B6WWP3 · B6WWP3_9BACT
- ProteinBiosynthetic arginine decarboxylase
- GenespeA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids644 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the biosynthesis of agmatine from arginine.
Catalytic activity
- L-arginine + H+ = 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 active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 511 | Proton donor | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | arginine decarboxylase activity | |
Molecular Function | metal ion binding | |
Molecular Function | monooxygenase activity | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Desulfovibrio
Accessions
- Primary accessionB6WWP3
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 112 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 87-354 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: SLHESFRKAIKNLNYQGQYRGVFPIKVNQQQQVVEKIAQFGSRYHHGLEVGSKAELIAAVSLMRDTEACIVCNGYKDEEFIDLGLQAQRLGFNLFFVLEMPSELDVLLSRSRELGIRPNIGVRAKLSVKASGHWTDSGGERSTFGLSPAQIVDVVDKLKACDMLDCFRLLHYHLGSQVSNIRDIRTGVMEGARLYVGLVQEGAPMGYLDLGGGLAVDYDGSHTNYISSRNYNLDEYSADIVEAIMSILDEQQVPHPHIITESGRATVA | ||||||
Domain | 380-460 | Arginine decarboxylase helical bundle | ||||
Sequence: EDTPEPVLNMREVYGNISLRNLQECYNDAIYYRDEMRKLFSTGRVNLRQRTLSERFFWAIIMRIAQEKVKLKTVPRDLQDI | ||||||
Domain | 589-642 | Arginine decarboxylase C-terminal helical | ||||
Sequence: VADILSYVEYDPRRILDDLRATAERAVRAGRLTPSDRFAVLQAFEDGLRGYTYF |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length644
- Mass (Da)72,739
- Last updated2009-01-20 v1
- ChecksumD2B968F6414CE5C9