Q7Z7W6 (KATG_ASPFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 64.
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 | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) | ||||||
| Taxonomic identifier | 330879 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 759 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May be involved in protection from the host during host infection. Ref.1 |
| Catalytic activity | Donor + H2O2 = oxidized donor + 2 H2O. 2 H2O2 = O2 + 2 H2O. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group. |
| Enzyme regulation | Sensitive to heat and heavy metals. Ref.1 |
| Subunit structure | Monomer. Ref.1 |
| Post-translational modification | Not glycosylated. 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 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 – 759 | 759 | Catalase-peroxidase | PRO_0000354100 | |||||||
Sites | |||||||||||
| Active site | 97 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 283 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 93 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 96 ↔ 242 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-268) By similarity | |||||||||
| Cross-link | 242 ↔ 268 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96) By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Catalases of Aspergillus fumigatus." Paris S., Wysong D., Debeaupuis J.-P., Shibuya K., Philippe B., Diamond R.D., Latge J.-P. Infect. Immun. 71:3551-3562(2003) [PubMed: 12761140] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 385-397, SUBUNIT, ENZYME REGULATION, FUNCTION. |
| [2] | "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. Denning D.W.Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY125354 Genomic DNA. Translation: AAM95780.1. AAHF01000014 Genomic DNA. Translation: EAL85001.1. |
| RefSeq | XP_747039.1. XM_741946.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ITK based on UniProtKB O59651. |
| ProteinModelPortal | Q7Z7W6. |
| SMR | Q7Z7W6. Positions 21-749. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q7Z7W6. |
Protein family/group databases | |
| Allergome | 8994. Asp f CP. |
| PeroxiBase | 1881. AfumCP01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADAFUAT00000896; CADAFUAP00000896; CADAFUAG00000896. |
| GeneID | 3504583. |
| GenomeReviews | Gene locus katG in contig CM000176_GR. |
| KEGG | afm:AFUA_8G01670. |
Phylogenomic databases | |
| eggNOG | fuNOG06405. |
| GeneTree | EFGT00050000003307. |
| HOGENOM | HBG285610. |
| OMA | KRHAPSM. |
| OrthoDB | EOG41CB4B. |
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. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KATG_ASPFU | ||||||||
| Accession | Primary (citable) accession number: Q7Z7W6 Secondary accession number(s): Q4WBB1 | ||||||||
| 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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