Q8X182 (KATG_NEUCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 80.
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): Catalase-2 Peroxidase/catalase | ||||||
| Gene names |
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| Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) | ||||||
| Taxonomic identifier | 367110 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora |
Protein attributes
| Sequence length | 753 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. |
| 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. Ref.1 |
| Enzyme regulation | Inhibited by KCN. Ref.1 |
| Subunit structure | Homodimer or homotetramer By similarity. |
| Induction | Induced in late stationary growth phase. Ref.1 |
| 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. |
| Biophysicochemical properties | Kinetic parameters: KM=13.2 mM for H2O2 for the catalase reaction Ref.1 pH dependence: Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the catalase reaction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome Direct protein sequencing 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 – 753 | 753 | Catalase-peroxidase | PRO_0000055582 | |||||||
Sites | |||||||||||
| Active site | 91 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 279 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 87 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 90 ↔ 238 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) By similarity | |||||||||
| Cross-link | 238 ↔ 264 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-90) By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Neurospora crassa catalases, singlet oxygen and cell differentiation." Peraza L., Hansberg W. Biol. Chem. 383:569-575(2002) [PubMed: 12033445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 654-670, HEME-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION. |
| [2] | "The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. Birren B.W.Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF459787 mRNA. Translation: AAL66352.2. AABX02000023 Genomic DNA. Translation: EAA30509.1. |
| RefSeq | XP_959745.1. XM_954652.2. |
3D structure databases | |
| ProteinModelPortal | Q8X182. |
| SMR | Q8X182. Positions 15-741. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8X182. |
Protein family/group databases | |
| PeroxiBase | 2181. NcCP01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | EFNCRT00000005784; EFNCRP00000005777; EFNCRG00000005774. |
| GeneID | 3875883. |
| KEGG | ncr:NCU05770. |
| NMPDR | fig|5141.1.peg.3558. |
Phylogenomic databases | |
| eggNOG | fuNOG06405. |
| GeneTree | EFGT00050000003307. |
| OMA | KRHAPSM. |
| OrthoDB | EOG41CB4B. |
Enzyme and pathway databases | |
| BioCyc | NCRA-XX3-01:NCRA-XX3-01-009518-MONOMER. |
| BRENDA | 1.11.1.6. 3627. |
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_NEUCR | ||||||||
| Accession | Primary (citable) accession number: Q8X182 Secondary accession number(s): Q7S4Q3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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