ID A0A2I4DDQ0_JUGRE Unreviewed; 610 AA.
AC A0A2I4DDQ0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Polyphenol oxidase, chloroplastic-like {ECO:0000313|RefSeq:XP_018805282.2};
GN Name=LOC108979139 {ECO:0000313|RefSeq:XP_018805282.2};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018805282.2};
RN [1] {ECO:0000313|RefSeq:XP_018805282.2}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018805282.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR RefSeq; XP_018805282.2; XM_018949737.2.
DR AlphaFoldDB; A0A2I4DDQ0; -.
DR STRING; 51240.A0A2I4DDQ0; -.
DR KEGG; jre:108979139; -.
DR InParanoid; A0A2I4DDQ0; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000235220; Chromosome 3.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:InterPro.
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:SF138; OS04G0624500 PROTEIN; 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|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:UP000235220};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 213..230
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 371..382
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT BINDING 192
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 222
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 344
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 348
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 378
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 116..131
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 130..193
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 196..213
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 610 AA; 67722 MW; B1D9BF533FBCDC49 CRC64;
MASLSTQPPS TNINSTVAAA TTTIPNFSFY PTFPKKTQIS KFGKRNLRLA PGALSCRATN
NDQNFTSSSK DGQPSQGKFE RRDVLIGLGG LYGVAGLYND PFALAAPVSA PDITKCGKAD
FPAGAKPTNC CPPPSTKIID FKLPTKNSPL RVRPAAHLAD KEYIAKYNKA IELMKALPAD
DPRNFTQQAN VHCAYCDGAY EQVGFPNLDL QVHNSWLFFP FHRYYLYFYE KILGKLIGDP
TFALPFWNWD APAGMQLPAM YANPKSSLYD ALRNANHQPP TLMDLDYNGT DEETTSQDQL
SANLSIMYRQ MVSNGKNAKL FLGSAYRAGD EPDPGAGSIE NIPHGPVHIW TGDNTQPNLE
DMGNFYSAGR DPIFFAHHSN VDRMWSIWKT LGGKRTDFTE SDWLNAGFLF YDENGQAVRV
KVKDCLDTTK LGYVYQDVDL PWLKSKPTRK SKLKKVAKFF HLGHQGDVAI AAETSPSVNF
PIVLDKVIST VVARPRKSRS KKEKEDEEEV LVIGAIEFDR DAPVKFDVFI NDEDDSPTTR
PDKTEFAGSF VNVPHKHKHG KKMNTCLRLG ISDLLEDLDA EDDDTIVVTL VPRYGKGLAS
INGIKIELLD
//
