A7FM34 · SPED_YERP3

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
    • Ordered locus names
      YpsIP31758_3355

Organism names

Accessions

  • Primary accession
    A7FM34

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10000603591-111S-adenosylmethionine decarboxylase beta chain
Modified residue112Pyruvic acid (Ser); by autocatalysis
ChainPRO_1000060360112-264S-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.

Structure

Family & Domains

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    264
  • Mass (Da)
    30,293
  • Last updated
    2007-09-11 v1
  • Checksum
    E4C0AEE946FEDC89
MSKLKLHGFNNLTKSLSFCIYDICYAKTADDRDGYIAYIDEQYNANRLTEILSETCSIIGANILNIARQDYDPQGASVTILVSEEPVDPRDVDTSEHPGPLPSAVVAHLDKSHICVHTYPESHPEAGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTMDYRVRGFTRDINGVKHFIDHKINSIQNFMSDDMKSLYHMMDVNVYQENIFHTKMMLKDFDLKHYLFNAKPEELSAEEKEQITRLLYKEMQEIYYGRNVPEV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000720
EMBL· GenBank· DDBJ
ABS49417.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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