B7LQM4 (B7LQM4_ESCF3) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 29.
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 | Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP] EMBL CAQ88917.1 | ||||
| Taxonomic identifier | 585054 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 173 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 CAQ88917.1 |
| 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] | "Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. Denamur E.PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU928158 Genomic DNA. Translation: CAQ88917.1. |
| RefSeq | YP_002382549.1. NC_011740.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 585054.EFER_1397. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAQ88917; CAQ88917; EFER_1397. |
| GeneID | 7122710. |
| KEGG | efe:EFER_1397. |
| PATRIC | 32127192. VBIEscFer122920_1350. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2032. |
| HOGENOM | HOG000263449. |
| KO | K04565. |
| ProtClustDB | PRK10290. |
Enzyme and pathway databases | |
| BioCyc | EFER585054:GJJM-1391-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 | B7LQM4_ESCF3 | ||||||||
| Accession | Primary (citable) accession number: B7LQM4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
