

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