P60659 · SPEA_SALTY
- ProteinBiosynthetic arginine decarboxylase
- GenespeA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids658 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the biosynthesis of agmatine from arginine.
Catalytic activity
- H+ + L-arginine = agmatine + CO2
Cofactor
Protein has several cofactor binding sites:
Pathway
Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 307-317 | substrate | ||||
Sequence: FDVGGGLGVDY |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | arginine decarboxylase activity | |
Molecular Function | metal ion binding | |
Biological Process | arginine catabolic process | |
Biological Process | putrescine biosynthetic process from arginine | |
Biological Process | spermidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBiosynthetic arginine decarboxylase
- EC number
- Short namesADC
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP60659
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149976 | 1-658 | Biosynthetic arginine decarboxylase | |||
Sequence: MSDDMSMGSPSSAGEQGVLRSMQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAKLVKAREAQGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLRDAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEEHGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTDPTAPAEDAPRALQNLWETWQEMHKPGTRRSLREWLHDSQMDLHDIHIGYSSGAFSLQERAWAEQLYLSMCHEVQKQLDPQNRAHRPIIDELQERMADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTHFRDQVKQTDLDDALQQQFLEEFEAGLYGYTYLEDE | ||||||
Modified residue | 127 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length658
- Mass (Da)73,833
- Last updated2004-03-29 v1
- Checksum8A689D85DB85D6CF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE006468 EMBL· GenBank· DDBJ | AAL21961.1 EMBL· GenBank· DDBJ | Genomic DNA |