A1UAE2 (A1UAE2_MYCSK) 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 |
| ||
| Organism | Mycobacterium sp. (strain KMS) [Complete proteome] [HAMAP] EMBL ABL89800.1 | ||
| Taxonomic identifier | 189918 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium![]() |
Protein attributes
| Sequence length | 228 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 |
| 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] | "Complete sequence of chromosome of Mycobacterium sp. KMS." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. Richardson P.Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KMS EMBL ABL89800.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000518 Genomic DNA. Translation: ABL89800.1. |
| RefSeq | YP_936590.1. NC_008705.1. |
3D structure databases | |
| ProteinModelPortal | A1UAE2. |
| SMR | A1UAE2. Positions 57-227. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 189918.Mkms_0584. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABL89800; ABL89800; Mkms_0584. |
| GeneID | 4614967. |
| KEGG | mkm:Mkms_0584. |
| PATRIC | 18100124. VBIMycSp70743_1113. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2032. |
| HOGENOM | HOG000263448. |
| KO | K04565. |
| OMA | YNQTNGT. |
| ProtClustDB | CLSK790516. |
Enzyme and pathway databases | |
| BioCyc | MSP189918:GH4X-641-MONOMER. |
Family and domain databases | |
| Gene3D | 2.60.40.200. 1 hit. |
| InterPro | IPR024136. SOD_Cu/Zn. IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view] |
| PANTHER | PTHR10003. PTHR10003. 1 hit. PTHR10003:SF11. PTHR10003:SF11. 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 | A1UAE2_MYCSK | ||||||||
| Accession | Primary (citable) accession number: A1UAE2 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
