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Protein

Acyl-coenzyme A oxidase 3, peroxisomal

Gene

ACX3

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 medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on C8:0- to C14:0-CoA with a maximal activity on C12:0-CoA.

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=3.7 µM for lauroyl-CoA

    pH dependencei

    Optimum pH is 8.5-9.0.

    Pathwayi: peroxisomal fatty acid beta-oxidation

    This protein is involved in the pathway peroxisomal fatty acid beta-oxidation, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway peroxisomal fatty acid beta-oxidation and in Lipid metabolism.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi442 – 45716FADSequence analysisAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    • fatty acid beta-oxidation Source: TAIR
    • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: GO_Central
    • fatty acid beta-oxidation using acyl-CoA oxidase Source: UniProtKB-UniPathway
    • lipid homeostasis Source: GO_Central
    • medium-chain fatty acid metabolic process 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

    BioCyciMetaCyc:AT1G06290-MONOMER.
    BRENDAi1.3.3.6. 399.
    ReactomeiR-ATH-389887. Beta-oxidation of pristanoyl-CoA.
    UniPathwayiUPA00661.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A oxidase 3, peroxisomal (EC:1.3.3.6)
    Short name:
    AOX 3
    Short name:
    Acyl-CoA oxidase 3
    Alternative name(s):
    Medium-chain acyl-CoA oxidase
    Short name:
    AtCX3
    Gene namesi
    Name:ACX3
    Ordered Locus Names:At1g06290, At1g06300
    ORF Names:F9P14.15, F9P14_11, T2D23.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G06290.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434PeroxisomeSequence analysisAdd
    BLAST
    Chaini35 – 675641Acyl-coenzyme A oxidase 3, peroxisomalPRO_0000000557Add
    BLAST

    Proteomic databases

    PaxDbiP0CZ23.
    PRIDEiP0CZ23.

    Expressioni

    Tissue specificityi

    Most abundant in flowers and senescing rosette leaves. Lower expression in hypocotyls, stems, young rosette leaves, cotyledons, cauline leaves and root tip of young seedlings.2 Publications

    Developmental stagei

    Induced by seed imbibition with a peak at day 2 and then declines steadily until day 7. Not detected in developing seeds. Constitutive expression in root axis.1 Publication

    Inductioni

    Not induced by dehydration or abscisic acid (ABA).1 Publication

    Gene expression databases

    GenevisibleiP0CZ23. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi22381. 2 interactions.
    IntActiP0CZ23. 1 interaction.
    STRINGi3702.AT1G06290.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP0CZ23.
    SMRiP0CZ23. Positions 78-662.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl-CoA oxidase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG0135. Eukaryota.
    COG1960. LUCA.
    HOGENOMiHOG000245077.
    InParanoidiP0CZ23.
    KOiK00232.
    OMAiCPVIPSQ.
    PhylomeDBiP0CZ23.

    Family and domain databases

    InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR012258. Acyl-CoA_oxidase.
    IPR002655. Acyl-CoA_oxidase_C.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF01756. ACOX. 1 hit.
    PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMiSSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0CZ23-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSDNRALRRA HVLANHILQS NPPSSNPSLS RELCLQYSPP ELNESYGFDV
    60 70 80 90 100
    KEMRKLLDGH NVVDRDWIYG LMMQSNLFNR KERGGKIFVS PDYNQTMEQQ
    110 120 130 140 150
    REITMKRIWY LLENGVFKGW LTETGPEAEL RKLALLEVCG IYDHSVSIKV
    160 170 180 190 200
    GVHFFLWGNA VKFFGTKRHH EKWLKNTEDY VVKGCFAMTE LGHGSNVRGI
    210 220 230 240 250
    ETVTTYDPKT EEFVINTPCE SAQKYWIGGA ANHATHTIVF SQLHINGTNQ
    260 270 280 290 300
    GVHAFIAQIR DQDGSICPNI RIADCGHKIG LNGVDNGRIW FDNLRIPREN
    310 320 330 340 350
    LLNAVADVSS DGKYVSSIKD PDQRFGAFMA PLTSGRVTIA SSAIYSAKVG
    360 370 380 390 400
    LSIAIRYSLS RRAFSVTANG PEVLLLDYPS HQRRLLPLLA KTYAMSFAAN
    410 420 430 440 450
    ELKMIYVKRT PETNKAIHVV SSGFKAVLTW HNMHTLQECR EAVGGQGVKT
    460 470 480 490 500
    ENLVGQLKGE FDVQTTFEGD NNVLMQQVSK ALFAEYVSCK KRNKPFKGLG
    510 520 530 540 550
    LEHMNSPRPV LPTQLTSSTL RCSQFQTNVF CLRERDLLEQ FTSEVAQLQG
    560 570 580 590 600
    RGESREFSFL LSHQLAEDLG KAFTEKAILQ TILDAEAKLP TGSVKDVLGL
    610 620 630 640 650
    VRSMYALISL EEDPSLLRYG YLSQDNVGDV RREVSKLCGE LRPHALALVT
    660 670
    SFGIPDSFLS PIAFNWVEAN AWSSV
    Length:675
    Mass (Da):75,676
    Last modified:July 27, 2011 - v1
    Checksum:iFABBCBA01C5FC103
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331L → V in AAF73843 (PubMed:10859203).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF207994 mRNA. Translation: AAF73843.1.
    AF253474 mRNA. Translation: AAF76137.1.
    AC068143 Genomic DNA. Translation: AAF82159.1.
    CP002684 Genomic DNA. Translation: AEE27972.1.
    AY099579 mRNA. Translation: AAM20431.1.
    BT008413 mRNA. Translation: AAP37772.1.
    AK176257 mRNA. Translation: BAD44020.1.
    PIRiG86198.
    RefSeqiNP_172119.1. NM_100511.2.
    UniGeneiAt.14938.

