Q0U324 (KATG_PHANO) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 40.
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-peroxidase Short name=CP EC=1.11.1.21 Alternative name(s): Peroxidase/catalase | ||||
| Gene names |
| ||||
| Organism | Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum) | ||||
| Taxonomic identifier | 321614 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Phaeosphaeriaceae › Phaeosphaeria |
Protein attributes
| Sequence length | 751 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. |
| Catalytic activity | Donor + H2O2 = oxidized donor + 2 H2O. 2 H2O2 = O2 + 2 H2O. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. |
| Subunit structure | Homodimer or homotetramer By similarity. |
| Post-translational modification | The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Peroxidase/catalase subfamily. |
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: InterPro 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 – 751 | 751 | Catalase-peroxidase | PRO_0000354109 | |||||||
Sites | |||||||||||
| Active site | 93 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 281 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 89 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 92 ↔ 240 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-266) By similarity | |||||||||
| Cross-link | 240 ↔ 266 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-92) By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum." Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P. Plant Cell 19:3347-3368(2007) [PubMed: 18024570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SN15 / ATCC MYA-4574 / FGSC 10173. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CH445352 Genomic DNA. Translation: EAT78864.1. |
| RefSeq | XP_001804042.1. XM_001803990.1. |
3D structure databases | |
| ProteinModelPortal | Q0U324. |
| SMR | Q0U324. Positions 17-746. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 3449. PnoCP01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | SNOT_13840; SNOT_13840; SNOG_13840. |
| GeneID | 5980964. |
| KEGG | pno:SNOG_13840. |
Phylogenomic databases | |
| OMA | KRHAPSM. |
| OrthoDB | EOG41CB4B. |
| PhylomeDB | Q0U324. |
Family and domain databases | |
| InterPro | IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| KO | K03782. |
| Pfam | PF00141. peroxidase. 2 hits. [Graphical view] |
| PRINTS | PR00460. BPEROXIDASE. PR00458. PEROXIDASE. |
| SUPFAM | SSF48113. Peroxidase_super. 2 hits. |
| TIGRFAMs | TIGR00198. Cat_per_HPI. 1 hit. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KATG_PHANO | ||||||||
| Accession | Primary (citable) accession number: Q0U324 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with