Detail Information for IndEnz0018001085
IED ID IndEnz0018001085
Enzyme Type ID peroxidase001085
Protein Name Catalase-peroxidase
CP
EC 1.11.1.21
Peroxidase/catalase
Gene Name katG BURPS1710b_3366
Organism Burkholderia pseudomallei (strain 1710b)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia pseudomallei group Burkholderia pseudomallei (Pseudomonas pseudomallei) Burkholderia pseudomallei (strain 1710b)
Enzyme Sequence MSNEAKCPFHQAAGNGTSNRDWWPNQLDLSILHRHSSLSDPMGKDFNYAQAFEKLDLAAVKRDLHALMTTSQDWWPADFGHYGGLFIRMAWHSAGTYRTADGRGGAGEGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGRAISWADLLILTGNVALESMGFKTFGFAGGRADTWEPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMGLIYVNPEGPDGNPDPVAAARDIRDTFARMAMNDEETVALIAGGHTFGKTHGAGPASNVGAEPEAAGIEAQGLGWKSAYRTGKGADAITSGLEVTWTTTPTQWSHNFFENLFGYEWELTKSPAGAHQWVAKGADAVIPDAFDPSKKHRPTMLTTDLSLRFDPAYEKISRRFHENPEQFADAFARAWFKLTHRDMGPRARYLGPEVPAEVLLWQDPIPAVDHPLIDAADAAELKAKVLASGLTVSQLVSTAWAAASTFRGSDKRGGANGARIRLAPQKDWEANQPEQLAAVLETLEAIRTAFNGAQRGGKQVSLADLIVLAGCAGVEQAAKNAGHAVTVPFAPGRADASQEQTDVESMAVLEPVADGFRNYLKGKYRVPAEVLLVDKAQLLTLSAPEMTVLLGGLRVLGANVGQSRHGVFTAREQALTNDFFVNLLDMGTEWKPTAADADVFEGRDRATGELKWTGTRVDLVFGSHSQLRALAEVYGSADAQEKFVRDFVAVWNKVMNLDRFDLA
Enzyme Length 728
Uniprot Accession Number Q3JNW6
Absorption
Active Site ACT_SITE 92; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01961
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
DNA Binding
EC Number 1.11.1.21
Enzyme Function FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (17); Chain (1); Cross-link (2); Helix (47); Metal binding (1); Site (1); Turn (7)
Keywords 3D-structure;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}.
Signal Peptide
Structure 3D X-ray crystallography (49)
Cross Reference PDB 5KQ0; 5KQ2; 5KQ3; 5KQ6; 5KQH; 5KQI; 5KQK; 5KQN; 5KQQ; 5KSF; 5KSG; 5KSK; 5KSN; 5KT8; 5KT9; 5L02; 5L05; 5SW4; 5SW5; 5SW6; 5SX0; 5SX1; 5SX2; 5SX3; 5SX6; 5SX7; 5SXQ; 5SXR; 5SXS; 5SXT; 5SXW; 5SXX; 5SYH; 5SYI; 5SYJ; 5SYK; 5SYL; 5SYU; 5SYV; 5SYW; 5SYY; 5TXQ; 5V4O; 5V53; 6B9B; 6CAW; 6CC6; 6CDQ; 6CEK;
Mapped Pubmed ID 12628252; 15567407; 16211084; 16618106; 17063492; 20554537; 24568093; 24785434; 28409923; 29732452;
Motif
Gene Encoded By
Mass 79,446
Kinetics
Metal Binding METAL 259; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_01961
Rhea ID RHEA:30275; RHEA:20309
Cross Reference Brenda 1.11.1.21;