A4T0J1 · KATG_POLAQ
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids717 (go to sequence)
- Protein existenceInferred from homology
- 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 | |
---|---|---|
Molecular Function | catalase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway 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 > Polynucleobacter
Accessions
- Primary accessionA4T0J1
Proteomes
PTM/Processing
Features
Showing features for signal, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-12 | |||||
Sequence: MTSKGMCPVAHG | ||||||
Chain | PRO_0000354860 | 13-717 | Catalase-peroxidase | |||
Sequence: ANTEASETPMAWWPKALNLDILHQQDTKTNPMGSSFSYRDELKKLDVGALKKDMKDLLTNSQDWWPADWGHYGGLMIRMAWHSAGSYRIADGRGGAGTGNQRFAPINSWPDNANLDKARRLLWPIKKKYGNKISWADLMILAGTIAYESMGLKTFGFSFGREDIWHPEKDIYWGSEKEWLQKSGGKGSRYSGERELSNPLAAVMMGLIYVNPEGVDGKPDPLKTAQDMRVTFARMAMNDEETVALTAGGHTVGKAHGNGNAANLGPAPEAAPIDEQGLGWMNHKTRGIGRDAVTSGLEGAWTTHPTQWDNGYFNLLLNYDWKLTESPAGAHQYEPINIKEEDKPVDVEDASIRCMPMMTDADIALKMDPEYRKISERFSKDQAYFSETFAKAWFKLTHRDMGPKARYFGPDVPKEELIWQDPIPSGPKSYDIDAVKAKIKASGLSMSDMVTTAWDSARTFRGSDKRGGANGARIRLAPQKDWMGNEPERLARVLAVYEKIGKECGISIADTIILGGNIGIEQAAKAGGFDVKVPFTSGRGDAIQAMTDVESFEVLEPLADGFRNWLKESYVVTPEELLLDRTQLMGLTAQEMTVLIGGMRVLGTNYGGSKQGVFTEKEGVLSNDFFVNLTDMNYLWKPTGQNSYDIVERNTEKTKWTATRADLVFGSNSILRAYAEVYAQDDNKEKFVNDFIAAWTKVMNADLFN | ||||||
Cross-link | 93↔221 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-247) | ||||
Sequence: WHSAGSYRIADGRGGAGTGNQRFAPINSWPDNANLDKARRLLWPIKKKYGNKISWADLMILAGTIAYESMGLKTFGFSFGREDIWHPEKDIYWGSEKEWLQKSGGKGSRYSGERELSNPLAAVMMGLIY | ||||||
Cross-link | 221↔247 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-93) | ||||
Sequence: YVNPEGVDGKPDPLKTAQDMRVTFARM |
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
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length717
- Mass (Da)79,677
- Last updated2007-05-15 v1
- Checksum123162FCD1A2A41B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000655 EMBL· GenBank· DDBJ | ABP35255.1 EMBL· GenBank· DDBJ | Genomic DNA |