ID A0A1S3X216_TOBAC Unreviewed; 578 AA.
AC A0A1S3X216;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=catechol oxidase {ECO:0000256|ARBA:ARBA00012298};
DE EC=1.10.3.1 {ECO:0000256|ARBA:ARBA00012298};
GN Name=LOC107760231 {ECO:0000313|RefSeq:XP_016433738.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016433738.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016433738.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-
CC diquinones. {ECO:0000256|ARBA:ARBA00002400}.
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 Evidence={ECO:0000256|ARBA:ARBA00001628};
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004456}.
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR RefSeq; XP_016433738.1; XM_016578252.1.
DR AlphaFoldDB; A0A1S3X216; -.
DR SMR; A0A1S3X216; -.
DR STRING; 4097.A0A1S3X216; -.
DR PaxDb; 4097-A0A1S3X216; -.
DR GeneID; 107760231; -.
DR KEGG; nta:107760231; -.
DR OMA; HIRTNAC; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF109; CATECHOL OXIDASE; 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; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR000290-1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 346..357
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT BINDING 170
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 319
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 323
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 353
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 92..108
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 107..171
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 174..188
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 578 AA; 66372 MW; AE883D50228B770F CRC64;
MASSFVLQAP WAITTNLSCF PSFTKPSHVF PHKKPNNKFK VSCNQNNEAN NSQEKVERRN
LLLGLGGIYG AAHLLPYDAL ASPIPSPTLT QCGTAIIEGD KPVPYTCCPP IPEIKDVPYY
NPPPVSRFRV RPAAHTVDDE YIAKYNEAYS RMKALPTDDP RSFMQQANIH CAYCNGAYKV
GGKELQVHFS WLFFPFHRWY IYFYERILAS LIDDPTFALP YWNWDNPKGM HLPDMFDVEG
TSIYNERRNQ KHRNGFIMDL GYAGEDVVAN DLQKLVNNLT LMYRQMITNA PCPSLFFGKP
YRFGSEPSPG MGTIENVPHN SIHRWVGDPR QPNEEDMGNF YSSGKDPAFF SLHANVDRMW
TIWKTLGGKR KDISDPDYLD TEFFFYDEKA KPFRVRVRDC LDEKKLGYTF QPMDIPWKNF
KPQPRKNKKN VKIDPNSVPP ASQVFPIKKL DKTVTFSVAR PKRLRTKKEK EDEEELLTFK
NVELDVRKFV RFDVFLNEDN DVIANEIDRT EFVGSFANLP HIHDDPKKEK FPEFSLAINE
LLEDLKLEGD DLVVVTLVPK SGGENVSIEA VEIQLVPC
//
