ID P93622_VITVI Unreviewed; 607 AA.
AC P93622;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:AAB41022.1};
DE EC=1.10.3.1 {ECO:0000313|EMBL:AAB41022.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:AAB41022.1};
RN [1] {ECO:0000313|EMBL:AAB41022.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:AAB41022.1};
RA Virador V.M., Gepts P., Whitaker J.R.;
RT "Molecular cloning and c-DNA sequence of Grenache (Vitis vinifera) leaf
RT polyphenol oxidase.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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; U83274; AAB41022.1; -; mRNA.
DR RefSeq; NP_001268045.1; NM_001281116.1.
DR AlphaFoldDB; P93622; -.
DR SMR; P93622; -.
DR GeneID; 100233086; -.
DR KEGG; vvi:100233086; -.
DR OrthoDB; 1075546at2759; -.
DR BRENDA; 1.10.3.1; 6671.
DR ExpressionAtlas; P93622; baseline and differential.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-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; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
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; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
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 ECO:0000313|EMBL:AAB41022.1};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 211..228
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 368..379
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 46..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 220
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 342
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 346
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 375
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 114..129
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 128..191
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 194..211
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 607 AA; 67389 MW; 544C1D7D7D6FE164 CRC64;
MASLPWSLTT FTAIANTTNI SAFPPSPLFQ RASHVPVARN RSRRFAPSKV SCNSANGDPN
SDSTSDVRET SSGKLDRRNV LLGIGGLYGA AGGLGATKPL AFGAPIQAPD ISKCGTATVP
DGVTPTNCCP PVTTKIIDFQ LPSSGSPMRT RPAAHLVSKE YLAKYKKAIE LQKALPDDDP
RSFKQQANVH CTYCQGAYDQ VGYTDLELQV HASWLFLPFH RYYLYFNERI LAKLIDDPTI
ALAYWAWDNP DGMYMPTIYA SSPSSLYDEK RNAKHLPPTV IDLDYDGTEP TIPDDELKTD
NLAIMYKQIV SGATTPKLFL GYPYRAGDAI DPGAGTLEHV PHNIVHKWTG LADKPSEDMG
NFYTAGRDPI FFGHHANVDR MWNIWKTIGG KNRKDFTDTD WLDATFVFYD ENKQLVKVKV
SDCVDTSKLR YQYQDIPIPW LPKKTKAKAK TTTKSSKSGV AKAAELPKTT ISSIGDFPKA
LNSVIRVEVP RPKKSRSKKE KEDEEEVLLI KGIELDRENF VKFDVYINDE DYSVSRPKNS
EFAGSFVNVP HKHMKEMKTK TNLRFAINEL LEDLGAEDDE SVIVTIVPRA GGDDVTIGGI
EIEFVSD
//
