A0A4Q5DSN5 · A0A4Q5DSN5_9BACE

  • 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
Site457-458Cleavage (non-hydrolytic); by autolysis
Active site458Schiff-base intermediate with substrate; via pyruvic acid
Active site463Proton acceptor; for processing activity
Active site478Proton 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
      GA560_19190

Organism names

  • Taxonomic identifier
  • Strain
    • BIOML-A73
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides

Accessions

  • Primary accession
    A0A4Q5DSN5

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50264172131-457S-adenosylmethionine decarboxylase beta chain
Modified residue458Pyruvic acid (Ser); by autocatalysis
ChainPRO_5026417212458-555S-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

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain111-303N4-bis(aminopropyl)spermidine synthase C-terminal
Region521-555Disordered
Compositional bias522-542Basic and acidic residues

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    555
  • Mass (Da)
    63,237
  • Last updated
    2019-07-31 v1
  • Checksum
    02D91954CEF690FD
MDYINKIFKTVSIKDNRRIIELYFQELYCCAPLSNKTLSQKLLLPVPIVTAIKNEGIKLGIFEQCGRGVGLTHNGKDYVEQALGFKGIDLCLYRRLAESEQARDAYADALSKKYRAAFDERPVADVALDQAQCTVQTAFRRALLCLANGTLTSRQIVCMGDDDFVSLAIGFLLKELYPGPSICPTHIHVLEMDGRYIECLNRLSERFSLPISCEQVDLRMPLPPHLCGRFDCLFTDPPYTQEGASLFLSRAISVLKEESGLRIFFSFGNKSATEVYFLQKCFQLHGLAIKDMFTRFNEYMGASLLGNKGQLFVLETTERTRALFPLEKRGRDDIYTADRNFRQNRYRCRQCSKVYAVGKEAEYQTIRELKKQGCSVCGATVFDRLHKNGNTDKKQYLPLGHHILADFYNCDPEKLDDVEQIRTFMHEAAVSAGATIVQENFHKYAPIGVSGVVVIQESHLTIHTWPECGYAAVDLFTCGTNVRPWTAFDYLQERLGCAKVEYSDLMRGAYERPSLLRYSETEQPAMRRKKRQRYDASSKWNRRAKSLTDCSVLSK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias522-542Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WDER01000065
EMBL· GenBank· DDBJ
KAB6079681.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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