Reviewed,
UniProtKB/Swiss-Prot P0A325 (CATA_BORPA)
Last modified
June 16, 2009.
Version 26.
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 | Bordetella parapertussis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 519 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 482 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 H2O2 = O2 + 2 H2O. |
| Cofactor | Heme group By similarity. |
| Subunit structure | Homodimer By similarity. |
| 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 |
| 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: EC heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253. |
Cross-references
Sequence databases | |
|---|---|
| BX640436 Genomic DNA. Translation: CAE39685.1. | |
| RefSeq | NP_886532.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M85 based on UniProtKB P42321. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0A325. |
Genome annotation databases | |
| GeneID | 1666639. |
| GenomeReviews | Gene locus BPP4406 in contig BX470249_GR. |
| KEGG | bpa:BPP4406. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A325. |
| OMA | P0A325. NIARHIN. |
Enzyme and pathway databases | |
| BioCyc | BPAR257311:BPP4406-MON. |
| BRENDA | 1.11.1.6. 263123. |
Family and domain databases | |
| InterPro | IPR002226. Catalase. IPR010582. Catalase-rel_immune_responsive. IPR011614. Catalase_N. IPR018028. Catalase_rel_subgroup. [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] |
| 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_BORPA | ||||||||
| Accession | Primary (citable) accession number: P0A325 Secondary accession number(s): P48062 | ||||||||
| 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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