| IED ID | IndEnz0015000031 |
| Enzyme Type ID | laccase000031 |
| Protein Name |
Laccase EC 1.10.3.2 BaCotA |
| Gene Name | cotA |
| Organism | Bacillus stratosphericus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus altitudinis complex Bacillus stratosphericus |
| Enzyme Sequence | MNLEKFVDELPIPEVAEPVKKNPRQTYYEIAMEEVFLKVHRDLPPTKLWTYNGSLPGPTIKANRNEKVKVKWMNKLPLKHFLPVDHTIHAGHHDEPEVKTVVHLHGGVTPASSDGYPEAWFSRDFEATGPFFEREVYEYPNHQQACTLWYHDHAMALTRLNVYAGLAGFYLISDAFEKSLELPKDEYDIPLMIMDRTFQEDGALFYPSRPNNTPEDSDLPDPSIVPFFCGETILVNGKVWPYLEVEPRKYRFRILNASNTRTYELHLDNDATILQIGSDGGFLPRPVHHQSFSIAPAERFDVIIDFSAYENKTIVLKNSAGCGQDVNPETDANIMQFKVTRPLKGRAAKTLRPIFKPLPPLRPSRADNERTLTLTGTQDKYGRPILLLDNQFWNDPVTENPRLGSVEVWNIVNPTRGTHPIHLHLVQFRVIDRRPFDTDIYQSTGEIVYTGPNEAPPLHEQGYKDTIQAHAGEVIRIIARFVPYSGRYVWHCHILEHEDYDMMRPMDIIQ |
| Enzyme Length | 510 |
| Uniprot Accession Number | A0A7T1FRB0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Resistant to alkali and organic solvents such as methanol, ethanol and acetone. Resistant to EDTA, which might be explained by the spatial protection of copper ions in the active sites. Inhibited by DMSO. Strongly inhibited by Fe(2+) and DTT. {ECO:0000269|PubMed:33676982}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:33676982}; |
| DNA Binding | |
| EC Number | 1.10.3.2 |
| Enzyme Function | FUNCTION: Multicopper oxidase that catalyzes the oxidation of a variety of substrates, including phenolic and non-phenolic compounds. Substrates include 2,6-dimethoxyphenol (2,6-DMP) and the non-phenolic compound 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Cannot use guaiacol and catechol. {ECO:0000269|PubMed:33676982}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:33676982}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:33676982}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (4); Metal binding (12); Site (2) |
| Keywords | Copper;Metal-binding;Oxidoreductase;Repeat |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,673 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.278 mM for ABTS {ECO:0000269|PubMed:33676982}; Vmax=555 umol/min/mg enzyme with ABTS as substrate {ECO:0000269|PubMed:33676982}; |
| Metal Binding | METAL 103; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:P07788; METAL 105; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:P07788; METAL 151; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:P07788; METAL 153; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:P07788; METAL 419; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P07788; METAL 422; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:P07788; METAL 424; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:P07788; METAL 491; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:P07788; METAL 492; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P07788; METAL 493; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:P07788; METAL 497; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P07788; METAL 502; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P07788 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |