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
//