O59924 (SODC_CANAX) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 66.
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: Superoxide dismutase [Cu-Zn] EC=1.15.1.1 | ||
| Gene names |
| ||
| Organism | Candida albicans (Yeast) | ||
| Taxonomic identifier | 5476 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 154 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
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 | Homodimer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | cellular response to oxidative stress Inferred from mutant phenotype. Source: CGD hyphal growthInferred from mutant phenotype. Source: CGD pathogenesisInferred from mutant phenotype. Source: CGD superoxide metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytosol Non-traceable author statement. Source: UniProtKB |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from direct assay Ref.1. Source: CGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 154 | 153 | Superoxide dismutase [Cu-Zn] | PRO_0000164112 | |||||||
Sites | |||||||||||
| Metal binding | 47 | 1 | Copper By similarity | ||||||||
| Metal binding | 49 | 1 | Copper By similarity | ||||||||
| Metal binding | 64 | 1 | Copper By similarity | ||||||||
| Metal binding | 64 | 1 | Zinc By similarity | ||||||||
| Metal binding | 72 | 1 | Zinc By similarity | ||||||||
| Metal binding | 81 | 1 | Zinc By similarity | ||||||||
| Metal binding | 84 | 1 | Zinc By similarity | ||||||||
| Metal binding | 121 | 1 | Copper By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 58 ↔ 147 | By similarity | |||||||||
Sequences
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References
| [1] | "Copper- and zinc-containing superoxide dismutase and its gene from Candida albicans." Hwang C.S., Rhie G., Kim S.T., Kim Y.R., Huh W.K., Baek Y.U., Kang S.O. Biochim. Biophys. Acta 1427:245-255(1999) [PubMed: 10216241] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF046872 Genomic DNA. Translation: AAC12872.1. |
3D structure databases | |
| ProteinModelPortal | O59924. |
| SMR | O59924. Positions 2-153. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O59924. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| CGD | CAL0006717. SOD1. |
Phylogenomic databases | |
| OMA | EEERHAG. |
| PhylomeDB | O59924. |
Family and domain databases | |
| InterPro | IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [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. |
| SUPFAM | SSF49329. SOD_Cu_Zn. 1 hit. |
| PROSITE | PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODC_CANAX | ||||||||
| Accession | Primary (citable) accession number: O59924 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with