P22220 (SPE1_AVESA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Arginine decarboxylase Short name=ADC Short name=ARGDC EC=4.1.1.19 | ||
| Gene names |
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| Organism | Avena sativa (Oat) | ||
| Taxonomic identifier | 4498 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Poeae › Aveninae › Avena |
Protein attributes
| Sequence length | 607 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 |
| Technical term | Direct protein sequencing |
| 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing." Bell E., Malmberg R.L. Mol. Gen. Genet. 224:431-436(1990) [PubMed: 2266946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 427-437. Tissue: Leaf. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X56802 mRNA. Translation: CAA40137.1. |
| PIR | S12265. |
3D structure databases | |
| ProteinModelPortal | P22220. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| Gramene | P22220. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-14981. |
Family and domain databases | |
| InterPro | IPR009006. Ala_racemase/Decarboxylase_C. IPR002985. Arg_decrbxlase. IPR022643. De-COase2_C. IPR022657. De-COase2_CS. IPR022644. De-COase2_N. IPR022653. De-COase2_pyr-phos_BS. IPR000183. Orn/DAP/Arg_de-COase. [Graphical view] |
| Gene3D | G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits. |
| PANTHER | PTHR11482:SF3. Arg_decrbxlase. 1 hit. |
| Pfam | PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view] |
| PIRSF | PIRSF001336. Arg_decrbxlase. 1 hit. |
| PRINTS | PR01180. ARGDCRBXLASE. PR01179. ODADCRBXLASE. |
| SUPFAM | SSF50621. Racem_decarbox_C. 1 hit. |
| PROSITE | PS00878. ODR_DC_2_1. 1 hit. PS00879. ODR_DC_2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SPE1_AVESA | ||||||||
| Accession | Primary (citable) accession number: P22220 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with