A6VVN4 · KATG_MARMS
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids737 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Oceanospirillaceae > Marinomonas
Accessions
- Primary accessionA6VVN4
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354829 | 1-737 | Catalase-peroxidase | |||
Sequence: MSKENMSNEGKCPFNHGAAGTNQSSGRGTSNKDWWPNQLNLNILHQHSPKSNPMGEDFDYAKEFNSLDLEAIRQDLFALMTDSQDWWPADYGHYGPFFIRMAWHSAGTYRTADGRGGATSGTQRFAPLNSWPDNVNLDKARRLLWPIKQKYGRKISWADLMILAGNCALESMGFKTFGFAGGRVDVWQPEEDIYWGTEKTWLDDERYTGDRELENPLAAVQMGLIYVNPEGPEGKPDTLASARDIRDTFGRMAMNDEETVALIAGGHTFGKAHGAGDAAQVGADPEAAGIAEQGFGWSNSMGTGKGVDTISSGLEGAWTKSPIAWDNGYFENLFEYDWELTKSPAGAWQWTPKDGAAANSVPDAHDSSKRHAPIMFTSDLALRDDPIYAPISKRFYENPDQLADAFARAWFKLTHRDMGPVARYLGPLVPQEELVWQDPIPAVTYVTVNDQDILDLKAKIQASGLTVAQLVSTAWASASTYRGSDMRGGANGARIRLAPQKDWAVNQPEQLAKVLSVLESIQAEFNRQDSTKQVSLADLIVLGGSVGVEQAAKASGHSVTVPFTAGRADASQEQTDVESFAFLEPAADGFRNYLKGKYTVSAEEMLVDRAQLLTLSAPEMTALLGGLRVLNANVGQSQHGVFTDKPETLSNDFFVNLLDMGTKWFATSEEEEEFQGRDRTTGKIKWTATRADLVFGSNSQLRAIAEVYACSDSQERFVKDFIAAWTKVMELDRFDLA | ||||||
Cross-link | 103↔226 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252) | ||||
Sequence: WHSAGTYRTADGRGGATSGTQRFAPLNSWPDNVNLDKARRLLWPIKQKYGRKISWADLMILAGNCALESMGFKTFGFAGGRVDVWQPEEDIYWGTEKTWLDDERYTGDRELENPLAAVQMGLIY | ||||||
Cross-link | 226↔252 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-103) | ||||
Sequence: YVNPEGPEGKPDTLASARDIRDTFGRM |
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
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MSKENMSNEGKCPFNHGAAGTNQSSGRGTSNK | ||||||
Compositional bias | 17-32 | Polar residues | ||||
Sequence: GAAGTNQSSGRGTSNK |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length737
- Mass (Da)81,182
- Last updated2007-08-21 v1
- ChecksumC16560A20E762F15
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-32 | Polar residues | ||||
Sequence: GAAGTNQSSGRGTSNK |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000749 EMBL· GenBank· DDBJ | ABR70513.1 EMBL· GenBank· DDBJ | Genomic DNA |