Q5RC19 (ACOX1_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peroxisomal acyl-coenzyme A oxidase 1 Short name=AOX EC=1.3.3.6 Alternative name(s): Palmitoyl-CoA oxidase | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 660 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs By similarity. |
| Catalytic activity | Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2. |
| Cofactor | FAD By similarity. |
| Pathway | |
| Subcellular location | Peroxisome By similarity. |
| Sequence similarities | Belongs to the acyl-CoA oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Cellular component | Peroxisome |
| Coding sequence diversity | Alternative splicing |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro generation of precursor metabolites and energyInferred from sequence or structural similarity. Source: UniProtKB prostaglandin metabolic processInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | peroxisome Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro acyl-CoA oxidase activityInferred from sequence or structural similarity. Source: UniProtKB flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q5RC19-1) 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. | ||||||
| Isoform 2 (identifier: Q5RC19-2) The sequence of this isoform differs from the canonical sequence as follows: 90-131: KLHLVNFVEP...KWLLSSKGLQ → NFVHRGRPEP...RFFMPAWNLE |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 660 | 660 | Peroxisomal acyl-coenzyme A oxidase 1 | PRO_0000204680 | |||||
Regions | |||||||||
| Motif | 658 – 660 | 3 | Microbody targeting signal By similarity | ||||||
Sites | |||||||||
| Active site | 421 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 139 | 1 | FAD By similarity | ||||||
| Binding site | 178 | 1 | FAD; via amide nitrogen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 26 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 255 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 267 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 310 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 437 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 500 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 504 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 643 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 649 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 651 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 90 – 131 | 42 | KLHLV…SKGLQ → NFVHRGRPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LE in isoform 2. | VSP_013217 | |||||
Experimental info | |||||||||
| Sequence conflict | 284 | 1 | F → L in CAH90691. Ref.1 | ||||||
Sequences
| ||||||||||||||||||||||||
References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Heart and Kidney. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR858463 mRNA. Translation: CAH90691.1. CR859802 mRNA. Translation: CAH91960.1. |
| RefSeq | NP_001125380.1. NM_001131908.1. NP_001128843.1. NM_001135371.1. |
| UniGene | Pab.19225. Pab.19725. |
3D structure databases | |
| ProteinModelPortal | Q5RC19. |
| SMR | Q5RC19. Positions 1-654. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100172283. 100189759. |
| KEGG | pon:100172283. pon:100189759. |
Organism-specific databases | |
| CTD | 51. |
Phylogenomic databases | |
| HOVERGEN | HBG050451. |
Family and domain databases | |
| InterPro | IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR023570. Acyl-CoA_oxidase_perosiome. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR009100. AcylCoA_DH/oxidase. [Graphical view] |
| Gene3D | G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits. |
| KO | K00232. |
| PANTHER | PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit. |
| Pfam | PF01756. ACOX. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view] |
| PIRSF | PIRSF000168. Acyl-CoA_oxidase. 1 hit. |
| SUPFAM | SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 2 hits. |
| ProtoNet | Search... |
Entry information
| Entry name | ACOX1_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RC19 Secondary accession number(s): Q5R8F0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with