A7K6N6 · A7K6N6_STEMA

Function

function

Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.

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 site, active site.

TypeIDPosition(s)Description
Site112-113Cleavage (non-hydrolytic); by autolysis
Active site113Schiff-base intermediate with substrate; via pyruvic acid
Active site118Proton acceptor; for processing activity
Active site141Proton donor; for catalytic activity

GO annotations

AspectTerm
Molecular Functionadenosylmethionine decarboxylase activity
Biological Processspermidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      speD
    • ORF names
      E5352_08945

Organism names

Accessions

  • Primary accession
    A7K6N6

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50347678411-112S-adenosylmethionine decarboxylase beta chain
Modified residue113Pyruvic acid (Ser); by autocatalysis
ChainPRO_5034767840113-264S-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.

Keywords

Interaction

Subunit

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.

Family & Domains

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    264
  • Mass (Da)
    30,719
  • Last updated
    2007-09-11 v1
  • Checksum
    69E7BEC64A80B692
MVKPLPRLRLQGFNNLTKALSFNIYDVCYARTEEERQRYIEYIDEEYNADRLTQILTDVAEIIGANILNVARQDYDPQGASVTILISEEPVIDKKLAGKELISDAVVAHMDKSHITVHTYPETHPQEGIATFRADIDVATCGVISPLKALNYLIESLESDIVIMDYRVRGFTRDVKGKKHYIDHKINSIQNFLAKNIKSRYEMFDVNVYQENIFHTKMHLKDFDLDQYLFEEKAKNISFKERMKIEALLKREIEELFHGRNLSE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF011625
EMBL· GenBank· DDBJ
ABM53760.1
EMBL· GenBank· DDBJ
Genomic DNA
SRYW01000006
EMBL· GenBank· DDBJ
TGY34560.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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