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Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

ACX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactori

FADNote: Binds 1 FAD per subunit.

Kineticsi

  1. KM=5.3 µM for C14-CoA

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei138 – 1381FADBy similarity
    Binding sitei177 – 1771FAD; via amide nitrogenBy similarity
    Active sitei424 – 4241Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi399 – 4046FAD

    GO - Molecular functioni

    GO - Biological processi

    • fatty acid beta-oxidation Source: TAIR
    • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: GO_Central
    • jasmonic acid biosynthetic process Source: TAIR
    • lipid homeostasis Source: GO_Central
    • long-chain fatty acid metabolic process Source: TAIR
    • response to cadmium ion Source: TAIR
    • response to fungus Source: TAIR
    • response to wounding Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciARA:GQT-2375-MONOMER.
    MetaCyc:AT4G16760-MONOMER.
    BRENDAi1.3.3.6. 399.
    ReactomeiR-ATH-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-ATH-2046106. alpha-linolenic acid (ALA) metabolism.
    R-ATH-389887. Beta-oxidation of pristanoyl-CoA.
    R-ATH-390247. Beta-oxidation of very long chain fatty acids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal acyl-coenzyme A oxidase 1 (EC:1.3.3.6)
    Short name:
    AOX 1
    Alternative name(s):
    Long-chain acyl-CoA oxidase
    Short name:
    AtCX1
    Gene namesi
    Name:ACX1
    Ordered Locus Names:At4g16760
    ORF Names:dl4405c, FCAALL.119
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G16760.

    Subcellular locationi

    GO - Cellular componenti

    • peroxisome Source: TAIR
    • plasmodesma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 664664Peroxisomal acyl-coenzyme A oxidase 1PRO_0000204689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi467 ↔ 576

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiO65202.
    PRIDEiO65202.

    Expressioni

    Tissue specificityi

    Expressed mainly in flowers and young seedlings. Lower expression in roots, leaves and bracts.1 Publication

    Developmental stagei

    Induced by seed imbibition with a peak at day 2 and then declines to reach a basal level 4 days after sowing.1 Publication

    Inductioni

    Induced by dehydration, abscisic acid (ABA) and jasmonic acid (JA), and localy and systemically by wounding.1 Publication

    Gene expression databases

    ExpressionAtlasiO65202. baseline and differential.
    GenevisibleiO65202. AT.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi12674. 5 interactions.
    IntActiO65202. 2 interactions.
    STRINGi3702.AT4G16760.1.

    Structurei

    Secondary structure

    1
    664
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Helixi18 – 269Combined sources
    Helixi29 – 4315Combined sources
    Helixi46 – 483Combined sources
    Turni51 – 544Combined sources
    Helixi58 – 7821Combined sources
    Helixi83 – 9311Combined sources
    Helixi98 – 1047Combined sources
    Helixi106 – 1138Combined sources
    Helixi116 – 12712Combined sources
    Beta strandi133 – 1364Combined sources
    Beta strandi142 – 1443Combined sources
    Helixi146 – 1483Combined sources
    Beta strandi152 – 1543Combined sources
    Turni157 – 1593Combined sources
    Beta strandi160 – 1656Combined sources
    Helixi169 – 1713Combined sources
    Beta strandi172 – 1743Combined sources
    Turni177 – 1826Combined sources
    Beta strandi184 – 19411Combined sources
    Beta strandi197 – 20711Combined sources
    Turni211 – 2133Combined sources
    Beta strandi220 – 2245Combined sources
    Beta strandi228 – 2325Combined sources
    Helixi233 – 2364Combined sources
    Beta strandi240 – 25011Combined sources
    Helixi251 – 2533Combined sources
    Beta strandi257 – 2615Combined sources
    Beta strandi267 – 2693Combined sources
    Helixi274 – 2763Combined sources
    Turni278 – 2825Combined sources
    Helixi283 – 30927Combined sources
    Helixi324 – 3263Combined sources
    Helixi328 – 36134Combined sources
    Turni362 – 3654Combined sources
    Helixi370 – 39728Combined sources
    Helixi398 – 4047Combined sources
    Helixi406 – 4083Combined sources
    Helixi410 – 4178Combined sources
    Helixi418 – 4214Combined sources
    Turni422 – 4243Combined sources
    Helixi427 – 44216Combined sources
    Turni443 – 4475Combined sources
    Helixi453 – 4608Combined sources
    Helixi461 – 4644Combined sources
    Helixi474 – 4785Combined sources
    Helixi480 – 50223Combined sources
    Beta strandi505 – 5073Combined sources
    Helixi508 – 5147Combined sources
    Helixi516 – 53823Combined sources
    Helixi548 – 56619Combined sources
    Helixi568 – 5736Combined sources
    Helixi579 – 59618Combined sources
    Helixi597 – 5993Combined sources
    Helixi600 – 6056Combined sources
    Helixi611 – 6144Combined sources
    Helixi626 – 63510Combined sources
    Helixi637 – 6404Combined sources
    Helixi647 – 6504Combined sources
    Helixi652 – 6554Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W07X-ray2.00A/B1-659[»]
    ProteinModelPortaliO65202.
    SMRiO65202. Positions 2-659.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO65202.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi662 – 6643Microbody targeting signal

    Sequence similaritiesi

    Belongs to the acyl-CoA oxidase family.Curated

    Phylogenomic databases

    eggNOGiKOG0136. Eukaryota.
    COG1960. LUCA.
    HOGENOMiHOG000181256.
    InParanoidiO65202.
    KOiK00232.
    OMAiDFAVWWA.
    OrthoDBiEOG093603O2.
    PhylomeDBiO65202.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR029320. Acyl-CoA_ox_N.
    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_NM_dom.
    [Graphical view]
    PfamiPF01756. ACOX. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF14749. Acyl-CoA_ox_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMiSSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

