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Database: UniProt
Entry: M7YQV3_TRIUA
LinkDB: M7YQV3_TRIUA
Original site: M7YQV3_TRIUA 
ID   M7YQV3_TRIUA            Unreviewed;       566 AA.
AC   M7YQV3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Polyphenol oxidase, chloroplastic {ECO:0000313|EMBL:EMS49817.1};
GN   ORFNames=TRIUR3_06458 {ECO:0000313|EMBL:EMS49817.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS49817.1};
RN   [1] {ECO:0000313|EMBL:EMS49817.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23535596; DOI=10.1038/nature11997;
RA   Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA   Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA   Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA   Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA   Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA   Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA   Wang D., Zhang A., Wang J.;
RT   "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL   Nature 496:87-90(2013).
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; KD238818; EMS49817.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7YQV3; -.
DR   STRING; 4572.M7YQV3; -.
DR   eggNOG; ENOG502QVBP; Eukaryota.
DR   OMA; AEHMAKY; -.
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:SF129; TYROSINASE COPPER-BINDING DOMAIN-CONTAINING 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; 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   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          333..344
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   BINDING         155
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         176
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         184
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         306
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         310
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
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   DISULFID        77..93
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   DISULFID        92..156
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   CROSSLNK        159..176
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ   SEQUENCE   566 AA;  64409 MW;  8E23EEFE6C2B55A7 CRC64;
     MANGHRAPLA ACVFLICASA AATVIVVYTA FLSAHHRLRP RPVHRLMRRR RRHRPTLRRQ
     RRQEEDRRSS VTSLHTCVKV TLPPHPIPPF YCCPPAPASE PIDFTLPDPA EPLRVRRPMH
     AVGAEHMAKY ERAIALMRAL PHSDPRSLYQ LANVHCAYCT GSYRQTGDPE LNMQIHFSWF
     FPFHRAYLYF FERIAARLLG EPGFALPFWG WDVPEGMRMP AEFANSSSPL HDPVRNPAHA
     PPTVVNLDFA RVENNLTDEQ QIQQNLRIMY KQMIGNAALP SLFHGQPFRA GQSDRPGPGT
     VEMTPHNTMH TWTGDLAFHN VEDMGTYYSA GRDPLFYPHH NNVDRQWEAW RDVGAARGYR
     GHVDFTDPDW LDSSFVFYDE EARLVRITVG DVLDIDKLRY RFDGVGMPWV DARPPPTPNV
     NRNKGSSSLK SVRFPLSLHA AVTVEVRRPR VLRSRREKAV REEVLVVEGI ETDGTEMVKF
     DVYVNAMEYE KVEPSGRELA GSYLCLSHPR MDGTGKATRI ETSMRVALNE LLEDLGADRD
     ESVTVTLVPR HGKVKIGGLK IVYMME
//
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