A0A3M8EZY7 · A0A3M8EZY7_DESBX
- ProteinBiosynthetic arginine decarboxylase
- GenespeA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids635 (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 binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 282-292 | substrate | ||||
Sequence: LDIGGGLGVDY | ||||||
Active site | 502 | Proton donor | ||||
Sequence: C |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales
Accessions
- Primary accessionA0A3M8EZY7
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 100 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 75-342 | Orn/DAP/Arg decarboxylase 2 N-terminal | ||||
Sequence: SINRVFKNAIEENDYPAKYQTFYPIKVNQQRQVVEAIAKFGKRYNIGLEVGSKPELVIGLSFATGNGIPIICNGYKDNEYIETVLYATKIGYDITIVVEKMFELEKIIALSKKTGIRPKLGIRVKLSSKGTGKWATSGGEDAKFGLRMSEIIAAINVLQRNDLLDNVKLLHFHIGSQITKIDKIKTALIEGTRIYTEMKKLGVGIEFLDIGGGLGVDYDGSKSSYFSSVNYSIEEYANDVIYQIKNICDDAGVECPNIISESGRATVA | ||||||
Domain | 372-449 | Arginine decarboxylase helical bundle | ||||
Sequence: KLAPTVKKLVDIYKSIDRYSLREDYHDTVQLINEAVSLFNLGYLTLSERAMAEWLHGKILRKINGIVEKIKPIPEELQ | ||||||
Domain | 584-633 | Arginine decarboxylase C-terminal helical | ||||
Sequence: LKYVQYKGPEILKHVRDNLEKDVALRKISIEESSHFLELLDRTLLGYTYL |
Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length635
- Mass (Da)71,765
- Last updated2019-02-13 v1
- Checksum97EB0AF4C557BA6B