A0A9E4TLU9 · A0A9E4TLU9_UNCCH

  • Protein
    S-adenosylmethionine decarboxylase proenzyme
  • Gene
    speD
  • 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
      speD
    • Synonyms
      speH
    • ORF names
      J4N33_01960

Organism names

Accessions

  • Primary accession
    A0A9E4TLU9

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50397715271-62S-adenosylmethionine decarboxylase beta chain
Modified residue63Pyruvic acid (Ser); by autocatalysis
ChainPRO_503977152663-121S-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    121
  • Mass (Da)
    13,055
  • Last updated
    2023-05-03 v1
  • Checksum
    8C693B0F632EA148
MNVLGLHLLLELRDCNSGLLNDLNHIRLAMLRAAEDAGAHVIGESFHQFSPQGVTGILAIAESHISIHTWPEYGYAAADIFTCGSGVQARKIAAILVDVLECRDPEITEVVRGLLHESAVS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGDOB010000046
EMBL· GenBank· DDBJ
MCI0845860.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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