P49725 · DCOR_PANRE

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

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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.

TypeIDPosition(s)Description
Site204Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates
Binding site207pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site244pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site283-286pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site339-340substrate; ligand shared between dimeric partners; in other chain
Active site368Proton donor; shared with dimeric partner
Binding site369substrate; ligand shared between dimeric partners
Binding site397pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionornithine decarboxylase activity
Biological Processputrescine biosynthetic process from ornithine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ornithine decarboxylase
  • EC number
  • Short names
    ODC

Gene names

    • Name
      ODC

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Panagrolaimoidea > Panagrolaimidae > Panagrellus

Accessions

  • Primary accession
    P49725

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001499021-435Ornithine decarboxylase
Modified residue76N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers.

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    435
  • Mass (Da)
    47,111
  • Last updated
    1996-10-01 v1
  • Checksum
    BBB093C1EF7FEFA4
MTLTGCVDYYEIIAGTKVAVCRNAIDNKTVATAIAATRTVNGNDDPFVVMNVSTIMAKVIQWQRTMPRVAPCYAVKCNDDKVLLRTLADLGMGFDCASKAEIEKVIGLVGPEKIVYANPCKTRGFIAHAEAAGVKRMTFDSVEELTKIKQNHADPSLILRISVSDPTAQCQLGIKFGCDPETVAPKLLRKAADMGMNVIGISFHVGSGCNEPATFRTALEYARGLFDLGISLGLSMTLLDIGGGFPGVDTAHISLDACAAVINPALEELFPLDSCPDVEVIAEPGRYFACAAVSVTTNVIASVKVPASRITEKADDVNRDGYMYYMNDGVYGSFNCKLFDHYQPRGMPLAEHDADEPRFPVCVWGPTCDGLDQVEESSVMPRLYEGDWLYYPDMGAYTSVAASTFNGFDKPKTYYFIDEATLGSIVRKADSAPRG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X82199
EMBL· GenBank· DDBJ
CAA57683.1
EMBL· GenBank· DDBJ
mRNA
X95719
EMBL· GenBank· DDBJ
CAA65024.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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