ID W9RDC2_9ROSA Unreviewed; 601 AA.
AC W9RDC2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:EXB82817.1};
GN ORFNames=L484_012131 {ECO:0000313|EMBL:EXB82817.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB82817.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KE344870; EXB82817.1; -; Genomic_DNA.
DR RefSeq; XP_010100574.1; XM_010102272.1.
DR AlphaFoldDB; W9RDC2; -.
DR SMR; W9RDC2; -.
DR STRING; 981085.W9RDC2; -.
DR GeneID; 21395360; -.
DR KEGG; mnt:21395360; -.
DR eggNOG; ENOG502QVBP; Eukaryota.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000030645; Unassembled WGS sequence.
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:UP000030645};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 209..226
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 367..378
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
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 218
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 340
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
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 374
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 112..127
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 126..189
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 192..209
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 601 AA; 67184 MW; 909EAC88B04E4D44 CRC64;
MASLSTTSPP TTTTGIAPST TSLSPSLQKK CQISTISKRS NKHCLPRKLS CKANNNDHDL
SPTNDVASKT SNPKLDRRNV LLGLGSLGGL AGLRADPFAF AAPISAPDIS QCGAADFPSG
VDPVNCCPPV SAQIVDFKLP ASPGKLRVRP PAHAVDSAYT AKFKRAFELM KALPDSDPRS
FKQQASIHCA YCDGAYEQIG FPDLDIQVHN SWLFFPFHRW YLYFFERILG KLIDDPSFAM
PFWNWDAPAG MQIPAIYADR RSPLYDQFRN KSHQPPSLVD LDFNGRDESI SNQAQIQSNL
TIMYRQMVSN SRSARIFMGE SYRAGDETDP GPGSFENIPH GSVHTWTGDN TQPYGEDMGN
FYSAGRDPIF FAHHSNIDRM WNVWKTLGGK RQDFTDPDWL DASFLFYDEN SQLVRVKVRD
SLDSRKLGYT YQDIELPWLN TRPRPRRVVD KVKRAFARIG VARADEYPTA NFPLTLDKPV
KTLVSRPKKS RSKKEKDEAD EVLVIQGIEF DRNVPIKFDV FINDEDDALT GPDKSEFAGS
FVSVPHRHKS KTKMNTGLRL DITELLEDLD AEEDENVVVT LVPKVGIGHV SIGGLKIEFV
S
//
