A8AAB6 · ARGDC_IGNH4
- ProteinArginine decarboxylase proenzyme
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids144 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.
Catalytic activity
- L-arginine + H+ = agmatine + CO2
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 79-80 | Cleavage (non-hydrolytic); by autolysis | ||||
Sequence: ES | ||||||
Active site | 80 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Active site | 85 | Proton acceptor; for processing activity | ||||
Sequence: H | ||||||
Active site | 100 | Proton donor; for catalytic activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | arginine decarboxylase activity | |
Biological Process | arginine catabolic process | |
Biological Process | polyamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArginine decarboxylase proenzyme
- EC number
- Short namesADC ; ArgDC
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Desulfurococcales > Desulfurococcaceae > Ignicoccus
Accessions
- Primary accessionA8AAB6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000364115 | 1-79 | Arginine decarboxylase beta chain | |||
Sequence: MKTVELTNGSKKKVEDRIVGRHVYGNLYGVDPAKLWDEEGLKELVREAAEVANMKLVEVRSWKFTGYHGGVSVMALVLE | ||||||
Modified residue | 80 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_0000364116 | 80-144 | Arginine decarboxylase alpha chain | |||
Sequence: SHITIHTWPDYEYATVDVYTCGERSDPWRAFELIVERLEPEDYVVHYSDRSSPKRPLGGTAGRIQ |
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
- PTM
Interaction
Subunit
Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length144
- Mass (Da)16,426
- Last updated2007-10-23 v1
- Checksum5471D495C23A939F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000816 EMBL· GenBank· DDBJ | ABU81868.1 EMBL· GenBank· DDBJ | Genomic DNA |