| IED ID | IndEnz0010001510 |
| Enzyme Type ID | esterase001510 |
| Protein Name |
Tannase EC 3.1.1.20 Cleaved into: Tannase 33 kDa subunit; Tannase 30 kDa subunit |
| Gene Name | AO090103000074 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MRQHSRMAVAALAAGANAASFTDVCTVSNVKAALPANGTLLGISMLPSAVTANPLYNQSAGMGSTTTYDYCNVTVAYTHTGKGDKVVIKYAFPKPSDYENRFYVAGGGGFSLSSDATGGLAYGAVGGATDAGYDAFDNSYDEVVLYGNGTINWDATYMFAYQALGEMTRIGKYITKGFYGQSSDSKVYTYYEGCSDGGREGMSQVQRWGEEYDGAITGAPAFRFAQQQVHHVFSSEVEQTLDYYPPPCELKKIVNATIAACDPLDGRTDGVVSRTDLCKLNFNLTSIIGEPYYCAAGTSTSLGFGFSNGKRSNVKRQAEGSTTSYQPAQNGTVTARGVAVAQAIYDGLHNSKGERAYLSWQIASELSDAETEYNSDTGKWELNIPSTGGEYVTKFIQLLNLDNLSDLNNVTYDTLVDWMNTGMVRYMDSLQTTLPDLTPFQSSGGKLLHYHGESDPSIPAASSVHYWQAVRSVMYGDKTEEEALEALEDWYQFYLIPGAAHCGTNSLQPGPYPENNMEIMIDWVENGNKPSRLNATVSSGTYAGETQMLCQWPKRPLWRGNSSFDCVNDEKSIDSWTYEFPAFKVPVY |
| Enzyme Length | 588 |
| Uniprot Accession Number | P78581 |
| Absorption | |
| Active Site | ACT_SITE 195; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 455; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89; ACT_SITE 501; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=digallate + H2O = 2 3,4,5-trihydroxybenzoate + H(+); Xref=Rhea:RHEA:16365, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16918, ChEBI:CHEBI:17866; EC=3.1.1.20; |
| DNA Binding | |
| EC Number | 3.1.1.20 |
| Enzyme Function | FUNCTION: Hydrolyzes ester bonds of tannic acid to produce gallic acid and glucose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (3); Metal binding (4); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 317; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:8917102 |
| Post Translational Modification | PTM: The protein is glycosylated to a carbohydrate content of 22.7%.; PTM: The N-terminus of the 30 kDa subunit is blocked. {ECO:0000269|PubMed:8917102}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:8917102 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,095 |
| Kinetics | |
| Metal Binding | METAL 262; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 265; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 269; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q2UP89; METAL 271; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q2UP89 |
| Rhea ID | RHEA:16365 |
| Cross Reference Brenda | 3.1.1.20; |