PPO1_IPOBA
ID PPO1_IPOBA Reviewed; 496 AA.
AC Q9ZP19; Q84V53;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Polyphenol oxidase I, chloroplastic;
DE Short=PPO-I;
DE EC=1.10.3.1;
DE AltName: Full=Catechol oxidase I;
GN Name=co-1;
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].
RC TISSUE=Root;
RA Gerdemann C., Eicken C., Meyer H., Spener F., Krebs B.;
RT "Cloning and characterization of cDNA coding for Ipomoea batatas catechol
RT oxidase.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-345 IN COMPLEX WITH COPPER AND
RP N-PHENYLTHIOUREA, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=9846879; DOI=10.1038/4193;
RA Klabunde T., Eicken C., Sacchettini J.C., Krebs B.;
RT "Crystal structure of a plant catechol oxidase containing a dicopper
RT center.";
RL Nat. Struct. Biol. 5:1084-1090(1998).
CC -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC diquinones.
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:0000269|PubMed:9846879};
CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:9846879};
CC -!- ACTIVITY REGULATION: Inhibited by phenylthiourea.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9846879}.
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; AJ006097; CAA06855.1; -; mRNA.
DR EMBL; AJ309175; CAC83609.1; -; Genomic_DNA.
DR PDB; 1BT1; X-ray; 2.70 A; A/B=1-345.
DR PDB; 1BT2; X-ray; 2.70 A; A/B=1-345.
DR PDB; 1BT3; X-ray; 2.50 A; A=1-345.
DR PDB; 1BUG; X-ray; 2.70 A; A/B=1-345.
DR PDBsum; 1BT1; -.
DR PDBsum; 1BT2; -.
DR PDBsum; 1BT3; -.
DR PDBsum; 1BUG; -.
DR AlphaFoldDB; Q9ZP19; -.
DR SMR; Q9ZP19; -.
DR BRENDA; 1.10.3.1; 2773.
DR EvolutionaryTrace; Q9ZP19; -.
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:0005507; F:copper ion binding; IDA:UniProtKB.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
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 PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Plastid; Thioether bond; Thylakoid.
FT CHAIN 1..496
FT /note="Polyphenol oxidase I, chloroplastic"
FT /id="PRO_0000186741"
FT BINDING 88
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:9846879"
FT BINDING 109
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:9846879"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:9846879"
FT BINDING 240
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:9846879"
FT BINDING 244
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:9846879"
FT BINDING 274
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:9846879"
FT DISULFID 11..28
FT /evidence="ECO:0000269|PubMed:9846879"
FT DISULFID 27..89
FT /evidence="ECO:0000269|PubMed:9846879"
FT CROSSLNK 92..109
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000269|PubMed:9846879"
FT CONFLICT 40..42
FT /note="LPA -> IPV (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="K -> R (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> D (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="K -> R (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="A -> G (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="T -> A (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..403
FT /note="VGI -> EGV (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="F -> S (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="T -> A (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="V -> I (in Ref. 2; CAC83609)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1BT2"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 114..133
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:1BT3"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:1BT3"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:1BT3"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1BT3"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:1BT3"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1BT3"
SQ SEQUENCE 496 AA; 55011 MW; 806717DBF5B09705 CRC64;
APIQAPEISK CVVPPADLPP GAVVDNCCPP VASNIVDYKL PAVTTMKVRP AAHTMDKDAI
AKFAKAVELM KALPADDPRN FYQQALVHCA YCNGGYDQVN FPDQEIQVHN SWLFFPFHRW
YLYFYERILG KLIGDPSFGL PFWNWDNPGG MVLPDFLNDS TSSLYDSNRN QSHLPPVVVD
LGYNGADTDV TDQQRITDNL ALMYKQMVTN AGTAELFLGK AYRAGDAPSP GAGSIETSPH
IPIHRWVGDP RNTNNEDMGN FYSAGRDIAF YCHHSNVDRM WTIWQQLAGK PRKRDYTDSD
WLNATFLFYD ENGQAVKVRI GDSLDNQKMG YKYAKTPLPW LDSKPVPTKK KGGYASKSKA
PFVASVFPVT LDKVVQVKVA RPKKSRSAEE KEAEEEILLI VGIEVEIDKY AKFDVYLNDS
DDPSGGKDKA EYAGSFAHLP HKHKGMKKIR TTLSLGLNEP LEDLGAEDDD TILVTLAPKV
GGGVVSVDNV KVVYGS
