Reviewed,
UniProtKB/Swiss-Prot Q939D2 (KATG_BURPS)
Last modified
May 26, 2009.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 |
| ||||
| Organism | Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 28450 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group |
Protein attributes
| Sequence length | 728 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity. Ref.4 |
| 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 subunit. HAMAP MF_01961 |
| Subunit structure | |
| Post-translational modification | The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme. HAMAP MF_01961 |
| Sequence similarities | Belongs to the peroxidase family. Peroxidase/catalase subfamily. |
| biophysicochemical properties | Kinetic parameters: KM=56 mM for H2O2 for the catalase reaction (at pH 5.5-6.0) HAMAP MF_01961 KM=4.5 mM for H2O2 for the catalase reaction (at pH 7.0) KM=700 µM for H2O2 for the peroxidase reaction KM=300 µM for ABTS for the peroxidase reaction KM=12.5 µM for NADH for the oxidase reaction Vmax=11900 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0) Vmax=4300 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0) Vmax=6.0 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.5 for the peroxidase reaction, 6.0 for the catalase reaction, and 8.75 for the NADH oxidase reaction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.3 | ||||||||
| Chain | 2 – 728 | 727 | Catalase-peroxidase HAMAP MF_01961 | PRO_0000345092 | |||||||
Sites | |||||||||||
| Active site | 92 | 1 | Proton acceptor HAMAP MF_01961 | ||||||||
| Metal binding | 259 | 1 | Iron (heme axial ligand) HAMAP MF_01961 | ||||||||
| Site | 88 | 1 | Transition state stabilizer HAMAP MF_01961 | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 91 ↔ 218 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) HAMAP MF_01961 | |||||||||
| Cross-link | 218 ↔ 244 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) HAMAP MF_01961 | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Burkholderia pseudomallei oxyR gene: expression analysis and mutant characterization." Loprasert S., Sallabhan R., Whangsuk W., Mongkolsuk S. Gene 296:161-169(2002) [PubMed: 12383513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243. |
| [3] | "Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry." Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T., Singh R., Switala J., Carpena X., Fita I., Loewen P.C. J. Biol. Chem. 278:35687-35692(2003) [PubMed: 12832453] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5, COVALENT BOND. |
| [4] | "Catalase-peroxidases (KatG) exhibit NADH oxidase activity." Singh R., Wiseman B., Deemagarn T., Donald L.J., Duckworth H.W., Carpena X., Fita I., Loewen P.C. J. Biol. Chem. 279:43098-43106(2004) [PubMed: 15280362] [Abstract] Cited for: FUNCTION. |
| [5] | "Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis." Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C. Biochemistry 46:1183-1193(2007) [PubMed: 17260948] [Abstract] Cited for: CATALYTIC MECHANISM. |
| [6] | "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. |
| [7] | "Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution." Carpena X., Loprasert S., Mongkolsuk S., Switala J., Loewen P.C., Fita I. J. Mol. Biol. 327:475-489(2003) [PubMed: 12628252] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-728 IN COMPLEX WITH HEME, SUBUNIT. |
| [8] | "Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei." Deemagarn T., Carpena X., Singh R., Wiseman B., Fita I., Loewen P.C. J. Mol. Biol. 345:21-28(2005) [PubMed: 15567407] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-304 IN COMPLEX WITH HEME, SUBUNIT. |
| [9] | "A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases." Carpena X., Wiseman B., Deemagarn T., Singh R., Switala J., Ivancich A., Fita I., Loewen P.C. EMBO Rep. 6:1156-1162(2005) [PubMed: 16211084] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| AY040244 Genomic DNA. Translation: AAK72466.3. Different initiation. BX571965 Genomic DNA. Translation: CAH36875.1. Different initiation. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| RefSeq | YP_109459.1. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PeroxiBase | 2303. BpCP01. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneID | 3092072. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus BPSL2865 in contig BX571965_GR. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG | bps:BPSL2865. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOGENOM | Q939D2. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| BioCyc | BPSE272560:BPSL2865-MON. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| BRENDA | 1.11.1.6. 275934. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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_BURPS | ||||||||
| Accession | Primary (citable) accession number: Q939D2 Secondary accession number(s): Q63R09 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


