Reviewed,
UniProtKB/Swiss-Prot P45737 (CATA_BACFR)
Last modified
November 25, 2008.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Catalase EC=1.11.1.6 | ||||||
| Gene names |
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| Organism | Bacteroides fragilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 817 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides |
Protein attributes
| Sequence length | 486 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. May be involved in aerotolerance of B.fragilis. |
| Catalytic activity | 2 H(2)O(2) = O(2) + 2 H(2)O. |
| Cofactor | Heme group. |
| Subunit structure | Homodimer. |
| Induction | Up-regulated by oxygenation and stationary phase. |
| Sequence similarities | Belongs to the catalase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred 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
| « Hide 'large scale' references | |
| [1] | "Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis." Rocha E.R., Smith C.J. J. Bacteriol. 177:3111-3119(1995) [PubMed: 7768808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20. Strain: 638. |
| [2] | "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation." Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y. Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YCH46. |
Cross-references
Sequence databases | |
|---|---|
| U18676 Genomic DNA. Translation: AAC43384.1. AP006841 Genomic DNA. Translation: BAD47995.1. | |
| PIR | A57262. |
| RefSeq | YP_098529.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M85 based on UniProtKB P42321. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3082781. |
| GenomeReviews | Gene locus BF1245 in contig AP006841_GR. |
| KEGG | bfr:BF1245. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P45737. |
Enzyme and pathway databases | |
| BioCyc | BFRA295405:BF1245-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_BACFR | ||||||||
| Accession | Primary (citable) accession number: P45737 | ||||||||
| 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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