A0QYP1 · KATG3_MYCS2
- ProteinCatalase-peroxidase 3
- GenekatG3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids744 (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
Names & Taxonomy
Protein names
- Recommended nameCatalase-peroxidase 3
- EC number
- Short namesCP 3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0QYP1
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354840 | 1-744 | Catalase-peroxidase 3 | |||
Sequence: MPESPDAYVNRTYDQTVAVRRSLKRRNSPAASEDGLGWPRRLNLRILAQPCRTSSPLGEDFDYAKEFLSLDLDELARDIDEVLTTSQDWWPADFGHYGPLVLRMAWHFAGTYRIGDGRGGAGAGMLRFAPLNSFPDNRNLDKARRLLWPVKKKYGRKISWSDLMIFAGNRALESMGCRTFGFAGGREDAWEADETYWGPESTWLADERHSGVRDLDQPLAASEMGLIYVDPQGPATLPDPLASARDIRETFRRMGMNDEETVALIAGGHTFGKSHGPTDPSRCLGPEPEGAPLEALGLGWVNSFGTGNGADTVTSGLDGIWTATPTKWDMSFLTTLFAYEWDVALSPAGMWQWVPRNGAGAGTVPDPYDPSRTHAPTMLTTDLALQEDPRYRVIALRFLENPDEFADTFARAWFKLTHIDMGPIQRYLGPLVPTERMIWQDPVPHVDHELADADDVAALKREILGSGLSVSQLVTTAWASASTFRNSDKRGGANGARIRLEPQRSWAVNEPEKLAIVLDRLERIRRRFNDSHRGGKQISAADLIMLGGCAAVEHAAAEAGHPIEVPCRLGRTDAPQEWTDIEWFSALEPTADAFRNYVGEGNRPPPEHLLVDRASQLTLTAPQMTVLLGGLRVLGANHGGSPLGVFTASPGALSNDFFVNLLDVNIEWTPRADTADWTAAYEGRDRRTGEVTWIASRVDLSFASDPVLRAISEVYASADAEEKFVRDFVSAWDKVMNLDLFDRT | ||||||
Cross-link | 106↔228 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-254) | ||||
Sequence: WHFAGTYRIGDGRGGAGAGMLRFAPLNSFPDNRNLDKARRLLWPVKKKYGRKISWSDLMIFAGNRALESMGCRTFGFAGGREDAWEADETYWGPESTWLADERHSGVRDLDQPLAASEMGLIY | ||||||
Cross-link | 228↔254 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-106) | ||||
Sequence: YVDPQGPATLPDPLASARDIRETFRRM |
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.
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length744
- Mass (Da)82,295
- Last updated2008-11-25 v2
- ChecksumA980D38FD8FCBF8E
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK74103.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP001663 EMBL· GenBank· DDBJ | AFP40103.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |