ID D1KEC6_ORYSA Unreviewed; 556 AA.
AC D1KEC6;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:ACS15326.1};
DE Flags: Fragment;
GN Name=PPO {ECO:0000313|EMBL:ACS15326.1};
OS Oryza sativa (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4530 {ECO:0000313|EMBL:ACS15326.1};
RN [1] {ECO:0000313|EMBL:ACS15326.1}
RP NUCLEOTIDE SEQUENCE.
RA Gross B.L., Skare K.J., Olsen K.M.;
RT "Novel Phr1 mutations and the evolution of phenol reaction variation in US
RT weedy rice (Oryza sativa).";
RL New Phytol. 184:842-850(2009).
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; GQ121712; ACS15326.1; -; Genomic_DNA.
DR AlphaFoldDB; D1KEC6; -.
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 Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 172..189
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 330..341
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 293..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 172
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 181
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 303
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 307
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 72..88
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 87..152
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 155..172
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACS15326.1"
SQ SEQUENCE 556 AA; 61267 MW; E188A4FC342B99BB CRC64;
PPPCITNLQS TLRYNNLLLH RKTKGWKPRN VSCRVDRRDV LLGISGAAAM VATQGGGGAL
AAPIQAPDLG DCHQPVDVPA TAPAINCCPT YSAGTVAVDF APPPASSPLR VRPAAHLADR
AYLAKYERAV SLMKKLPADD PRSFEQQWRV HCAYCDGAYD QVGFPGLEIQ IHSCWLFFPW
HRMYLYFHER ILGKLIGDET FALPFWNWDA PDGMSFPAIY ANRWSPLYDP RRNQAHLPPF
PLDLDYSGTD TNIPKDQLID QNLNIMYRQM ISGARKAELF MGQPYRAGDQ PEPGAGTVES
VPHNPVHRWT GDPRQPNGED MGIFYSAARD PVFFAHHGNV DRMWHIRRGL LFPGDTDFTD
PDWLDASFFF YDEEARLVRV RVRDTLDPSA LRFTYQDVGL PWLNAKPSTG AASTPAPAAG
AFPATLDKTV RVAVTRPRAS RSREEKEEEE EVLVIEGIEI PDHSTYVKFD VFVNAPESGD
GAATCAATCA GSVALAPHGI HREGQLSPRK TEARFGICDL LDDIGADGDK TIVVSIVPRC
GCDSVTVAGV SIGYAK
//
