P24168 (CATA_LISSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 67.
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: Catalase EC=1.11.1.6 | ||
| Gene names |
| ||
| Organism | Listeria seeligeri | ||
| Taxonomic identifier | 1640 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 488 AA. |
| Sequence status | Complete. |
| 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 H2O2 = O2 + 2 H2O. |
| Cofactor | Heme group. |
| Subcellular location | Cytoplasm Probable. |
| 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 |
| Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | catalase activity Inferred from electronic annotation. Source: EC heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases." Haas A., Brehm K., Kreft J., Goebel W. J. Bacteriol. 173:5159-5167(1991) [PubMed: 1860824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M75944 Genomic DNA. Translation: AAB53655.1. |
| PIR | A40367. |
3D structure databases | |
| ProteinModelPortal | P24168. |
| SMR | P24168. Positions 5-480. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR018028. Catalase. IPR020835. Catalase-like_dom. IPR024708. Catalase_AS. IPR024711. Catalase_clade1/3. IPR011614. Catalase_core. IPR002226. Catalase_haem_BS. IPR010582. Catalase_immune_responsive. [Graphical view] |
| Gene3D | G3DSA:2.40.180.10. Catalase_N. 1 hit. |
| PANTHER | PTHR11465. Catalase. 1 hit. |
| Pfam | PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view] |
| PIRSF | PIRSF038928. Catalase_clade1-3. 1 hit. |
| PRINTS | PR00067. CATALASE. |
| SMART | SM01060. Catalase. 1 hit. [Graphical view] |
| SUPFAM | SSF56634. Catalase_N. 1 hit. |
| 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_LISSE | ||||||||
| Accession | Primary (citable) accession number: P24168 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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