Reviewed,
UniProtKB/Swiss-Prot P11964 (SODCP_PEA)
Last modified
June 16, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Superoxide dismutase [Cu-Zn], chloroplastic EC=1.15.1.1 | ||||
| Gene names |
| ||||
| Organism | Pisum sativum (Garden pea) | ||||
| Taxonomic identifier | 3888 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum |
Protein attributes
| Sequence length | 202 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| Catalytic activity | 2 superoxide + 2 H+ = O2 + H2O2. |
| Cofactor | Binds 1 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from electronic annotation. Source: EC zinc 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 48 | 48 | Chloroplast | ||||||||
| Chain | 49 – 202 | 154 | Superoxide dismutase [Cu-Zn], chloroplastic | PRO_0000032848 | |||||||
Sites | |||||||||||
| Metal binding | 94 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 96 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 111 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 111 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 119 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 128 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 131 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 168 | 1 | Copper; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 105 ↔ 194 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 55 | 1 | S → A | ||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and characterization of a cDNA encoding the chloroplastic copper/zinc-superoxide dismutase from pea." Scioli J.R., Zilinskas B.A. Proc. Natl. Acad. Sci. U.S.A. 85:7661-7665(1988) [PubMed: 2845417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Sequence divergence of pea Cu/Zn superoxide dismutase II cDNAs." Isin S.H., Burke J.J., Allen R.D. Plant Mol. Biol. 15:789-791(1990) [PubMed: 2102887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| J04087 mRNA. Translation: AAA33688.1. X56435 mRNA. Translation: CAA39819.1. | |
| PIR | DSPMCZ. A30204. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1SRD based on UniProtKB P07505. |
| SMR | P11964. Positions 49-202. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.15.1.1. 287. |
Family and domain databases | |
| InterPro | IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn. [Graphical view] |
| Gene3D | G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit. |
| PANTHER | PTHR10003. SOD_Cu_Zn. 1 hit. |
| Pfam | PF00080. Sod_Cu. 1 hit. [Graphical view] |
| PRINTS | PR00068. CUZNDISMTASE. |
| ProDom | PD000469. SOD_CU_ZN. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODCP_PEA | ||||||||
| Accession | Primary (citable) accession number: P11964 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


