A0A0X8IAU9 · A0A0X8IAU9_9CREN

  • 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.

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.

Type
IDPosition(s)Description
Site72-73Cleavage (non-hydrolytic); by autolysis
Active site73Schiff-base intermediate with substrate; via pyruvic acid
Active site78Proton acceptor; for processing activity
Active site93Proton 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
      SE86_06075

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 7A
  • Taxonomic lineage
    Archaea > Thermoproteota > Thermoprotei > Acidilobales > Acidilobaceae > Acidilobus

Accessions

  • Primary accession
    A0A0X8IAU9

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50234544781-72S-adenosylmethionine decarboxylase beta chain
Modified residue73Pyruvic acid (Ser); by autocatalysis
ChainPRO_502345447973-125S-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
    125
  • Mass (Da)
    13,959
  • Last updated
    2016-04-13 v1
  • MD5 Checksum
    B64E49ECD9D1CFA71D14054492ACBA38
MTQERLPEDTPRVIGRHVYGNLKGCRNYDALTNPAVIERVLREAGRVGRMTILDVKSWKIGEGVSAVAIVLESHITIHTWPEYRFATVDVYACGSQSNPLKAFNYIAKVLEPEDVVMGSADRSLE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010515
EMBL· GenBank· DDBJ
AMD31358.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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