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Database: UniProt
Entry: A5X3P0_ORYRU
LinkDB: A5X3P0_ORYRU
Original site: A5X3P0_ORYRU 
ID   A5X3P0_ORYRU            Unreviewed;       570 AA.
AC   A5X3P0;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:ABG23088.1};
GN   Name=PPO {ECO:0000313|EMBL:ABG23088.1};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EMBL:ABG23088.1};
RN   [1] {ECO:0000313|EMBL:ABG23088.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W0154d {ECO:0000313|EMBL:ABG23088.1}, and W1125
RC   {ECO:0000313|EMBL:ABG23094.1};
RX   PubMed=19033526; DOI=10.1105/tpc.108.060426;
RA   Yu Y., Tang T., Qian Q., Wang Y., Yan M., Zeng D., Han B., Wu C.I., Shi S.,
RA   Li J.;
RT   "Independent losses of function in a polyphenol oxidase in rice:
RT   differentiation in grain discoloration between subspecies and the role of
RT   positive selection under domestication.";
RL   Plant Cell 20:2946-2959(2008).
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; DQ532421; ABG23088.1; -; Genomic_DNA.
DR   EMBL; DQ532427; ABG23094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5X3P0; -.
DR   SMR; A5X3P0; -.
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:SF76; TYROSINASE; 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|ARBA:ARBA00023008, 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   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          192..209
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          350..361
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         171
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
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         201
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         323
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         327
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         357
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   DISULFID        92..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   DISULFID        107..172
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   CROSSLNK        175..192
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ   SEQUENCE   570 AA;  62681 MW;  977440BF78FB4854 CRC64;
     MESINVAPGT TATPRMAPPP PPPCITNLQS TLRYNNLLLH RKTKGWKPRN VSCRVDRRDV
     LLGISGAAAM VATQGGGGAL AAPIQAPDLG DCHQPVDVPA TAPAINCCPT YSAGTVAVDF
     APPPASSPLR VRPAAHLADR AYLAKYERAV SLMKKLPADD PRSFEQQWRV HCAYCDGAYD
     QVGFPGLEIQ IHSCWLFFPW HRMYLYFHER ILGKLIGDET FALPFWNWDA PDGMSFPAMY
     ANRWSPLYDP RRNQAHLPPF PLDLDYSGTD TNIPKDQLID QNLNIMYRQM ISGARKAELF
     MGQPYRAGDQ PEPGAGTVES VPHNPVHRWT GDPRQPNGED MGIFYSAARD PVFFAHHGNV
     DRMWHIRRGL LFPGDTDFTD PDWLDASFFF YDEEARLVRV RVRDTLDPSA LRFTYQDVGL
     PWLNAKPSTG AASTPAPAAG AFPATLDKTV RVAVTRPRAS RSREEKEEEE EVEIPDHSTY
     VKFDVFVNAP ESGDGAATCA ATCAGSVALA PHGIHREGQL SPRKTEARFG ICDLLDDIGA
     DGDKTIVVSI VPRCGCDSVT VAGVSIGYAK
//
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