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Protein

Acyl-coenzyme A oxidase 4, peroxisomal

Gene

ACX4

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 short-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Has no activity as acyl-CoA dehydrogenase or on crotonyl-CoA (an unsaturated C4:1 carbocyclic ester) or glutaryl-CoA (a dicarboxylic ester).

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=8.3 µM for hexanoyl-CoA

    pH dependencei

    Optimum pH is 8.5-9.0.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei181 – 1811Substrate; via carbonyl oxygenBy similarity
    Binding sitei288 – 2881Substrate
    Binding sitei313 – 3131FAD
    Binding sitei409 – 4091Substrate; via amide nitrogen
    Binding sitei420 – 4201Substrate
    Binding sitei428 – 4281FAD; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi172 – 18110FAD
    Nucleotide bindingi205 – 2073FAD
    Nucleotide bindingi324 – 3263FAD
    Nucleotide bindingi381 – 3855FAD
    Nucleotide bindingi410 – 4123FAD

    GO - Molecular functioni

    GO - Biological processi

    • embryo development ending in seed dormancy Source: TAIR
    • fatty acid beta-oxidation Source: TAIR
    • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: GO_Central
    • lipid homeostasis Source: GO_Central
    • short-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

    BioCyciARA:AT3G51840-MONOMER.
    MetaCyc:AT3G51840-MONOMER.
    BRENDAi1.3.3.6. 399.
    ReactomeiR-ATH-71064. Lysine catabolism.

    Chemistry

    SwissLipidsiSLP:000000862.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A oxidase 4, peroxisomal (EC:1.3.3.6)
    Short name:
    AOX 4
    Alternative name(s):
    G6p
    Short-chain acyl-CoA oxidase
    Short name:
    AtCX4
    Short name:
    AtG6
    Short name:
    SAOX
    Gene namesi
    Name:ACX4
    Synonyms:G6
    Ordered Locus Names:At3g51840
    ORF Names:ATEM1.9
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G51840.

    Subcellular locationi

    GO - Cellular componenti

    • glyoxysome Source: UniProtKB-SubCell
    • peroxisome Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Glyoxysome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 436435Acyl-coenzyme A oxidase 4, peroxisomalPRO_0000201211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ96329.
    PRIDEiQ96329.

    PTM databases

    iPTMnetiQ96329.

    Expressioni

    Tissue specificityi

    Particularly abundant in etiolated cotyledons. Also present in flowers, roots and siliques, but not detected in green cotyledons, rosette leaves and stems.1 Publication

    Developmental stagei

    Induced by seed imbibition with a peak at day 5 to 7. Decreases after illumination but still detectable 5 days after illumination.

    Inductioni

    Induced by dehydration and abscisic acid (ABA).1 Publication

    Gene expression databases

    GenevisibleiQ96329. AT.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi9665. 1 interaction.
    STRINGi3702.AT3G51840.1.

    Structurei

    Secondary structure

    1
    436
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 235Combined sources
    Helixi28 – 314Combined sources
    Helixi51 – 544Combined sources
    Helixi57 – 7317Combined sources
    Helixi75 – 8410Combined sources
    Helixi89 – 913Combined sources
    Helixi92 – 965Combined sources
    Turni97 – 993Combined sources
    Turni101 – 1044Combined sources
    Helixi115 – 12814Combined sources
    Helixi130 – 14011Combined sources
    Helixi143 – 1508Combined sources
    Helixi153 – 16412Combined sources
    Beta strandi170 – 1734Combined sources
    Beta strandi179 – 1813Combined sources
    Helixi183 – 1853Combined sources
    Beta strandi189 – 1935Combined sources
    Beta strandi196 – 20712Combined sources
    Turni208 – 2114Combined sources
    Beta strandi213 – 2219Combined sources
    Turni222 – 2243Combined sources
    Beta strandi225 – 2339Combined sources
    Beta strandi239 – 2435Combined sources
    Beta strandi247 – 2504Combined sources
    Beta strandi255 – 26612Combined sources
    Helixi267 – 2693Combined sources
    Helixi277 – 31236Combined sources
    Helixi320 – 3223Combined sources
    Helixi324 – 35229Combined sources
    Helixi358 – 38225Combined sources
    Helixi383 – 3886Combined sources
    Helixi390 – 3923Combined sources
    Helixi394 – 40613Combined sources
    Beta strandi407 – 4093Combined sources
    Helixi411 – 42313Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IX5X-ray2.70A/B/C/D1-436[»]
    2IX6X-ray3.90A/B/C/D/E/F1-436[»]
    ProteinModelPortaliQ96329.
    SMRiQ96329. Positions 17-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96329.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi434 – 4363Microbody targeting signalSequence analysis

