IED ID | IndEnz0018001024 |
Enzyme Type ID | peroxidase001024 |
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; |