| IED ID | IndEnz0015000006 |
| Enzyme Type ID | laccase000006 |
| Protein Name |
Laccase-15 EC 1.10.3.2 Benzenediol:oxygen oxidoreductase 15 Diphenol oxidase 15 Protein TRANSPARENT TESTA 10 Urishiol oxidase 15 |
| Gene Name | TT10 LAC15 At5g48100 MDN11.18 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MSHSFFNLFLISLFLYNNCIAHHYTFTVREVPYTKLCSTKAILTVNSQFPGPIIKVHKGDTIYVNVQNRASENITMHWHGVEQPRNPWSDGPEYITQCPIRPGSDFLYKVIFSIEDTTVWWHAHSSWTRATVHGLIFVYPRPPQILPFPKADHEVPIILGEWWKRDVREVVEEFVRTGGAPNVSDALTINGHPGFLYPCSKSDTFHLTVEKGKTYRIRMVNAAMNLPLFFAIANHSLTVVSADGHYIKPIKATYITISPGETLDMLLHADQDPERTYYMAARAYQSGNIDFNNSTTIGILSYTSSCKAKTSSFSGYYPTLPFYNDTSAAFGFFTKIKCLFSGQVPVQISRRIITTVSINLRMCPQNSCEGPNGSRLAASMNNISFVTPSHVDILKAYYYHIKGVYGTRFPEFPPLIFNFTAENQPLFLETPRLATEVKVIEFGQVVELVIQGTSLVGGGLDHPMHLHGFSFYVVGVGFGNYNISEEDPSSRYNLYDPPYKNTMTVPRNGWIAIRFVADNPGVWFMHCHLDRHQTWGMNVVFIVKNGREPNQQILPPPDDLPPCYE |
| Enzyme Length | 565 |
| Uniprot Accession Number | Q84J37 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| 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; |
| DNA Binding | |
| EC Number | 1.10.3.2 |
| Enzyme Function | FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity). Involved in lignin synthesis in seed coats, in seed coat permeability, in seed germination, and in root elongation. Required for the seed coat (testa) brown pigmentation by mediating the polymerization of proanthocyanidin (tannin) from its monomer precursor epicatechin. Slightly promotes seed dormancy. {ECO:0000250, ECO:0000269|PubMed:10677433, ECO:0000269|PubMed:16243908, ECO:0000269|PubMed:16779554, ECO:0000269|PubMed:16804053, ECO:0000269|Ref.4}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Erroneous gene model prediction (1); Glycosylation (9); Metal binding (12); Mutagenesis (2); Signal peptide (1) |
| Keywords | Apoplast;Copper;Glycoprotein;Lignin degradation;Metal-binding;Oxidoreductase;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10504561; 11283341; 17893725; 18408011; 19129166; 21063888; 21447792; 23592226; 23613820; 23771594; 24532452; 26720211; 8528278; 9914531; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,994 |
| Kinetics | |
| Metal Binding | METAL 77; /note=Copper 1; type 2; /evidence=ECO:0000250; METAL 79; /note=Copper 2; type 3; /evidence=ECO:0000250; METAL 122; /note=Copper 2; type 3; /evidence=ECO:0000250; METAL 124; /note=Copper 3; type 3; /evidence=ECO:0000250; METAL 462; /note=Copper 4; type 1; /evidence=ECO:0000250; METAL 465; /note=Copper 1; type 2; /evidence=ECO:0000250; METAL 467; /note=Copper 3; type 3; /evidence=ECO:0000250; METAL 526; /note=Copper 3; type 3; /evidence=ECO:0000250; METAL 527; /note=Copper 4; type 1; /evidence=ECO:0000250; METAL 528; /note=Copper 2; type 3; /evidence=ECO:0000250; METAL 532; /note=Copper 4; type 1; /evidence=ECO:0000250; METAL 537; /note=Copper 4; type 1; /evidence=ECO:0000250 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |