Reviewed,
UniProtKB/Swiss-Prot Q6FMG7 (CCPR_CANGA)
Last modified
November 3, 2009.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome c peroxidase, mitochondrial Short name=CCP EC=1.11.1.5 | ||
| Gene names |
| ||
| Organism | Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome] | ||
| Taxonomic identifier | 5478 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces |
Protein attributes
| Sequence length | 357 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. |
| Catalytic activity | 2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. |
| Subunit structure | Forms a one-to-one complex with cytochrome c By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Cytochrome c peroxidase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stressInferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cytochrome-c peroxidase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 23 | 23 | Mitochondrion Potential | ||||||
| Chain | 24 – 357 | 334 | Cytochrome c peroxidase, mitochondrial | PRO_0000045288 | |||||
Regions | |||||||||
| Compositional bias | 49 – 55 | 7 | Poly-Asn | ||||||
| Compositional bias | 60 – 67 | 8 | Poly-Ala | ||||||
Sites | |||||||||
| Active site | 116 | 1 | Proton acceptor By similarity | ||||||
| Active site | 255 | 1 | Tryptophan radical intermediate By similarity | ||||||
| Metal binding | 239 | 1 | Iron (heme axial ligand) | ||||||
| Site | 112 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65. |
Cross-references
Sequence databases | |
|---|---|
| CR380957 Genomic DNA. Translation: CAG61540.1. | |
| RefSeq | XP_448577.1. |
3D structure databases | |
| SMR | Q6FMG7. Positions 69-357. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6FMG7. |
Protein family/group databases | |
| PeroxiBase | 2366. CglCcP01. |
Genome annotation databases | |
| GeneID | 2890345. |
| GenomeReviews | Gene locus CAGL0K08184g in contig CR380957_GR. |
| KEGG | cgr:CAGL0K08184g. |
Phylogenomic databases | |
| HOGENOM | Q6FMG7. |
| OMA | HALGKTH. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.5. 189220. |
Family and domain databases | |
| InterPro | IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| Pfam | PF00141. peroxidase. 1 hit. [Graphical view] |
| PRINTS | PR00459. ASPEROXIDASE. PR00458. PEROXIDASE. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CCPR_CANGA | ||||||||
| Accession | Primary (citable) accession number: Q6FMG7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


