B3EAF3 · SPEA_TRIL1
- ProteinBiosynthetic arginine decarboxylase
- GenespeA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids635 (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 | 282-292 | substrate | ||||
Sequence: LDIGGGLGVDY |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | arginine decarboxylase activity | |
Molecular Function | metal ion binding | |
Biological Process | arginine catabolic process | |
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 > Thermodesulfobacteriota > Desulfuromonadia > Geobacterales > Geobacteraceae > Trichlorobacter
Accessions
- Primary accessionB3EAF3
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000145595 | 1-635 | Biosynthetic arginine decarboxylase | |||
Sequence: MERWSINESAKVYNLDNWGADLFSINKKGNICVHPSSNSKNAIDLRALVDDLIKRKIKPPILLRFMDVLQGRIASINRVFRNAIAENDYPAKYQTFYPIKVNQQRQVVEAIASYGKRYNIGLEVGSKPELVAGIAISTGNGLPIICNGYKDAEYIETVLFATRVGYNITIVVEKLFELEKIIELAKKTGIRPSLGIRVKLSSKGTGKWATSGGEDAKFGLRMSEIMAAIKMLQEADLLDCVNLLHSHIGSQVTKIDKIKTALIEAARIYSEMRKLGVNIQYLDIGGGLGVDYDGSKSSYFSSVNYTVEEYANDVIYQIKNICDEAGVDCPNIISESGRATVAHYSVLVTNVLNTNTQNLMPDYEQILEEMEKPAPTVKKLLDIYKSIDRYSLREDYHDTLQLINEAVSLFNLGYLTLQDRAIAEWLYSKIIKKINSIVEKIKPIPEELQNFQLALRQTYFANFSLFQSIPDSWAIDQLFPIMPLQRLGQRPDVMASIADITCDSDGEITSFVGENGRSKFLPMHKLKKDEDYYIGFFLIGAYQEILGDLHNLFGDTNAVHITFNKKTGYMIDTVINGDATWETLKYVQYKGPEILKHVRDNLEKQVAIKKVSIEESSHFIELLDRTLLGYTYLGE | ||||||
Modified residue | 100 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length635
- Mass (Da)71,685
- Last updated2008-07-22 v1
- Checksum9165D56672C0CBF9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001089 EMBL· GenBank· DDBJ | ACD95391.1 EMBL· GenBank· DDBJ | Genomic DNA |