Q59296 (CATA_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 73.
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 | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 507 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. |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 507 | 507 | Catalase | PRO_0000084983 | |||||
Sites | |||||||||
| Active site | 52 | 1 | By similarity | ||||||
| Active site | 124 | 1 | By similarity | ||||||
| Metal binding | 334 | 1 | Iron (heme axial ligand) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 23 | 1 | T → A in CAL35497. Ref.2 | ||||||
| Sequence conflict | 82 | 1 | I → V in CAL35497. Ref.2 | ||||||
| Sequence conflict | 177 | 1 | R → S in CAL35497. Ref.2 | ||||||
| Sequence conflict | 283 | 1 | L → F in CAL35497. Ref.2 | ||||||
| Sequence conflict | 440 | 1 | T → A in CAL35497. Ref.2 | ||||||
| Sequence conflict | 455 | 1 | E → K in CAL35497. Ref.2 | ||||||
| Sequence conflict | 472 – 507 | 36 | FPIVS…YEPEA → LEK in CAL35497. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange." Grant K.A., Park S.F. Microbiology 141:1369-1376(1995) [PubMed: 7670638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33560 / CIP 702 / DSM 4688 / NCTC 11351. |
| [2] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X85130 Genomic DNA. Translation: CAA59444.1. AL111168 Genomic DNA. Translation: CAL35497.1. |
| PIR | F81283. I40767. |
| RefSeq | YP_002344773.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | Q59296. |
| SMR | Q59296. Positions 2-474. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q59296. 39 interactions. |
Protein family/group databases | |
| PeroxiBase | 5383. CjejKat01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 905678. |
| GenomeReviews | Gene locus Cj1385 in contig AL111168_GR. |
| KEGG | cje:Cj1385. |
| PATRIC | 20059735. VBICamJej33762_1366. |
Phylogenomic databases | |
| HOGENOM | HBG339355. |
| ProtClustDB | CLSK879231. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ1385-MONOMER. |
Family and domain databases | |
| InterPro | IPR018028. Catalase. IPR020835. Catalase-like_dom. 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. |
| KO | K03781. |
| 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. False negative. PS51402. CATALASE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATA_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q59296 Secondary accession number(s): Q0P8M4 | ||||||||
| 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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