ID A0T1D6_WHEAT Unreviewed; 577 AA.
AC A0T1D6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Polyphenol oxidase {ECO:0000313|EMBL:ABK62804.1};
GN Name=Ppo {ECO:0000313|EMBL:ABK62804.1};
GN ORFNames=CAMPLR22A2D_LOCUS4671 {ECO:0000313|EMBL:SPT20044.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EMBL:ABK62804.1};
RN [1] {ECO:0000313|EMBL:ABK62804.1}
RP NUCLEOTIDE SEQUENCE.
RA He X., He Z., Zhang L., Sun D., Xia X.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABK62804.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17426955; DOI=10.1007/s00122-007-0539-8;
RA He X.Y., He Z.H., Zhang L.P., Sun D.J., Morris C.F., Fuerst E.P., Xia X.C.;
RT "Allelic variation of polyphenol oxidase (PPO) genes located on chromosomes
RT 2A and 2D and development of functional markers for the PPO genes in common
RT wheat.";
RL Theor. Appl. Genet. 115:47-58(2007).
RN [3] {ECO:0000313|EMBL:SPT20044.1, ECO:0000313|Proteomes:UP000280104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Thind KAUR A.;
RL Submitted (MAY-2018) 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; EF070150; ABK62804.1; -; Genomic_DNA.
DR EMBL; LS480641; SPT20044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0T1D6; -.
DR SMR; A0T1D6; -.
DR Gramene; TraesCAD_scaffold_005671_01G000100.1; TraesCAD_scaffold_005671_01G000100.1; TraesCAD_scaffold_005671_01G000100.
DR Gramene; TraesCLE_scaffold_002903_01G000100.1; TraesCLE_scaffold_002903_01G000100.1; TraesCLE_scaffold_002903_01G000100.
DR Gramene; TraesPAR_scaffold_003597_01G000100.1; TraesPAR_scaffold_003597_01G000100.1; TraesPAR_scaffold_003597_01G000100.
DR Gramene; TraesROB_scaffold_008753_01G000100.1; TraesROB_scaffold_008753_01G000100.1; TraesROB_scaffold_008753_01G000100.
DR Proteomes; UP000280104; Chromosome ii.
DR ExpressionAtlas; A0T1D6; baseline and differential.
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:SF134; TYROSINASE COPPER-BINDING DOMAIN-CONTAINING 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 189..206
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 347..358
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT BINDING 168
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 189
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 320
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 324
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 354
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 92..107
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 106..169
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 172..189
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 577 AA; 63955 MW; D3A4C65023C3921F CRC64;
MESSRMPLSA TSRMSCSLQT LARRNLLRAL HRRKDARQPR RLSISCEATG GRRVDRREVL
LGLGGAAAAG LATDQGRGAI AAPIQAPDLS NCQTPALPNT PPDTNCCPTP GTGITDFELP
PASSPLRVRP AAHLVDAEYL AKYERAVALM KQLPADDPRS FEQQWHVHCA YCDAAYDQVG
FPDLELQIHN CWLFFPWHRF YLYFHERILG KLIGDDTFAL PFWNWDAPAG MKLPVIYANR
SSPLYDERRD PAHQPPVLVD LDYSGTDANI PRDQQIDENL KIMYRQMISN AKKTLLFLGQ
PYRAGDQPDP GAGSVENVPH GPVHNWTGDP RQPNGEDMGN FYSAARDPIF FAHHGNIDRL
WHVWRGLRPS NTDFTDPDWL DAGFLFYDEE ARPVRVRVRD CLDPAALRYT YQDVGLPWLN
ARPAKASGGT PAPATTGTLP ATLDRTIRVT VTRPRVSRSR REKDEEEEVL VVEGIEIADH
FNKFVKFDVL VNEPEGGVGG TPATATGYCA GSFAHTPHMV RPEEMRKGPV KTVARFGVCD
LMDDIGADGD QTVVVSLVPR CGGDLVTIGG VSISYVK
//
