Q3JNW6 · KATG_BURP1
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids728 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Catalytic activity
- AH2 + H2O2 = A + 2 H2O
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Features
Showing features for site, active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | catalase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to hydrogen peroxide | |
Biological Process | hydrogen peroxide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCatalase-peroxidase
- EC number
- Short namesCP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > pseudomallei group
Accessions
- Primary accessionQ3JNW6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354748 | 1-728 | Catalase-peroxidase | |||
Sequence: MSNEAKCPFHQAAGNGTSNRDWWPNQLDLSILHRHSSLSDPMGKDFNYAQAFEKLDLAAVKRDLHALMTTSQDWWPADFGHYGGLFIRMAWHSAGTYRTADGRGGAGEGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGRAISWADLLILTGNVALESMGFKTFGFAGGRADTWEPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMGLIYVNPEGPDGNPDPVAAARDIRDTFARMAMNDEETVALIAGGHTFGKTHGAGPASNVGAEPEAAGIEAQGLGWKSAYRTGKGADAITSGLEVTWTTTPTQWSHNFFENLFGYEWELTKSPAGAHQWVAKGADAVIPDAFDPSKKHRPTMLTTDLSLRFDPAYEKISRRFHENPEQFADAFARAWFKLTHRDMGPRARYLGPEVPAEVLLWQDPIPAVDHPLIDAADAAELKAKVLASGLTVSQLVSTAWAAASTFRGSDKRGGANGARIRLAPQKDWEANQPEQLAAVLETLEAIRTAFNGAQRGGKQVSLADLIVLAGCAGVEQAAKNAGHAVTVPFAPGRADASQEQTDVESMAVLEPVADGFRNYLKGKYRVPAEVLLVDKAQLLTLSAPEMTVLLGGLRVLGANVGQSRHGVFTAREQALTNDFFVNLLDMGTEWKPTAADADVFEGRDRATGELKWTGTRVDLVFGSHSQLRALAEVYGSADAQEKFVRDFVAVWNKVMNLDRFDLA | ||||||
Cross-link | 91↔218 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) | ||||
Sequence: WHSAGTYRTADGRGGAGEGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGRAISWADLLILTGNVALESMGFKTFGFAGGRADTWEPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMGLIY | ||||||
Cross-link | 218↔244 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) | ||||
Sequence: YVNPEGPDGNPDPVAAARDIRDTFARM |
Post-translational modification
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Interaction
Subunit
Homodimer or homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length728
- Mass (Da)79,446
- Last updated2005-11-08 v1
- ChecksumFB6EC6E5261F6740
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000124 EMBL· GenBank· DDBJ | ABA50840.1 EMBL· GenBank· DDBJ | Genomic DNA |