Reviewed,
UniProtKB/Swiss-Prot Q8Y3P9 (CATA_LISMO)
Last modified
November 25, 2008.
Version 44.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Catalase EC=1.11.1.6 | ||||
| Gene names |
| ||||
| Organism | Listeria monocytogenes [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1639 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 488 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. |
| Catalytic activity | 2 H(2)O(2) = O(2) + 2 H(2)O. |
| Cofactor | Heme group. |
| Subcellular location | CytoplasmProbable. |
| Sequence similarities | Belongs to the catalase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Cellular component | Cytoplasm |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | catalase activity Inferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. Cossart P.Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a. |
Cross-references
Sequence databases | |
|---|---|
| AL591984 Genomic DNA. Translation: CAD00998.1. | |
| PIR | AH1422. |
| RefSeq | NP_466307.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M7S based on UniProtKB P46206. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 984948. |
| GenomeReviews | Gene locus lmo2785 in contig AL591824_GR. |
| KEGG | lmo:lmo2785. |
Organism-specific databases | |
| ListiList | LMO02785. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8Y3P9. |
Enzyme and pathway databases | |
| BioCyc | LMON169963:LMO2785-MON. |
Family and domain databases | |
| InterPro | IPR002226. Catalase. IPR011614. Catalase_N. [Graphical view] |
| Gene3D | G3DSA:2.40.180.10. Catalase_N. 1 hit. |
| PANTHER | PTHR11465. Catalase. 1 hit. |
| Pfam | PF00199. Catalase. 1 hit. [Graphical view] |
| PRINTS | PR00067. CATALASE. |
| ProDom | PD000510. Catalase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATA_LISMO | ||||||||
| Accession | Primary (citable) accession number: Q8Y3P9 | ||||||||
| 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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