ID A5X3N0_ORYRU Unreviewed; 576 AA.
AC A5X3N0;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:ABG23078.1};
GN Name=PPO {ECO:0000313|EMBL:ABG23078.1};
GN Synonyms=Ph {ECO:0000313|EMBL:QTO32240.1};
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:ABG23078.1};
RN [1] {ECO:0000313|EMBL:ABG23078.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G25 {ECO:0000313|EMBL:ABG23078.1}, and G40
RC {ECO:0000313|EMBL:ABG23080.1};
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).
RN [2] {ECO:0000313|EMBL:QTO32240.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ph_NSFTV490 {ECO:0000313|EMBL:QTO32242.1}, and Ph_NSFTV766
RC {ECO:0000313|EMBL:QTO32240.1};
RX PubMed=33281840;
RA Singh N., Wang D.R., Ali L., Kim H., Akther K.M., Harrington S.E.,
RA Kang J.W., Shakiba E., Shi Y., DeClerck G., Meadows B., Govindaraj V.,
RA Ahn S.N., Eizenga G.C., McCouch S.R.;
RT "A Coordinated Suite of Wild-Introgression Lines in Indica and Japonica
RT Elite Backgrounds.";
RL Front. Plant Sci. 11:0-0(0).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ532411; ABG23078.1; -; Genomic_DNA.
DR EMBL; DQ532413; ABG23080.1; -; Genomic_DNA.
DR EMBL; MW310677; QTO32240.1; -; Genomic_DNA.
DR EMBL; MW310679; QTO32242.1; -; Genomic_DNA.
DR AlphaFoldDB; A5X3N0; -.
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 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 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 576 AA; 63288 MW; 01FE70B1E86E2188 CRC64;
MESINVAPGT TATPRMAPPP 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
//
