O02767 · ACOX2_RABIT
- ProteinPeroxisomal acyl-coenzyme A oxidase 2
- GeneACOX2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids681 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids (PubMed:9218493).
Capable of oxidizing short as well as long chain 2-methyl branched fatty acids (By similarity).
Capable of oxidizing short as well as long chain 2-methyl branched fatty acids (By similarity).
Catalytic activity
- (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + A + H2O = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + AH2This reaction proceeds in the forward direction.
- (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + O2 = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-en-26-oyl-CoA + H2O2This reaction proceeds in the forward direction.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity | |
Molecular Function | FAD binding | |
Molecular Function | fatty acid binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | palmitoyl-CoA oxidase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | bile acid biosynthetic process | |
Biological Process | fatty acid beta-oxidation using acyl-CoA oxidase | |
Biological Process | lipid homeostasis | |
Biological Process | very long-chain fatty acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePeroxisomal acyl-coenzyme A oxidase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionO02767
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000204683 | 1-681 | Peroxisomal acyl-coenzyme A oxidase 2 | |||
Sequence: MGIPVHRVSLGDAWSSRMHPDMESERCAQSFSVERLTNILDGGAQHTALRRKVESIIHGNPQFSSKDNYFMSQNELYEAATRKRYHLQKIAQRMGWTEEGRELEYAHRALSADLNLNLQGIFLKALRSLGSEEQIAKWEPLGKTFQIISTYAQTELGHGTYLQGLETEATYDAATQEFVIHSPTVTATKWWPGDLGRSATHALILAQLICSGARRGMHAFIVPVRSLQDHTPLPGITIGDIGPKMGLQHIDNGFLKMDHVRVPRENMLSRFAQVLPDGAYIKLGTAQSNYLGMLVTRVHLLLGAILSPLQKACVIATRYSVIRHQCRLRPSDPEVKILEHQTQQQKLFPQLAMCYAFHFLATGLLEFFQQAYKNILDRDFTLLPELHALSTGTKAMMSDFCTQGAEQCRRACGGHGYSKLSGLPSLVTSVTASCTYEGENTVLYLQVARFLVKSCLQAQGFPGSTSQRSLPRSVSYLALPDLARCPAQTAADFFCPALYTAAWAHVAARLTKDSVHHLQALRQSGADEHEAWNQTTIIHLQAAKAHCYYISVKSFKEALEKLENEPAIQQVLKRLCDLHALHGILTNSGDFLHDGFLSGAQVDMARTAYMDLLPLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFEWAQRSPTNTQENPAYKKYIQPLLQSWRSNL | ||||||
Modified residue | 9 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 66 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 137 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 453 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 561 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 667 | N6-succinyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Liver and kidney.
Interaction
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length681
- Mass (Da)76,199
- Last updated1997-07-01 v1
- Checksum7BF3550F353FB2E3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y13279 EMBL· GenBank· DDBJ | CAA73728.1 EMBL· GenBank· DDBJ | mRNA |