Q4F6N6 · KATG2_BURCJ
- ProteinCatalase-peroxidase 2
- GenekatG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids736 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Shows peroxidase specificity towards odianisidine, ABTS and pyrogallol, but methoxyphenol and 2-chloronaphthol are not peroxidized.
Catalytic activity
- AH2 + H2O2 = A + 2 H2O
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
pH Dependence
Optimum pH is 5.5 for the peroxidase reaction and 6.0 for the catalase reaction. Active from pH 5.5 to 8.5.
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 2
- EC number
- Short namesCP 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionQ4F6N6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354740 | 1-736 | Catalase-peroxidase 2 | |||
Sequence: MSNEGQCPFNHANGGGTTNRDWWPNELRLDLLSQHSSKTDPLDPGFNYAEAFNSLDLDALRKDLAALMTDSQDWWPADFGHYGPLFVRMAWHSAGTYRMGDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLLILTGDVALTTMGFKTFGYAGGREDTWEPDRDVYWGSETTWLGGDLRYDKGGACESQHGGNAGRNLENPLAAVQMGLIYVNPEGPDGNPDPVAAAYDIREVFGRMAMNDEETVALIAGGHAFGKTHGAGPADNVGLEPEAAGLEQQGLGWKNSFGTGKGADTITSGLEVTWSDTPTQWGMGFFKNLFGYEWELTKSPAGAHQWVAKNAEPTIPHAHDPSKKLLPTMLTTDLSLRFDPVYEKISRHFMDNPDVFADAFARAWFKLTHRDMGPRARYLGPDVPTEELIWQDPIPAVDHVLVDDTDVAPLKETILASGLSVAELVSTAWASASTFRGSDKRGGANGARIRLAPQKDWAVNEPARLAKVLKVLERIQGEFNSTQPGGKKISLADLIVLAGGAGIEQAAKRAGHDVVVPFAPGRMDASQEQTDAHSFAVLEPVADGFRNFVKGKFAVPAEALLIDKAQLLTLTAPQMTALVGGLRVLNVQTGDEKHGVFTDQPETLTVDFFRNLLDMATEWKPIAGEDTYEGRDRRTGELKWTGTRVDLVFGSNAVLRALSEVYASADGEAKFIRDFVAAWVKVMNLDRFDLA | ||||||
Cross-link | 91↔227 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-253) | ||||
Sequence: WHSAGTYRMGDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLLILTGDVALTTMGFKTFGYAGGREDTWEPDRDVYWGSETTWLGGDLRYDKGGACESQHGGNAGRNLENPLAAVQMGLIY | ||||||
Cross-link | 227↔253 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) | ||||
Sequence: YVNPEGPDGNPDPVAAAYDIREVFGRM |
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
- Length736
- Mass (Da)80,487
- Last updated2005-08-30 v1
- Checksum48CC314FEA9C30A3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ112341 EMBL· GenBank· DDBJ | AAZ14051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM747721 EMBL· GenBank· DDBJ | CAR55964.1 EMBL· GenBank· DDBJ | Genomic DNA |