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A0A0M4Q6C0 · A0A0M4Q6C0_9PSEU

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.
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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.
Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.

Features

Showing features for site, active site, binding site.

Type
IDPosition(s)Description
Site66-67Cleavage (non-hydrolytic); by autolysis
Active site67Schiff-base intermediate with substrate; via pyruvic acid
Active site72Proton acceptor; for processing activity
Active site87Proton donor; for catalytic activity
Binding site149S-methyl-5'-thioadenosine (UniProtKB | ChEBI)
Binding site179spermidine (UniProtKB | ChEBI)
Binding site203spermidine (UniProtKB | ChEBI)
Binding site222S-methyl-5'-thioadenosine (UniProtKB | ChEBI)
Binding site260-261S-methyl-5'-thioadenosine (UniProtKB | ChEBI)
Active site278Proton acceptor
Binding site287S-methyl-5'-thioadenosine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionadenosylmethionine decarboxylase activity
Molecular Functionspermidine synthase activity
Biological Processspermidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      speE
    • Synonyms
      speH
    • ORF names
      XF36_10195

Organism names

  • Taxonomic identifier
  • Strain
    • HH130629-09
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Pseudonocardia

Accessions

  • Primary accession
    A0A0M4Q6C0

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50235335101-66S-adenosylmethionine decarboxylase beta chain
Modified residue67Pyruvic acid (Ser); by autocatalysis
ChainPRO_502353350967-408S-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

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain120-364PABS

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Belongs to the spermidine/spermine synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    408
  • Mass (Da)
    44,236
  • Last updated
    2015-12-09 v1
  • MD5 Checksum
    B64C49A07A1BB03A4FA53F300E011A05
MPSTSSPVGRHVLAELGGIAPEMLDDCARLRSDLTAALTEAGAQVRQVVVERFEPQGATVVAVLAESHASIHTWPEHGGMHVDVFTCGESADPVDAVRRLADRVGATDTALQVVDRGGAPRTVTEPLSPGLTRRWDLGRVHHVADTGFQHVVVADTAHGVTLFCDDERQSTEHTQLTYHEALVWPGALLARELDRVLIIGSSEGVASEMAVAAGASRVDHVDIDAEAVRICAEHLPYGYTPESLAAAERGEGPVHLTYGDGRQFVLDAREDWDLVIVDLPDERPDEPDAQINRLYEEEFVRACAQRLTPGGVLVFQAGSPAVWRDATLRSAWQQRFAAVFGETGGRGVYIGCEEHEWAFLAGVREPMADPGAVAAERLASMPSRPELWDATALRHRLVAPLSLRRLTD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011868
EMBL· GenBank· DDBJ
ALE83472.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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