PPO2_IPOBA
ID PPO2_IPOBA Reviewed; 588 AA.
AC Q9MB14; Q84V52; Q9ARD3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Polyphenol oxidase II, chloroplastic;
DE Short=PPO-II;
DE EC=1.10.3.1;
DE AltName: Full=Catechol oxidase II;
DE Flags: Precursor;
GN Name=co-2; Synonyms=ppo-I;
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hashimoto H., Nozue M., Tanaka I.;
RT "Ipomoea batatas polyphenol oxidase I mRNA.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 89-588.
RC STRAIN=cv. Bushbuck; TISSUE=Root;
RA Gerdemann C., Eicken C., Magrini A., Meier H.E., Spener F., Krebs B.;
RT "Sequence and structural implications of two isozymes of Ipomoea batatas
RT catechol oxidase differing in catalase activity.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-588.
RC STRAIN=cv. Bushbuck;
RA Greving J., Gerdemann C., Spener F., Krebs B.;
RT "Sequencing and cloning of genomic DNA encoding two isozymes of Ipomoea
RT batatas catechol oxidase.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC diquinones. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O;
CC Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; AB038994; BAA92317.1; -; mRNA.
DR EMBL; AJ245880; CAC29040.1; -; mRNA.
DR EMBL; AJ309176; CAC83610.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9MB14; -.
DR SMR; Q9MB14; -.
DR PRIDE; Q9MB14; -.
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; -; 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 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.
PE 2: Evidence at transcript level;
KW Chloroplast; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW Plastid; Thioether bond; Thylakoid; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 51..88
FT /note="Thylakoid"
FT /evidence="ECO:0000250"
FT CHAIN 89..588
FT /note="Polyphenol oxidase II, chloroplastic"
FT /id="PRO_0000035909"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 208
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 99..116
FT /evidence="ECO:0000250"
FT DISULFID 115..179
FT /evidence="ECO:0000250"
FT CROSSLNK 182..199
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CONFLICT 130
FT /note="K -> R (in Ref. 2; CAC29040)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> N (in Ref. 2; CAC29040)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="Q -> E (in Ref. 1; BAA92317)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="A -> P (in Ref. 3; CAC83610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 65651 MW; F0DF1A03FDC33AC2 CRC64;
MASFTTSPCT SAAPKTPKSL SSSATISSPL PKPSQIHIAT AKRTHHFKVS CNAPNGDSQP
KLDRRDVLLG LGGLAGAASL INNPLAFAEP IHAPEISKCV VPPKDLPPDA IVDNCCPPLA
TNVIPYKVPK TSPSAMKIRP AIHRMDKEYI AKFEKAIRLM KELPADDPRN FYQQALVHCA
YCNGGYVQTD YPDKEIQVHN SWLFFPFHRW YLYFYERILG KLIGDPTFGL PFWNWDTPAG
MLIPQYFRNQ NSPLYDENRN QSHLPLVMDL GYAGTDTDVT DQERISNNLA LMYKSMVTNA
GTAELFLGKP YKAGDDPVNK GGGSIENIPH TPVHRWVGDV KPRTQNGEDM GNFYSAGRDI
LFYCHHSNVD RMWTIWQQLG GKGRRRDFTD SDWLDATFIF YDENKQAVRV RVGDALDNQK
LGYKYEFTNL PWLNSKPLPT KKKTGLAARS KAPFVTDVFP LTLDKVVQVK VPRPKKSRSK
EEKEAEEEIL EIQGIEVAID QYAKFDVYLN DEDEPEAGKE KAEYAGSFAH LPHKHTGSKK
IRTSLSLGLN EPLEDLGAED DDAVLVTLAP KVGGGVVTVE NIKIVYGS
