A3MTU5 · ARGDC_PYRCJ

Function

function

Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

Note: Binds 1 pyruvoyl group covalently per subunit.

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site73-74Cleavage (non-hydrolytic); by autolysis
Active site74Schiff-base intermediate with substrate; via pyruvic acid
Active site79Proton acceptor; for processing activity
Active site94Proton donor; for catalytic activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionarginine decarboxylase activity
Biological Processarginine catabolic process
Biological Processpolyamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Ordered locus names
      Pcal_0636

Organism names

Accessions

  • Primary accession
    A3MTU5

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003641211-73Arginine decarboxylase beta chain
Modified residue74Pyruvic acid (Ser); by autocatalysis
ChainPRO_000036412274-126Arginine 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

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    126
  • Mass (Da)
    14,324
  • Last updated
    2007-04-03 v1
  • Checksum
    8D4073B4DFF84F26
MQATAQVQTPVVGRHVYGELYGVDESLLKDEERLRRIVIEAAHIANMHLVEVNSWKFKGGDKEGVSVIALVLESHIAIHTWPVYNFATVDVYTCGEHSDPMAAFRYIVSQLNPKRFTVNYSDRSYK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000561
EMBL· GenBank· DDBJ
ABO08062.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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