P49725 · DCOR_PANRE
- ProteinOrnithine decarboxylase
- GeneODC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids435 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Catalytic activity
- H+ + L-ornithine = CO2 + putrescine
Cofactor
Activity regulation
Inhibited by antizyme (AZ) in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Pathway
Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 204 | Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates | ||||
Sequence: H | ||||||
Binding site | 207 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 244 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 283-286 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EPGR | ||||||
Binding site | 339-340 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: FD | ||||||
Active site | 368 | Proton donor; shared with dimeric partner | ||||
Sequence: C | ||||||
Binding site | 369 | substrate; ligand shared between dimeric partners | ||||
Sequence: D | ||||||
Binding site | 397 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ornithine decarboxylase activity | |
Biological Process | putrescine biosynthetic process from ornithine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOrnithine decarboxylase
- EC number
- Short namesODC
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Panagrolaimoidea > Panagrolaimidae > Panagrellus
Accessions
- Primary accessionP49725
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149902 | 1-435 | Ornithine decarboxylase | |||
Sequence: MTLTGCVDYYEIIAGTKVAVCRNAIDNKTVATAIAATRTVNGNDDPFVVMNVSTIMAKVIQWQRTMPRVAPCYAVKCNDDKVLLRTLADLGMGFDCASKAEIEKVIGLVGPEKIVYANPCKTRGFIAHAEAAGVKRMTFDSVEELTKIKQNHADPSLILRISVSDPTAQCQLGIKFGCDPETVAPKLLRKAADMGMNVIGISFHVGSGCNEPATFRTALEYARGLFDLGISLGLSMTLLDIGGGFPGVDTAHISLDACAAVINPALEELFPLDSCPDVEVIAEPGRYFACAAVSVTTNVIASVKVPASRITEKADDVNRDGYMYYMNDGVYGSFNCKLFDHYQPRGMPLAEHDADEPRFPVCVWGPTCDGLDQVEESSVMPRLYEGDWLYYPDMGAYTSVAASTFNGFDKPKTYYFIDEATLGSIVRKADSAPRG | ||||||
Modified residue | 76 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers.
Structure
Sequence
- Sequence statusComplete
- Length435
- Mass (Da)47,111
- Last updated1996-10-01 v1
- ChecksumBBB093C1EF7FEFA4