Reviewed,
UniProtKB/Swiss-Prot O28050 (KATG_ARCFU)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Catalase-peroxidase Short name=CP EC=1.11.1.6 EC=1.11.1.7 Alternative name(s): Peroxidase/catalase | ||||||
| Gene names |
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| Organism | Archaeoglobus fulgidus [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 2234 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus |
Protein attributes
| Sequence length | 741 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity. HAMAP MF_01961 |
| Catalytic activity | 2 H2O2 = O2 + 2 H2O. HAMAP MF_01961 Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961 |
| 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. |
| biophysicochemical properties | Kinetic parameters: KM=32 mM for H2O2 for the catalase reaction (at pH 5.5-6.0) HAMAP MF_01961 KM=3.8 mM for H2O2 for the catalase reaction (at pH 7.0) KM=95 mM for H2O2 for the peroxidase reaction KM=16 mM for ABTS for the peroxidase reaction Vmax=11760 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0) Vmax=5500 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0) Vmax=12 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.5 for the peroxidase reaction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | catalase activity Inferred from electronic annotation. Source: HAMAP 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 – 741 | 741 | Catalase-peroxidase HAMAP MF_01961 | PRO_0000055579 | |||||||
Sites | |||||||||||
| Active site | 87 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 249 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 83 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 86 ↔ 208 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-234) By similarity | |||||||||
| Cross-link | 208 ↔ 234 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-86) By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C.Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126. |
| [2] | "Comparative study of catalase-peroxidases (KatGs)." Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C. Arch. Biochem. Biophys. 471:207-214(2008) [PubMed: 18178143] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES. |
Cross-references
Sequence databases | |
|---|---|
| AE000782 Genomic DNA. Translation: AAB89022.1. | |
| PIR | A69529. |
| RefSeq | NP_071058.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ITK based on UniProtKB O59651. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 1858. AfCP01. |
Genome annotation databases | |
| GeneID | 1485464. |
| GenomeReviews | Gene locus AF_2233 in contig AE000782_GR. |
| KEGG | afu:AF2233. |
| NMPDR | fig|224325.1.peg.2219. |
| TIGR | AF_2233. |
Phylogenomic databases | |
| HOGENOM | O28050. |
| OMA | O28050. FEWELTK. |
Enzyme and pathway databases | |
| BioCyc | AFUL224325:AF_2233-MON. |
| BRENDA | 1.11.1.6. 7576. |
Family and domain databases | |
| HAMAP | MF_01961. [Tree] |
| InterPro | IPR000763. Catalase_proxase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| Pfam | PF00141. peroxidase. 2 hits. [Graphical view] |
| PRINTS | PR00460. BPEROXIDASE. PR00458. PEROXIDASE. |
| 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_ARCFU | ||||||||
| Accession | Primary (citable) accession number: O28050 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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