O65202 · ACOX1_ARATH
- ProteinPeroxisomal acyl-coenzyme A oxidase 1
- GeneACX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids664 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
- a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 FAD per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
5.3 μM | C14-CoA |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 135 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 137 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 138 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 144 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 177 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 310 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 330 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 333 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 401 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 422 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 424 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 426 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | peroxisome | |
Cellular Component | plasmodesma | |
Molecular Function | acyl-CoA oxidase activity | |
Molecular Function | FAD binding | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | jasmonic acid biosynthetic process | |
Biological Process | long-chain fatty acid metabolic process | |
Biological Process | response to fungus | |
Biological Process | response to wounding |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisomal acyl-coenzyme A oxidase 1
- EC number
- Short namesAOX 1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO65202
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000204689 | 1-664 | Peroxisomal acyl-coenzyme A oxidase 1 | |||
Sequence: MEGIDHLADERNKAEFDVEDMKIVWAGSRHAFEVSDRIARLVASDPVFEKSNRARLSRKELFKSTLRKCAHAFKRIIELRLNEEEAGRLRHFIDQPAYVDLHWGMFVPAIKGQGTEEQQKKWLSLANKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHTPTQTASKWWPGGLGKVSTHAVVYARLITNGKDYGIHGFIVQLRSLEDHSPLPNITVGDIGTKMGNGAYNSMDNGFLMFDHVRIPRDQMLMRLSKVTREGEYVPSDVPKQLVYGTMVYVRQTIVADASNALSRAVCIATRYSAVRRQFGAHNGGIETQVIDYKTQQNRLFPLLASAYAFRFVGEWLKWLYTDVTERLAASDFATLPEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLWCSGLPELFAVYVPACTYEGDNVVLQLQVARFLMKTVAQLGSGKVPVGTTAYMGRAAHLLQCRSGVQKAEDWLNPDVVLEAFEARALRMAVTCAKNLSKFENQEQGFQELLADLVEAAIAHCQLIVVSKFIAKLEQDIGGKGVKKQLNNLCYIYALYLLHKHLGDFLSTNCITPKQASLANDQLRSLYTQVRPNAVALVDAFNYTDHYLNSVLGRYDGNVYPKLFEEALKDPLNDSVVPDGYQEYLRPVLQQQLRTARL | ||||||
Disulfide bond | 467↔576 | |||||
Sequence: CRSGVQKAEDWLNPDVVLEAFEARALRMAVTCAKNLSKFENQEQGFQELLADLVEAAIAHCQLIVVSKFIAKLEQDIGGKGVKKQLNNLCYIYALYLLHKHLGDFLSTNC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed mainly in flowers and young seedlings. Lower expression in roots, leaves and bracts.
Induction
Induced by dehydration, abscisic acid (ABA) and jasmonic acid (JA), and locally and systemically by wounding.
Developmental stage
Induced by seed imbibition with a peak at day 2 and then declines to reach a basal level 4 days after sowing.
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 662-664 | Microbody targeting signal | ||||
Sequence: ARL |
Sequence similarities
Belongs to the acyl-CoA oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
O65202-1
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.
- Name1
- Length664
- Mass (Da)74,302
- Last updated1998-08-01 v1
- Checksum44AFD139D5434636
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JMK8 | F4JMK8_ARATH | ACX1 | 651 |
Sequence caution
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF057044 EMBL· GenBank· DDBJ | AAC13498.1 EMBL· GenBank· DDBJ | mRNA | ||
Z97341 EMBL· GenBank· DDBJ | CAB10450.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161544 EMBL· GenBank· DDBJ | CAB78718.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE83798.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY058849 EMBL· GenBank· DDBJ | AAL24237.1 EMBL· GenBank· DDBJ | mRNA | ||
BT001067 EMBL· GenBank· DDBJ | AAN46824.1 EMBL· GenBank· DDBJ | mRNA |