ID B9RZ47_RICCO Unreviewed; 589 AA.
AC B9RZ47;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 03-APR-2013, entry version 24.
DE SubName: Full=Polyphenol oxidase, chloroplast, putative;
DE EC=1.10.3.1;
GN ORFNames=RCOM_0935110;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae;
OC Acalypheae; Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B.,
RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M.,
RA Ravel J., Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity).
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DR EMBL; EQ973834; EEF43227.1; -; Genomic_DNA.
DR RefSeq; XP_002519016.1; XM_002518970.1.
DR ProteinModelPortal; B9RZ47; -.
DR GeneID; 8278545; -.
DR KEGG; rcu:RCOM_0935110; -.
DR ProtClustDB; CLSN2718865; -.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:EC.
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; Di-copper_centre; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase.
FT METAL 167 167 Copper A (By similarity).
FT METAL 188 188 Copper A (By similarity).
FT METAL 197 197 Copper A (By similarity).
FT METAL 319 319 Copper B (By similarity).
FT METAL 323 323 Copper B (By similarity).
FT METAL 353 353 Copper B (By similarity).
FT DISULFID 91 106 By similarity.
FT DISULFID 105 168 By similarity.
FT CROSSLNK 171 188 2'-(S-cysteinyl)-histidine (Cys-His) (By
FT similarity).
SQ SEQUENCE 589 AA; 66208 MW; F49CF4CED6EA8926 CRC64;
MSSFTTSITI STSSFCPFLS KTSQLSIPKN RNCNYVNPHL ISCKATANDH DQNPTTRRDI
LIVLGGLYVA ITLGDPLAFA KPVSAPDLTK CGKADLPSSA KPTNCCPPPS TKILDFKLPS
SNSPLRIRPA AHVVDDAYLA KYSKAIELMK ALPDDDPRSF MQQANVHCAY CDGAYHQVGL
PDLDLQVHNS WLFFPFHRYF LYFHEKILGK LIDDPTFALP FWNWDSPAGM QLPAIYVDPK
SPLYDQFRNK NHQPPTLVDL DYNGSENPTS KQELLSSNLT IMYRQMVSNG KTARLFHGSA
YRAGDEADPG AGSIENIPHG PVHVWCGDNT QPNLEDMGNF YSAARDPIFF AHHSNVDRMW
TIWKTLGGNK RTEFTDPDWL DAEFIFYDEN ANPVRVKVRD CIDTKKLGYI YQDVDIPWLK
SRPKSRRLIK KVANKVFHHD GQAAHAAETL NLPPITAFPL VLDKVISTVA KRPKKSRSKK
EKEEEEEVLL IDAIEFERNA LVKFDVYVND EHDSTSARPD NSEFAGSFVN IPHKHKHGKK
MKTCLRLGLT DLLEDMGAED DDTVVVTLVP RYGKGLVKIG GIMIDYIQD
//