E1PB64 (E1PB64_ECOAB) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 23.
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 coli OR:K5:H- (strain ABU 83972) [Complete proteome] [HAMAP] EMBL ADN46444.1 | ||||
| Taxonomic identifier | 655817 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 178 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 ADN46444.1 |
| 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] | "Host imprints on bacterial genomes--rapid, divergent evolution in individual patients." Zdziarski J., Brzuszkiewicz E., Wullt B., Liesegang H., Biran D., Voigt B., Gronberg-Hernandez J., Ragnarsdottir B., Hecker M., Ron E.Z., Daniel R., Gottschalk G., Hacker J., Svanborg C., Dobrindt U. PLoS Pathog. 6:e1001078-e1001078(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ABU 83972 EMBL ADN46444.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001671 Genomic DNA. Translation: ADN46444.1. |
| RefSeq | YP_006105975.1. NC_017631.1. |
3D structure databases | |
| ProteinModelPortal | E1PB64. |
| SMR | E1PB64. Positions 25-178. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADN46444; ADN46444; ECABU_c18990. |
| GeneID | 12727256. |
| KEGG | eab:ECABU_c18990. |
| PATRIC | 42948502. VBIEscCol35126_1985. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000263449. |
| KO | K04565. |
| OMA | NTNSHQG. |
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 | E1PB64_ECOAB | ||||||||
| Accession | Primary (citable) accession number: E1PB64 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
