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 27-MAR-2024, entry version 87. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Di-copper center containing domain from catechol oxidase; 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 PANTHER; PTHR11474:SF87; POLYPHENOL OXIDASE CHLOROPLASTIC; 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 PRINTS; PR00092; TYROSINASE. DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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 //