    Note: A number of isoforms are produced. According to EST sequences.
    Isoform 1 (identifier: O65202-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MEGIDHLADE RNKAEFDVED MKIVWAGSRH AFEVSDRIAR LVASDPVFEK
    60 70 80 90 100
    SNRARLSRKE LFKSTLRKCA HAFKRIIELR LNEEEAGRLR HFIDQPAYVD
    110 120 130 140 150
    LHWGMFVPAI KGQGTEEQQK KWLSLANKMQ IIGCYAQTEL GHGSNVQGLE
    160 170 180 190 200
    TTATFDPKTD EFVIHTPTQT ASKWWPGGLG KVSTHAVVYA RLITNGKDYG
    210 220 230 240 250
    IHGFIVQLRS LEDHSPLPNI TVGDIGTKMG NGAYNSMDNG FLMFDHVRIP
    260 270 280 290 300
    RDQMLMRLSK VTREGEYVPS DVPKQLVYGT MVYVRQTIVA DASNALSRAV
    310 320 330 340 350
    CIATRYSAVR RQFGAHNGGI ETQVIDYKTQ QNRLFPLLAS AYAFRFVGEW
    360 370 380 390 400
    LKWLYTDVTE RLAASDFATL PEAHACTAGL KSLTTTATAD GIEECRKLCG
    410 420 430 440 450
    GHGYLWCSGL PELFAVYVPA CTYEGDNVVL QLQVARFLMK TVAQLGSGKV
    460 470 480 490 500
    PVGTTAYMGR AAHLLQCRSG VQKAEDWLNP DVVLEAFEAR ALRMAVTCAK
    510 520 530 540 550
    NLSKFENQEQ GFQELLADLV EAAIAHCQLI VVSKFIAKLE QDIGGKGVKK
    560 570 580 590 600
    QLNNLCYIYA LYLLHKHLGD FLSTNCITPK QASLANDQLR SLYTQVRPNA
    610 620 630 640 650
    VALVDAFNYT DHYLNSVLGR YDGNVYPKLF EEALKDPLND SVVPDGYQEY
    660
    LRPVLQQQLR TARL
    Length:664
    Mass (Da):74,302
    Last modified:August 1, 1998 - v1
    Checksum:i44AFD139D5434636
    GO

    Sequence cautioni

    The sequence CAB10450 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence CAB78718 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF057044 mRNA. Translation: AAC13498.1.
    Z97341 Genomic DNA. Translation: CAB10450.1. Sequence problems.
    AL161544 Genomic DNA. Translation: CAB78718.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE83798.1.
    AY058849 mRNA. Translation: AAL24237.1.
    BT001067 mRNA. Translation: AAN46824.1.
    PIRiH71434.
    T52121.
    RefSeqiNP_567513.4. NM_117778.7. [O65202-1]
    UniGeneiAt.20864.

    Genome annotation databases

    EnsemblPlantsiAT4G16760.1; AT4G16760.1; AT4G16760. [O65202-1]
    GeneIDi827381.
    KEGGiath:AT4G16760.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF057044 mRNA. Translation: AAC13498.1.
    Z97341 Genomic DNA. Translation: CAB10450.1. Sequence problems.
    AL161544 Genomic DNA. Translation: CAB78718.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE83798.1.
    AY058849 mRNA. Translation: AAL24237.1.
    BT001067 mRNA. Translation: AAN46824.1.
    PIRiH71434.
    T52121.
    RefSeqiNP_567513.4. NM_117778.7. [O65202-1]
    UniGeneiAt.20864.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W07X-ray2.00A/B1-659[»]
    ProteinModelPortaliO65202.
    SMRiO65202. Positions 2-659.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi12674. 5 interactions.
    IntActiO65202. 2 interactions.
    STRINGi3702.AT4G16760.1.

    Proteomic databases

    PaxDbiO65202.
    PRIDEiO65202.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G16760.1; AT4G16760.1; AT4G16760. [O65202-1]
    GeneIDi827381.
    KEGGiath:AT4G16760.

    Organism-specific databases

    TAIRiAT4G16760.

    Phylogenomic databases

    eggNOGiKOG0136. Eukaryota.
    COG1960. LUCA.
    HOGENOMiHOG000181256.
    InParanoidiO65202.
    KOiK00232.
    OMAiDFAVWWA.
    OrthoDBiEOG093603O2.
    PhylomeDBiO65202.

    Enzyme and pathway databases

    BioCyciARA:GQT-2375-MONOMER.
    MetaCyc:AT4G16760-MONOMER.
    BRENDAi1.3.3.6. 399.
    ReactomeiR-ATH-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-ATH-2046106. alpha-linolenic acid (ALA) metabolism.
    R-ATH-389887. Beta-oxidation of pristanoyl-CoA.
    R-ATH-390247. Beta-oxidation of very long chain fatty acids.

    Miscellaneous databases

    EvolutionaryTraceiO65202.
    PROiO65202.

    Gene expression databases

    ExpressionAtlasiO65202. baseline and differential.
    GenevisibleiO65202. AT.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR029320. Acyl-CoA_ox_N.
    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_NM_dom.
    [Graphical view]
    PfamiPF01756. ACOX. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF14749. Acyl-CoA_ox_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMiSSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACOX1_ARATH
    AccessioniPrimary (citable) accession number: O65202
    Secondary accession number(s): O23518
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: August 1, 1998
    Last modified: September 7, 2016
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.