Q7XRA1 · ADC2_ORYSJ
- ProteinArginine decarboxylase 2
- GeneADC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids623 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
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 | 295-305 | substrate | ||||
Sequence: LDCGGGLGVDY |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | arginine decarboxylase activity | |
Biological Process | arginine catabolic process | |
Biological Process | putrescine biosynthetic process | |
Biological Process | spermidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArginine decarboxylase 2
- EC number
- Short namesARGDC2; OsADC2
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ7XRA1
- Secondary accessions
Proteomes
Genome annotation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000392206 | 1-623 | UniProt | Arginine decarboxylase 2 | |||
Sequence: MAKKNYGQVYNILGWGDPYFTVNSHGHLAVKPHGRDTMSGQDIDVHSVIHRALATTITTNDGDKKPQFPMILRFPDVLKNRLDSLHAAFHGAVDSTGYASRYQGVFPIKVNQNKAVVQDLVTFGHGYSYGLEAGSKPELLIAMSCLAKAKPGAYLVCNGYKDADYVALALSARAMGLNAIIVLEMEEELDIVVEQSARLGVEPVIGVRAKLLTKIPGHFGSTAGKHGKFGMLADKIYEVAGKLKKMGKLHWLKLLHYHVGSMIPTTDIVYNAAAEAAGIYCALVKEHGATGMTTLDCGGGLGVDYDGTRSGSSDMSVAYGLEQYASSIVQAVRLTCDDNGVPHPVLCTESGRAMASHHSMIILEALSAIPEPQDEEDTHHRLLSKIQDLSSKQPRTAHTVNGGGGVDAMHSHAVELKKHGIEMYKLAKKLSKRVTGDANGIYNYHMNLSVFSLVPDFWGIGQLFPMMPVSRLNEKPTINGTLVDITCDSDGKVEKFIRDAVTLPLHPLDDAAAEHGGYYVAALLSGAYQEALACKHNLFSGPTLVRVESAGGGGAFKIVSVELGPTAEEVIGTMRYDVKNDISDVIEKVATENGVWPMVEPLMKKGLTTMPYLNDYKPPKTTF | |||||||
Modified residue | 109 | UniProt | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 390 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Tissue specificity
Expressed in stems (at protein level).
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length623
- Mass (Da)67,335
- Last updated2004-03-01 v2
- ChecksumA4980874AE0FBA87
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FJ746894 EMBL· GenBank· DDBJ | ACN65507.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AL606620 EMBL· GenBank· DDBJ | CAE02767.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008210 EMBL· GenBank· DDBJ | BAF13932.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014960 EMBL· GenBank· DDBJ | BAS87548.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000141 EMBL· GenBank· DDBJ | EAZ29450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK058573 EMBL· GenBank· DDBJ | BAG86737.1 EMBL· GenBank· DDBJ | mRNA | ||
AK121110 EMBL· GenBank· DDBJ | BAH00321.1 EMBL· GenBank· DDBJ | mRNA |