    Genome annotation databases

    EnsemblPlantsiAT1G06290.1; AT1G06290.1; AT1G06290.
    GeneIDi837140.
    GrameneiAT1G06290.1; AT1G06290.1; AT1G06290.
    KEGGiath:AT1G06290.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF207994 mRNA. Translation: AAF73843.1.
    AF253474 mRNA. Translation: AAF76137.1.
    AC068143 Genomic DNA. Translation: AAF82159.1.
    CP002684 Genomic DNA. Translation: AEE27972.1.
    AY099579 mRNA. Translation: AAM20431.1.
    BT008413 mRNA. Translation: AAP37772.1.
    AK176257 mRNA. Translation: BAD44020.1.
    PIRiG86198.
    RefSeqiNP_172119.1. NM_100511.2.
    UniGeneiAt.14938.

    3D structure databases

    ProteinModelPortaliP0CZ23.
    SMRiP0CZ23. Positions 78-662.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi22381. 2 interactions.
    IntActiP0CZ23. 1 interaction.
    STRINGi3702.AT1G06290.1.

    Proteomic databases

    PaxDbiP0CZ23.
    PRIDEiP0CZ23.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G06290.1; AT1G06290.1; AT1G06290.
    GeneIDi837140.
    GrameneiAT1G06290.1; AT1G06290.1; AT1G06290.
    KEGGiath:AT1G06290.

    Organism-specific databases

    TAIRiAT1G06290.

    Phylogenomic databases

    eggNOGiKOG0135. Eukaryota.
    COG1960. LUCA.
    HOGENOMiHOG000245077.
    InParanoidiP0CZ23.
    KOiK00232.
    OMAiCPVIPSQ.
    PhylomeDBiP0CZ23.

    Enzyme and pathway databases

    UniPathwayiUPA00661.
    BioCyciMetaCyc:AT1G06290-MONOMER.
    BRENDAi1.3.3.6. 399.
    ReactomeiR-ATH-389887. Beta-oxidation of pristanoyl-CoA.

    Miscellaneous databases

    PROiP0CZ23.

    Gene expression databases

    GenevisibleiP0CZ23. AT.

    Family and domain databases

    InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR012258. Acyl-CoA_oxidase.
    IPR002655. Acyl-CoA_oxidase_C.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF01756. ACOX. 1 hit.
    PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMiSSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis."
      Froman B.E., Edwards P.C., Bursch A.G., Dehesh K.
      Plant Physiol. 123:733-742(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: cv. No-0.
    2. "Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during Arabidopsis seed germination."
      Eastmond P.J., Hooks M.A., Williams D., Lange P., Bechtold N., Sarrobert C., Nussaume L., Graham I.A.
      J. Biol. Chem. 275:34375-34381(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
      Tissue: Hypocotyl.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      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.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis."
      Cruz-Castillo M., Martinez C., Buchala A., Metraux J.-P., Leon J.
      Plant Physiol. 135:85-94(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiACOX3_ARATH
    AccessioniPrimary (citable) accession number: P0CZ23
    Secondary accession number(s): Q9C839
    , Q9LKX5, Q9LLH9, Q9LMI8, Q9M7X6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: July 27, 2011
    Last modified: June 8, 2016
    This is version 41 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

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.