A2XV58 · DCAM_ORYSI

Function

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 active site, site.

139850100150200250300350
TypeIDPosition(s)Description
Active site18
Active site21
Site77-78Cleavage (non-hydrolytic); by autolysis
Active site78Schiff-base intermediate with substrate; via pyruvic acid
Active site92Proton donor; for catalytic activity
Active site243Proton acceptor; for processing activity
Active site256Proton acceptor; for processing activity

GO annotations

AspectTerm
Molecular Functionadenosylmethionine decarboxylase activity
Biological Processspermidine biosynthetic process
Biological Processspermine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      SAMDC
    • ORF names
      OsI_015951

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Pokkali
    • cv. 93-11
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    A2XV58
  • Secondary accessions
    • O24215
    • O81269
    • Q56CX9
    • Q7XU78
    • Q7XUL0
    • Q9SC65

Proteomes

Genome annotation databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003020511-77S-adenosylmethionine decarboxylase beta chain
Modified residue78Pyruvic acid (Ser); by autocatalysis
ChainPRO_000030205278-398S-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 (By similarity).

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the eukaryotic AdoMetDC family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    398
  • Mass (Da)
    43,309
  • Last updated
    2007-09-11 v2
  • Checksum
    1324EDA871B2AF39
MGVLSAADPPPVSAIGFEGYEKRLEITFSEAPVFADPDGRGLRALSRAQIDSVLDLARCTIVSELSNKDFDSYVLSESSLFIYSDKIVIKTCGTTKLLLTIPRILELAEGLSMPLAAVKYSRGMFIFPSAQPAPHRSFSEEVAVLNRYFGHLKSGGNAYVIGDPAKPGQKWHIYYATQHPEQPMVTLEMCMTGLDKEKASVFFKTSADGHTSCAKEMTKLSGISDIIPEMEICDFDFEPCGYSMNAIHGLAFSTIHVTPEDGFSYASYEVVGFDASTLAYGDLVKRVLRCFGPSEFSVAVTIFGGHGHAGTWAKELNADAYKCNNMVEQELPCGGLLIYQSFDATEDVPVAVGSPKSVLHCFEAENMVNPAPVKEGKLGNLLPWGEDALEENDGVFDE

Sequence caution

The sequence EAY94718.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict3in Ref. 3; AAX76987
Sequence conflict96in Ref. 2; CAB64671
Sequence conflict157in Ref. 3; AAX76987
Sequence conflict235in Ref. 3; AAX76987
Sequence conflict294in Ref. 3; AAX76987
Sequence conflict394in Ref. 3; AAX76987

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF067194
EMBL· GenBank· DDBJ
AAC79990.1
EMBL· GenBank· DDBJ
mRNA
AJ252213
EMBL· GenBank· DDBJ
CAB64671.1
EMBL· GenBank· DDBJ
Genomic DNA
AY966487
EMBL· GenBank· DDBJ
AAX76987.1
EMBL· GenBank· DDBJ
mRNA
CM000129
EMBL· GenBank· DDBJ
EAY94718.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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