Detail Information for IndEnz0007000457
IED ID IndEnz0007000457
Enzyme Type ID catalase000457
Protein Name Dye-decolorizing peroxidase Tfu_3078
DyP
EC 1.11.1.19
Peroxidase Tfu_3078
Gene Name Tfu_3078
Organism Thermobifida fusca (strain YX)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida fusca (Thermomonospora fusca) Thermobifida fusca (strain YX)
Enzyme Sequence MTEPDTERKGSSRRGFLAGLGAAALTGAGIGMAAGEVLRPLLPDSDPAASPEAEQRLRMAAQRADATAAPQPGISGPAPAFVHVIALDLAEEARKNPDTARDSAAAALRSWTELAARLHEESPHDIAEGAASAGLLPASLMVTVGIGGSLLSAIDAEDRRPDALADLPEFSTDDLHPRWCGGDFMLQVGAEDPMVLTAAVEELVAAAADATAVRWSLRGFRRTAAAARDPDATPRNLMGQIDGTANPAQDHPLFDRTITARPADNPAHAWMDGGSYLVVRRIRMLLTEWRKLDVAARERVIGRRLDTGAPLGSRNETDPVVLSARDEEGEPLIPENAHVRLASPENNLGARMFRRGYSYDQGWRDDGVRDAGLLFMAWQGDPATGFIPVQRSLADQGDALNRYIRHEGSALFAVPAAREGRYLGQDLIEG
Enzyme Length 430
Uniprot Accession Number Q47KB1
Absorption
Active Site ACT_SITE 242; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:19967355
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278; EC=1.11.1.19;
DNA Binding
EC Number 1.11.1.19
Enzyme Function FUNCTION: Peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. Shows high reactivity towards anthraquinone dyes (e.g. Reactive Blue 19) and a modest activity towards standard peroxidase substrates (such as guaiacol and 2,6-dimethoxyphenol) and azo dyes (e.g. Reactive Blue 5). Is also able to oxidize aromatic sulfides enantioselectively, resulting in the corresponding (R)-sulfoxides, but with a poor efficiency. Does not display catalase activity. {ECO:0000269|PubMed:19967355}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 25 degrees Celsius. Thermostable. Retains 50% of its activity after heating 2 hours at 60 degrees Celsius, while no decrease in activity is observed within the same time at 30 or 40 degrees Celsius. {ECO:0000269|PubMed:19967355};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 with Reactive Blue 19 as substrate. {ECO:0000269|PubMed:19967355};
Pathway
nucleotide Binding
Features Active site (1); Beta strand (9); Chain (1); Helix (21); Metal binding (1); Mutagenesis (2); Region (1); Signal peptide (1); Turn (4)
Keywords 3D-structure;Heme;Iron;Metal-binding;Oxidoreductase;Peroxidase;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19967355}.
Modified Residue
Post Translational Modification PTM: Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Signal Peptide SIGNAL 1..39; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5FW4;
Mapped Pubmed ID 26901432;
Motif
Gene Encoded By
Mass 45,928
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29 uM for Reactive Blue 19 {ECO:0000269|PubMed:19967355}; KM=27 uM for H(2)O(2) {ECO:0000269|PubMed:19967355}; Note=kcat is 10 sec(-1) with Reactive Blue 19 as substrate.;
Metal Binding METAL 338; /note=Iron (heme proximal ligand); /evidence=ECO:0000305
Rhea ID RHEA:28086
Cross Reference Brenda 1.11.1.19;