P66827 (SODC_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 48.
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 | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 174 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 | Homodimer By similarity. |
| Subcellular location | Periplasm By similarity. |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
| Sequence caution | The sequence AAN33888.1 differs from that shown. Reason: Erroneous initiation. The sequence AEM20163.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
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 | superoxide metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Potential | ||||||||
| Chain | 21 – 174 | 154 | Superoxide dismutase [Cu-Zn] | PRO_0000032822 | |||||||
Sites | |||||||||||
| Metal binding | 68 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 70 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 93 | 1 | Copper; catalytic By similarity | ||||||||
| Metal binding | 93 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 102 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 110 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 113 | 1 | Zinc; structural By similarity | ||||||||
| Metal binding | 148 | 1 | Copper; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 75 ↔ 170 | By similarity | |||||||||
Sequences
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References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014292 Genomic DNA. Translation: AAN33888.1. Different initiation. CP002998 Genomic DNA. Translation: AEM20163.1. Different initiation. |
| RefSeq | NP_699883.1. NC_004311.2. |
3D structure databases | |
| ProteinModelPortal | P66827. |
| SMR | P66827. Positions 21-174. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1165145. |
| GenomeReviews | Gene locus BRA0703 in contig AE014292_GR. |
| KEGG | bms:BRA0703. |
| PATRIC | 17794214. VBIBruSui107850_2918. |
| TIGR | BRA0703. |
Phylogenomic databases | |
| HOGENOM | HBG609879. |
| PhylomeDB | P66827. |
| ProtClustDB | CLSK898879. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_A0703-MONOMER. |
Family and domain databases | |
| InterPro | IPR024136. SOD_Cu/Zn. 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. |
| KO | K04565. |
| PANTHER | PTHR10003:SF11. PTHR10003:SF11. 1 hit. PTHR10003. SOD_Cu_Zn. 1 hit. |
| Pfam | PF00080. Sod_Cu. 1 hit. [Graphical view] |
| 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_BRUSU | ||||||||
| Accession | Primary (citable) accession number: P66827 Secondary accession number(s): G0KD75, P58645 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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