Reviewed,
UniProtKB/Swiss-Prot P0AGD2 (SODC_ECO57)
Last modified
December 15, 2009.
Version 32.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Superoxide dismutase [Cu-Zn] EC=1.15.1.1 Alternative name(s): Bacteriocuprein | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 173 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 By similarity. |
| 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 | Monomer By similarity. |
| Subcellular location | Periplasm By similarity. |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | By similarity | ||||||||
| Chain | 20 – 173 | 154 | Superoxide dismutase [Cu-Zn] | PRO_0000045306 | |||||||
Sites | |||||||||||
| Metal binding | 67 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 69 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 92 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 92 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 101 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 109 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 112 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 147 | 1 | Copper; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 74 ↔ 169 | By similarity | |||||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG56635.1. BA000007 Genomic DNA. Translation: BAB35778.1. | |
| PIR | C90923. G85771. |
| RefSeq | NP_288082.1. NP_310382.1. |
3D structure databases | |
| SMR | P0AGD2. Positions 20-173. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 914926. 961605. |
| GenomeReviews | Gene locus Z2661 in contig AE005174_GR. Gene locus ECs2355 in contig BA000007_GR. |
| KEGG | ece:Z2661. ecs:ECs2355. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG609879. |
| OMA | HGFHLHA. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS2355-MON. |
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] |
| PROSITE | PS00087. SOD_CU_ZN_1. False negative. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODC_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AGD2 Secondary accession number(s): P53635, P96756 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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