| IED ID | IndEnz0016000199 |
| Enzyme Type ID | tyrosinase000199 |
| Protein Name |
Polyphenol oxidase A1, chloroplastic PPO EC 1.10.3.1 Catechol oxidase |
| Gene Name | |
| Organism | Vicia faba (Broad bean) (Faba vulgaris) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Fabeae Vicia Vicia faba (Broad bean) (Faba vulgaris) |
| Enzyme Sequence | MTSISALSFISTINVSSNSKISHSSVYPFLQKQHQSSKLRKPKRQVTCSSNNNQNNPKEEQELSNIVGHRRNVLIGLGGIYGTLATNPSALASPISPPDLSKCVPPSDLPSGTTPPNINCCPPYSTKITDFKFPSNQPLRVRQAAHLVDNEFLEKYKKATELMKALPSNDPRNFTQQANIHCAYCDGAYSQIGFPDLKLQVHGSWLFFPFHRWYLYFYERILGSLINDPTFALPFWNYDAPDGMQLPTIYADKASPLYDELRNASHQPPTLIDLNFCDIGSDIDRNELIKTNLSIMYRQVYSNGKTSRLFLGNPYRAGDAEPQGAGSIENVPHAPVHTWTGDNTQTNIEDMGIFYSAARDPIFYSHHSNVDRLWYIWKTLGGKKHDFTDKDWLESGFLFYDENKNLVRVNVKDSLDIDKLGYAYQDVPIPWEKAKPVPRRTKVQKLVEVEVNDGNLRKSPTIFLVRQQSPRKYVTFPLVLNNKVSAIVKRPKKLRSKKEKEEEEEVLVIEGIEFYMNIAIKFDVYINDEDDKVGAGNTEFAGSFVNIPHSAHGHKNKKIITSLRLGITDLLEDLHVEGDDNIVVTLVPKCGSGQVKINNVEIVFED |
| Enzyme Length | 606 |
| Uniprot Accession Number | Q06215 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O; Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1; |
| DNA Binding | |
| EC Number | 1.10.3.1 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Cross-link (1); Disulfide bond (2); Metal binding (6); Region (1); Transit peptide (1) |
| Keywords | Chloroplast;Copper;Direct protein sequencing;Disulfide bond;Metal-binding;Oxidoreductase;Plastid;Thioether bond;Thylakoid;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,541 |
| Kinetics | |
| Metal Binding | METAL 181; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 202; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 211; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 333; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 337; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 367; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:21632 |
| Cross Reference Brenda |