B5EIW4 · SPEA_CITBB
- 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 > Citrifermentans
Accessions
- Primary accessionB5EIW4
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000145594 | 1-635 | Biosynthetic arginine decarboxylase | |||
Sequence: MAKWTINDSSKIYNIDNWGAELFSINKKGNVCVHPSPNSKYSIDLKVLVDDLIKRKIKPPILLRFMNILEGRIASISRVFKNAISDNNYPAKYQTFYPIKVNQQRQVVEAIANFGKKYNIGLEVGSKPELVAAISMSTGNNLPILCNGYKDTEFIETVLFATRVGYDITIVVEKLFELEKIVEVSKRTGIVPKLGIRVKLSSKGIGKWSTSGGDDAKFGLRISELIAAIDMLKQNDMLDSVKLLHFHVGSQITKIDKIKNALIEGTRIYAEMRKLGVNLEFLDIGGGLGVDYDGSKSSYFSSVNYSLEEYANDVIYQVKNICDDAGVPCPNIISESGRATVAHYSVLVTDVLNNNTQTLMPDFESILTEPEKLSPTVKKLVDIYKSIDKHSLREDYHDTIQLIQESVSLFNLGYLNMAERANAEWICSKIIRKINSIVEKMKPIPDELQNFQLSLRQTYFANFSLFQSIPDSWAIDQLFPIVPIQRLDEKPDVLTSIADITCDSDGEITSFVGENGRTKALPLHKIKVDEQYYIGFFLIGAYQEILGDMHNLFGDTNAVHITFNKKTNYKIDTVISGDATWESLKYVQYDSQEILKRVRNNLEKDVSLQKVSIEESSHFLELLDKTLQSYTYLGE | ||||||
Modified residue | 100 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length635
- Mass (Da)71,687
- Last updated2008-10-14 v1
- Checksum0AF4EC3505D54F1D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001124 EMBL· GenBank· DDBJ | ACH39919.1 EMBL· GenBank· DDBJ | Genomic DNA |