ID M1BMR6_SOLTU Unreviewed; 598 AA.
AC M1BMR6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=catechol oxidase {ECO:0000256|ARBA:ARBA00012298};
DE EC=1.10.3.1 {ECO:0000256|ARBA:ARBA00012298};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400048684, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400048684}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400048684};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC diquinones. {ECO:0000256|ARBA:ARBA00002400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O;
CC Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001628};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR000290-1};
CC Note=Binds 2 copper ions per subunit. {ECO:0000256|PIRSR:PIRSR000290-
CC 1};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004456}.
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR AlphaFoldDB; M1BMR6; -.
DR SMR; M1BMR6; -.
DR STRING; 4113.M1BMR6; -.
DR PaxDb; 4113-PGSC0003DMT400048684; -.
DR EnsemblPlants; PGSC0003DMT400048684; PGSC0003DMT400048684; PGSC0003DMG400018916.
DR Gramene; PGSC0003DMT400048684; PGSC0003DMT400048684; PGSC0003DMG400018916.
DR eggNOG; ENOG502QVBP; Eukaryota.
DR HOGENOM; CLU_029668_1_0_1; -.
DR InParanoid; M1BMR6; -.
DR OMA; PAHEANE; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1BMR6; baseline and differential.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF112; POLYPHENOL OXIDASE D, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF12142; PPO1_DWL; 1.
DR Pfam; PF12143; PPO1_KFDV; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000290; PPO_plant; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR000290-1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000290-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000290-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 200..217
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 365..376
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 209
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 372
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 100..116
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 115..183
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 186..200
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 598 AA; 67144 MW; 3C3A001B7FC46141 CRC64;
MASLCNSSNT SLKTPFTSSS TSLSSTPKPS STFHPWKTYQ MFKVSCKVTN NNGDQNQNVE
TNSVDRRNVL LGLGGLYGVA NAIPLAASAS PTPPPDLSSC SKATINETTV VPYSCCAPKP
DDMEKVPYYK FPSMTKLRVR QPAHEANEEY IAKYNLAVSK MRDLDKTQPL NPIGFKQQAN
IHCAYCNGAY RIGGKELQVH NSWLFFPFHR WYLYFYERIV GKLIDDPTFA LPYWNWDHPK
GMRFPAMYDR EGTSLFDVTR DQSHRNGAVI DIGFFGNEVE TTQLQLMSNN LTLMYRQMVT
NAPCPRMFFG GPYDLGSNVE LPGTIENIPH GPVHIWSGTV RGSTLPNGAI SNGENMGHFY
SAGLDPVFFC HHSNVDRMWS EWKATGGKRT DITHKDWLNS EFFFYDENEN PYRVKVRDCL
DTKKMGYDYK PMATPWRNFK PLTKASAGKK VNTSSIPPVS QVFPLAKLDK AISFSINRPT
SSRTQQEKNA QEEMLTFSSI RYDNRGYIRF DVFLNVDNNV NANELDKAEF AGSYTSLPHV
HRAGETNHIA TVDFQLAITE LLEDIGLEDE ETIAVTLVPK RGGEGISIEG ATISLADC
//
