B4R8U3 · KATG_PHEZH
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids745 (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 | |
---|---|---|
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
Names & Taxonomy
Protein names
- Recommended nameCatalase-peroxidase
- EC number
- Short namesCP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Caulobacterales > Caulobacteraceae > Phenylobacterium
Accessions
- Primary accessionB4R8U3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354858 | 1-745 | Catalase-peroxidase | |||
Sequence: MDDASPLSNPAKEPAALRSLLGRTNRDWWPNQLSLDILHQHGRHGNPMGDDFDYAEAFKTLDYFAVKRDLHALMTDSQPWWPADYGHYGPFFIRMAWHSAGTYRTGDGRGGANSGNQRFAPLNSWPDNANLDKARRLLWPVKKKYGAKLSWADLMIMAGNVAFESMGAPVFGFGGGRADIFEPEKDVYWGTEEQWVGKGAKTRIVEGKAFEDPLAAVQMGLIYVNPEGPDGSPDPWASARDIRMTFARMGMNDEETLALTAGGHTFGKCHGAGDAAKIGAEPEGADIAQQGLGWTSSHESGMGDHTITSGLEGPWTPTPIKWDMSYFHMLLDYKYELVRSPAGAKQWQPVNPKPEDLAPGAHSPDRRVPTMMTTADLAFAMDPEYRKIAERFRDNPDQFADAFARAWFKLCHRDMGPKSRYLGPEVPAEDLIWQDPIPPVDHPLAEAADIASLKAKLLDSGLSVADLVRTAWASAATYRGSDHRGGANGARIRLAPQKDWEVNEPEKLARVLGVLEKVKADFDASAGGGKKISLADLIVLGGCAGIEKAARDAGHAIEVPFAPGRTDASPEQTDVESFEVLEPKADGFRNYLQVRFSVPTEELLIDRSQLLGLSAPEMTVLVGGLRVLGVNHGGSKNGVFTDRPGQLTNDFFVNLLDMGTAWKQVDDKADDLFVGTCRRTHEEKWTATRTDLVFGSNSQLRALSEVYASDDAGERFVKDFVRAWTKVMNADRFDLPRAQRLARAA | ||||||
Cross-link | 97↔223 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249) | ||||
Sequence: WHSAGTYRTGDGRGGANSGNQRFAPLNSWPDNANLDKARRLLWPVKKKYGAKLSWADLMIMAGNVAFESMGAPVFGFGGGRADIFEPEKDVYWGTEEQWVGKGAKTRIVEGKAFEDPLAAVQMGLIY | ||||||
Cross-link | 223↔249 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-97) | ||||
Sequence: YVNPEGPDGSPDPWASARDIRMTFARM |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 345-368 | Disordered | ||||
Sequence: KQWQPVNPKPEDLAPGAHSPDRRV |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length745
- Mass (Da)81,913
- Last updated2008-09-23 v1
- Checksum02BD6F645AFC27A4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000747 EMBL· GenBank· DDBJ | ACG79308.1 EMBL· GenBank· DDBJ | Genomic DNA |