Reviewed,
UniProtKB/Swiss-Prot P07820 (CATA_CANTR)
Last modified
June 16, 2009.
Version 69.
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: Peroxisomal catalase EC=1.11.1.6 Alternative name(s): PXP-9 | ||
| Gene names |
| ||
| Organism | Candida tropicalis (Yeast) | ||
| Taxonomic identifier | 5482 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 485 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. |
| Catalytic activity | 2 H2O2 = O2 + 2 H2O. |
| Cofactor | Heme group. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the catalase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Cellular component | Peroxisome |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | 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 |
| Cellular component | peroxisome 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 485 | 484 | Peroxisomal catalase | PRO_0000084920 | |||||
Sites | |||||||||
| Active site | 53 | 1 | By similarity | ||||||
| Active site | 126 | 1 | By similarity | ||||||
| Metal binding | 336 | 1 | Iron (heme axial ligand) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 166 | 1 | T → S in AAA34327. Ref.2 | ||||||
| Sequence conflict | 377 | 1 | L → V in CAA29093. Ref.4 | ||||||
| Sequence conflict | 390 | 1 | I → V in AAA34327. Ref.2 | ||||||
Sequences
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References
| [1] | "Catalase gene of the yeast Candida tropicalis. Sequence analysis and comparison with peroxisomal and cytosolic catalases from other sources." Okada H., Ueda M., Sugaya T., Atomi H., Mozaffar S., Hishida T., Teranishi Y., Okazaki K., Takechi T., Kamiryo T., Tanaka A. Eur. J. Biochem. 170:105-110(1987) [PubMed: 3691514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The nucleotide sequence of complementary DNA and the deduced amino acid sequence of peroxisomal catalase of the yeast Candida tropicalis pK233." Murray W.W., Rachubinski R.A. Gene 61:401-413(1987) [PubMed: 3446581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 20336 / pK233 / NCYC 997. |
| [3] | "Nucleotide sequence of peroxisomal catalase from the yeast Candida tropicalis pK233: identification of an upstream BamHI site polymorphism." Murray W.W., Rachubinski R.A. Nucleic Acids Res. 17:3600-3600(1989) [PubMed: 2726500] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20336 / pK233 / NCYC 997. |
| [4] | "Isolation of cDNA clones coding for peroxisomal proteins of Candida tropicalis: identification and sequence of a clone for catalase." Rachubinski R.A., Fujiki Y., Lazarow P.B. Biochim. Biophys. Acta 909:35-43(1987) [PubMed: 3580373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-385. Strain: ATCC 20336 / pK233 / NCYC 997. |
| [5] | "Isolation of several cDNAs encoding yeast peroxisomal enzymes." Ueda M., Okada H., Hishida T., Teranishi Y., Tanaka A. FEBS Lett. 220:31-35(1987) [PubMed: 2440725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 394-451, PARTIAL PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| M18832 mRNA. Translation: AAA34327.1. X05886 mRNA. Translation: CAA29310.1. X05604 mRNA. Translation: CAA29093.1. X06660 Genomic DNA. Translation: CAA29859.1. X13978 Genomic DNA. Translation: CAA32159.1. | |
| PIR | CSCKPT. A29629. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A4E based on UniProtKB P15202. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 5256. CtKat01. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.6. 1242. |
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_CANTR | ||||||||
| Accession | Primary (citable) accession number: P07820 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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