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Database: UniProt
Entry: Q6R3L2_WHEAT
LinkDB: Q6R3L2_WHEAT
Original site: Q6R3L2_WHEAT 
ID   Q6R3L2_WHEAT            Unreviewed;       542 AA.
AC   Q6R3L2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   19-MAR-2014, entry version 44.
DE   SubName: Full=Polyphenol oxidase;
DE   Flags: Fragment;
GN   Name=PPO;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   AGRICOLA=IND43859238;
RA   Anderson J.V., Fuerst E.P., Hurkman W.J., Vensel W.H., Morris C.F.;
RT   "Biochemical and genetic characterization of wheat (Triticum spp.)
RT   kernel polyphenol oxidases.";
RL   J. Cereal Sci. 44:353-367(2006).
CC   -!- COFACTOR: Binds 2 copper ions per subunit (By similarity).
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DR   EMBL; AY515506; AAS00454.1; -; mRNA.
DR   UniGene; Ta.69136; -.
DR   ProteinModelPortal; Q6R3L2; -.
DR   Gramene; Q6R3L2; -.
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; -; 1.
DR   InterPro; IPR016213; Polyphenol_oxidase.
DR   InterPro; IPR022740; Polyphenol_oxidase_C.
DR   InterPro; IPR022739; Polyphenol_oxidase_cen.
DR   InterPro; IPR002227; Tyrosinase.
DR   InterPro; IPR008922; Unchr_di-copper_centre.
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; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Metal-binding.
FT   METAL       133    133       Copper A (By similarity).
FT   METAL       154    154       Copper A (By similarity).
FT   METAL       163    163       Copper A (By similarity).
FT   METAL       285    285       Copper B (By similarity).
FT   METAL       289    289       Copper B (By similarity).
FT   METAL       319    319       Copper B (By similarity).
FT   DISULFID     57     72       By similarity.
FT   DISULFID     71    134       By similarity.
FT   CROSSLNK    137    154       2'-(S-cysteinyl)-histidine (Cys-His) (By
FT                                similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   542 AA;  59911 MW;  E4D8092608D0FD83 CRC64;
     IRHEGRISIS CEATGGGRVD RREVLLGLGG AAAAGLATDQ GRGAIAAPIQ APDLRNCQTP
     DLPNTPPDTN CCPTPGTGIT DFELPPASSP LRVRPAAHLV DAEYLAKYER AVALMKQLPA
     DDPRSFEQQW HVHCAYCDAA FDQVGFPDLE IQVHNCWLFF PWHRFYVYFH ERILGKLIGD
     DTFALPFWNW DAPAGMTLPA IYANRSSPLY DERRDPAHQP PVLTDLDSSG TDANIPRDQQ
     IDQNLKIMYR QMISDAKKTL LFLGQPYRAG DQPDPGAGSL ENVPHGTVHV WTGDPAQPNL
     EDMGNFFSAA RDPIFFAHHG NIDRLWHVWR RLRPSNTDFT DPDWLDAAFL FYDEEARPVR
     VRVRDCLDPA ALRYTYQDVG LPWLNARPAK ASGGTPAPAT TGTLPATLDR TIRVTVTRPR
     VSRSRREKEE EEEVLVVEGI EIADHFNKFV KFDVLVNEPE GGVGSTPATA TGYCAGSFAH
     TPHMVRPEEM RKGPVKTVAR FGVCDLMDDI GADDDQTVVV SLVPRCGGEL VTVGGVSISY
     LK
//
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