Reviewed,
UniProtKB/Swiss-Prot O81160 (SPE2_THECC)
Last modified
July 28, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Arginine decarboxylase Short name=ARGDC Short name=ADC EC=4.1.1.19 | ||
| Gene names |
| ||
| Organism | Theobroma cacao (Cacao) (Cocoa) | ||
| Taxonomic identifier | 3641 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Malvales › Malvaceae › Byttnerioideae › Theobroma |
Protein attributes
| Sequence length | 406 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | L-arginine = agmatine + CO2. |
| Cofactor | Pyridoxal phosphate. Magnesium. |
| Pathway | Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. |
| Sequence similarities | Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Putrescine biosynthesis Spermidine biosynthesis |
| Ligand | Magnesium Pyridoxal phosphate |
| Molecular function | Decarboxylase Lyase |
| Gene Ontology (GO) | |
| Biological process | arginine catabolic process Inferred from electronic annotation. Source: InterPro putrescine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW spermidine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | arginine decarboxylase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›406 | ›406 | Arginine decarboxylase | PRO_0000149955 | |||||
Regions | |||||||||
| Region | 192 – 202 | 11 | Substrate-binding By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 8 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 406 | 1 | |||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Phylogenetic utility of the nuclear gene arginine decarboxylase: an example from Brassicaceae." Galloway G.L., Malmberg R.L., Price R.A. Mol. Biol. Evol. 15:1312-1320(1998) [PubMed: 9787437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ADC. |
Cross-references
Sequence databases | |
|---|---|
| AF045666 Genomic DNA. Translation: AAC68511.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.1.1.19. 18928. |
Family and domain databases | |
| InterPro | IPR002985. Arg_decrbxlase. IPR000183. De-COase2. [Graphical view] |
| PANTHER | PTHR11482:SF3. Arg_decrbxlase. 1 hit. |
| Pfam | PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view] |
| PRINTS | PR01180. ARGDCRBXLASE. PR01179. ODADCRBXLASE. |
| PROSITE | PS00878. ODR_DC_2_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SPE2_THECC | ||||||||
| Accession | Primary (citable) accession number: O81160 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