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiKOG0138. Eukaryota.
    COG1960. LUCA.
    HOGENOMiHOG000131662.
    InParanoidiQ96329.
    KOiK00232.
    OMAiYQFAQDK.
    OrthoDBiEOG09360BI1.
    PhylomeDBiQ96329.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96329-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVLSSADRA SNEKKVKSSY FDLPPMEMSV AFPQATPAST FPPCTSDYYH
    60 70 80 90 100
    FNDLLTPEEQ AIRKKVRECM EKEVAPIMTE YWEKAEFPFH ITPKLGAMGV
    110 120 130 140 150
    AGGSIKGYGC PGLSITANAI ATAEIARVDA SCSTFILVHS SLGMLTIALC
    160 170 180 190 200
    GSEAQKEKYL PSLAQLNTVA CWALTEPDNG SDASGLGTTA TKVEGGWKIN
    210 220 230 240 250
    GQKRWIGNST FADLLIIFAR NTTTNQINGF IVKKDAPGLK ATKIPNKIGL
    260 270 280 290 300
    RMVQNGDILL QNVFVPDEDR LPGVNSFQDT SKVLAVSRVM VAWQPIGISM
    310 320 330 340 350
    GIYDMCHRYL KERKQFGAPL AAFQLNQQKL VQMLGNVQAM FLMGWRLCKL
    360 370 380 390 400
    YETGQMTPGQ ASLGKAWISS KARETASLGR ELLGGNGILA DFLVAKAFCD
    410 420 430
    LEPIYTYEGT YDINTLVTGR EVTGIASFKP ATRSRL
    Length:436
    Mass (Da):47,557
    Last modified:February 1, 1997 - v1
    Checksum:iB6050262D9482C6D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U72505 mRNA. Translation: AAB18129.1.
    AB017643 mRNA. Translation: BAA82478.1.
    AF049236 Genomic DNA. Translation: AAC14411.1.
    CP002686 Genomic DNA. Translation: AEE78851.1.
    AY094441 mRNA. Translation: AAM19813.1.
    AY125536 mRNA. Translation: AAM78046.1.
    AY087793 mRNA. Translation: AAM65329.1.
    PIRiT46895.
    RefSeqiNP_190752.1. NM_115043.2.
    UniGeneiAt.21620.

    Genome annotation databases

    EnsemblPlantsiAT3G51840.1; AT3G51840.1; AT3G51840.
    GeneIDi824347.
    GrameneiAT3G51840.1; AT3G51840.1; AT3G51840.
    KEGGiath:AT3G51840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U72505 mRNA. Translation: AAB18129.1.
    AB017643 mRNA. Translation: BAA82478.1.
    AF049236 Genomic DNA. Translation: AAC14411.1.
    CP002686 Genomic DNA. Translation: AEE78851.1.
    AY094441 mRNA. Translation: AAM19813.1.
    AY125536 mRNA. Translation: AAM78046.1.
    AY087793 mRNA. Translation: AAM65329.1.
    PIRiT46895.
    RefSeqiNP_190752.1. NM_115043.2.
    UniGeneiAt.21620.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IX5X-ray2.70A/B/C/D1-436[»]
    2IX6X-ray3.90A/B/C/D/E/F1-436[»]
    ProteinModelPortaliQ96329.
    SMRiQ96329. Positions 17-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi9665. 1 interaction.
    STRINGi3702.AT3G51840.1.

    Chemistry

    SwissLipidsiSLP:000000862.

    PTM databases

    iPTMnetiQ96329.

    Proteomic databases

    PaxDbiQ96329.
    PRIDEiQ96329.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G51840.1; AT3G51840.1; AT3G51840.
    GeneIDi824347.
    GrameneiAT3G51840.1; AT3G51840.1; AT3G51840.
    KEGGiath:AT3G51840.

    Organism-specific databases

    TAIRiAT3G51840.

    Phylogenomic databases

    eggNOGiKOG0138. Eukaryota.
    COG1960. LUCA.
    HOGENOMiHOG000131662.
    InParanoidiQ96329.
    KOiK00232.
    OMAiYQFAQDK.
    OrthoDBiEOG09360BI1.
    PhylomeDBiQ96329.

    Enzyme and pathway databases

    BioCyciARA:AT3G51840-MONOMER.
    MetaCyc:AT3G51840-MONOMER.
    BRENDAi1.3.3.6. 399.
    ReactomeiR-ATH-71064. Lysine catabolism.

    Miscellaneous databases

    EvolutionaryTraceiQ96329.
    PROiQ96329.

    Gene expression databases

    GenevisibleiQ96329. AT.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACOX4_ARATH
    AccessioniPrimary (citable) accession number: Q96329
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: February 1, 1997
    Last modified: September 7, 2016
    This is version 122 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.