A0A6L3VIB0 · A0A6L3VIB0_9BACI

  • Protein
    S-adenosylmethionine decarboxylase proenzyme
  • Gene
    speH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
Site62-63Cleavage (non-hydrolytic); by autolysis
Active site63Schiff-base intermediate with substrate; via pyruvic acid
Active site68Proton acceptor; for processing activity
Active site83Proton 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
      speH
    • ORF names
      F7731_04405

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BZ1
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Cytobacillus

Accessions

  • Primary accession
    A0A6L3VIB0

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50271803111-62S-adenosylmethionine decarboxylase beta chain
Modified residue63Pyruvic acid (Ser); by autocatalysis
ChainPRO_502718031063-126S-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.

Family & Domains

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    126
  • Mass (Da)
    13,836
  • Last updated
    2020-10-07 v1
  • Checksum
    BD2370A536F80103
METMGRHVISELWGCDFEKLNDMDFIERTFVDAALKSGAEIREVAFHKFAPQGVSGVVIISESHLTIHSFPEHGYASIDVYTCGDLDPSIAANYIAEALGAETRENIEIPRGMGPVQVKQAQANIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WBOS01000001
EMBL· GenBank· DDBJ
KAB2338795.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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