Q27883 · DCAM_ONCVO

  • Protein
    S-adenosylmethionine decarboxylase proenzyme
  • Gene
    smd-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )
Note: Binds 1 pyruvoyl group covalently per subunit.

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.

Features

Showing features for active site, site.

136550100150200250300350
Type
IDPosition(s)Description
Active site31
Active site34
Site86-87Cleavage (non-hydrolytic); by autolysis
Active site87Schiff-base intermediate with substrate; via pyruvic acid
Active site101Proton donor; for catalytic activity
Active site248Proton acceptor; for processing activity
Active site263Proton acceptor; for processing activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionadenosylmethionine decarboxylase activity
Biological Processspermidine biosynthetic process
Biological Processspermine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      smd-1
    • Synonyms
      samdc

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Spiruromorpha > Filarioidea > Onchocercidae > Onchocerca

Accessions

  • Primary accession
    Q27883

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000299771-86S-adenosylmethionine decarboxylase beta chain
Modified residue87Pyruvic acid (Ser); by autocatalysis
ChainPRO_000002997887-365S-adenosylmethionine decarboxylase alpha chain

Post-translational modification

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain (By similarity).

Keywords

Interaction

Subunit

Heterotetramer of two alpha and two beta chains.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the eukaryotic AdoMetDC family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    365
  • Mass (Da)
    41,893
  • Last updated
    1996-11-01 v1
  • Checksum
    F8615CE029BA40B8
MSTSTLSDGSLDEGTFAAEDVSGVIEDYFFEGAEKLLEIWFDKNQNGATSLRNIPYSELVSMLDIAQCRILHSKSNECMDSYVLSESSMFISDFRIILKTCGTTRLLHAIERILHIAKIYCNMDNVVSVFYSRKNFMHPEKQPYPHSSFETEVDYLEEHFAGGSAYCIGPQRQDRWFLYTMVTPQAVFPFPEHTLEILMNGLPEDVLSTFSPNVSKDGKDCRMKSAINTILPPDIVVHEELFSPCGYSLNGLIPHSDHYITIHVTPEPDFSYVSFETNQHTLNLCEQMLKVLEIFKPSKFLLTIFTNELSNEGKKMQKNLWDLKICGCRRTNLQFLELPTETLIYVQFERIKSAEQVTCKEVFDR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X95714
EMBL· GenBank· DDBJ
CAA65018.1
EMBL· GenBank· DDBJ
Genomic DNA
X95713
EMBL· GenBank· DDBJ
CAA65017.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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