A0A2D3T0D6 · A0A2D3T0D6_9ENTR

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
Site111-112Cleavage (non-hydrolytic); by autolysis
Active site112Schiff-base intermediate with substrate; via pyruvic acid
Active site117Proton acceptor; for processing activity
Active site140Proton donor; for catalytic activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionadenosylmethionine decarboxylase activity
Biological Processspermidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      speD
    • ORF names
      BJP41_01665
      , BJP43_01960
      , CJJ18_06700

Organism names

  • Taxonomic identifier
  • Strains
    • A2C
    • ZA17
    • MI47
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > aphid secondary symbionts > Candidatus Hamiltonella

Accessions

  • Primary accession
    A0A2D3T0D6

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50415025161-111S-adenosylmethionine decarboxylase beta chain
Modified residue112Pyruvic acid (Ser); by autocatalysis
ChainPRO_5041502515112-264S-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)
    30,503
  • Last updated
    2018-01-31 v1
  • Checksum
    6710550C1B4D2ECE
MNKLKLHGFNNLTKSLGFCIYDICYAQTFADRDGYIAYIDDEYNADRLTEILRETCSIIGANILNIARQDYNPQGASVTILISEEAIDPRDVDTSEHPGPLPDSIVAHLDKSHICVHTYPESHPTEGLCTFRADIEVSTCGIISPLNALNYLIHQLESDIVTIDYRVRGFTRDVNGVKHYIDHQINSIQNFMCKDIQSLYHMMDVNVYQENIFHTKMMLKDFDLKHYLFNSHPEQLSVQEKDLITKRLYKEMQEIYYGRNVVEV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP022932
EMBL· GenBank· DDBJ
ASV33739.1
EMBL· GenBank· DDBJ
Genomic DNA
CP017606
EMBL· GenBank· DDBJ
ATW29269.1
EMBL· GenBank· DDBJ
Genomic DNA
CP017613
EMBL· GenBank· DDBJ
ATW33253.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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