Q5YVJ4 · KATG_NOCFA
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids739 (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 | |
---|---|---|
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCatalase-peroxidase
- EC number
- Short namesCP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Nocardia
Accessions
- Primary accessionQ5YVJ4
Proteomes
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354851 | 1-739 | Catalase-peroxidase | |||
Sequence: MSVEHPPIGEANTEPAAGGCPVTGRLRHPLQGGGNHEWWPNQLNLKVLAKNPAEGNPLGDFDYKAAFNSLDLAAVKADIAEVLTTSQDWWPADFGNYGPLMIRMAWHSAGTYRSSDGRGGANTGQQRFAPLNSWPDNGNLDKARRLLWPVKKKYGQNISWADLMILAGNVALETMGFKTFGFAGGRVDVWEPEEDVYWGPEAEWLGDKRYSGERDLENPLAAVQMGLIYVNPEGPNGNPDPLAAAVDIKDTFGRMGMTVEETVALIAGGHTFGKTHGAGDAALVGAEPEAAPLEQMGLGWKSSHGTGKGADAITSGLEVVWTTKPTQWSNDFFEILFGYEWELTKSPAGANQWVAKDAQPIIPDPFDPAKKRLPTMLTTDLSLRVDPEMEVISRRFKDNPDEFADAFARAWFKLTHRDLGPVTRYLGPEVPSEVQLWQDPIPAVDHELVDAADIAALKEQILASELSISQLVKTAWAAASSFRGSDYRGGANGGRIRLQPQLGWEVNEPDELARVIAVLEGIQEQFNAAQTGNKKVSFADLVVLGGVAAVEQAARNAGVAVEVPFTPGRADTTQELTDPEGFAVLEPKADGFRNYLGKANPLPAEYLLVDKANLLTLTAPEMTVLVGGLRVLNANYQRSPLGVLTETPESLTNDFFVNLLDMGVVWEPSPADDGTYVGKDAATGAQKWTGSRVDLLFGSNSVLRSLAEVYATDDAKPKFVQDFVAAWNKVMNLDRFDLA | ||||||
Cross-link | 106↔229 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) | ||||
Sequence: WHSAGTYRSSDGRGGANTGQQRFAPLNSWPDNGNLDKARRLLWPVKKKYGQNISWADLMILAGNVALETMGFKTFGFAGGRVDVWEPEEDVYWGPEAEWLGDKRYSGERDLENPLAAVQMGLIY | ||||||
Cross-link | 229↔255 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-106) | ||||
Sequence: YVNPEGPNGNPDPLAAAVDIKDTFGRM |
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 | 1-33 | Disordered | ||||
Sequence: MSVEHPPIGEANTEPAAGGCPVTGRLRHPLQGG | ||||||
Region | 113-134 | Disordered | ||||
Sequence: RSSDGRGGANTGQQRFAPLNSW | ||||||
Compositional bias | 115-133 | Polar residues | ||||
Sequence: SDGRGGANTGQQRFAPLNS |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length739
- Mass (Da)80,210
- Last updated2004-11-23 v1
- Checksum51B7275E2C4651CB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 115-133 | Polar residues | ||||
Sequence: SDGRGGANTGQQRFAPLNS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP006618 EMBL· GenBank· DDBJ | BAD57797.1 EMBL· GenBank· DDBJ | Genomic DNA |