A1KFQ4 (A1KFQ4_MYCBP) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Superoxide dismutase [Cu-Zn] RuleBase RU000393 EC=1.15.1.1 RuleBase RU000393 | ||||
| Gene names |
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| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] EMBL CAL70456.1 | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › ![]() |
Protein attributes
| Sequence length | 240 AA. |
| Sequence status | Complete. |
| 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 By similarity. RuleBase RU000393 |
| Catalytic activity | 2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000393 |
| Cofactor | Binds 1 copper ion per subunit By similarity. RuleBase RU000393 Binds 1 zinc ion per subunit By similarity. RuleBase RU000393 |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. RuleBase RU000393 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Copper RuleBase RU000393 Metal-binding RuleBase RU000393 Zinc RuleBase RU000393 |
| Molecular function | Oxidoreductase RuleBase RU000393 EMBL CAL70456.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | superoxide metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM408590 Genomic DNA. Translation: CAL70456.1. |
| RefSeq | YP_976569.1. NC_008769.1. |
3D structure databases | |
| ProteinModelPortal | A1KFQ4. |
| SMR | A1KFQ4. Positions 70-240. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 410289.BCG_0471. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL70456; CAL70456; BCG_0471. |
| GeneID | 4697120. |
| KEGG | mbb:BCG_0471. |
| PATRIC | 18011459. VBIMycBov80988_0509. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2032. |
| HOGENOM | HOG000263448. |
| KO | K04565. |
| OMA | YNQTNGT. |
| ProtClustDB | CLSK790516. |
Enzyme and pathway databases | |
| BioCyc | MBOV410289:GJW7-477-MONOMER. |
Family and domain databases | |
| Gene3D | 2.60.40.200. 1 hit. |
| InterPro | IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view] |
| PANTHER | PTHR10003. PTHR10003. 1 hit. |
| Pfam | PF00080. Sod_Cu. 1 hit. [Graphical view] |
| SUPFAM | SSF49329. SOD_Cu_Zn. 1 hit. |
| PROSITE | PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | A1KFQ4_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KFQ4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
