ID A0A1S4B7N5_TOBAC Unreviewed; 591 AA.
AC A0A1S4B7N5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=catechol oxidase {ECO:0000256|ARBA:ARBA00012298};
DE EC=1.10.3.1 {ECO:0000256|ARBA:ARBA00012298};
GN Name=LOC107805360 {ECO:0000313|RefSeq:XP_016484879.1};
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_016484879.1};
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_016484879.1}
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}.
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 RefSeq; XP_016484879.1; XM_016629393.1.
DR AlphaFoldDB; A0A1S4B7N5; -.
DR SMR; A0A1S4B7N5; -.
DR STRING; 4097.A0A1S4B7N5; -.
DR PaxDb; 4097-A0A1S4B7N5; -.
DR OMA; KAHINET; -.
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:SF92; POLYPHENOL OXIDASE F, 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 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|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 198..215
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 360..371
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT BINDING 180
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 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 329
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 333
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 367
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 99..115
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 114..181
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 184..198
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 591 AA; 66903 MW; 03DEA05CF437DE08 CRC64;
MASSSSTLPL CANKTPSSSF TNTNTNSSFF AKPSQLFLHG KRNQNFKFSC NANSGEHDKN
LDAVDRRNVL LGLGGLYGAA NLAPLATAAP IPPPDLKSCS KAHINDKEEV SYSCCPPIPS
DMDSVPYYKF PSMPKLRIRP AAHAADEEYI AKYQLATSRM RELDKDPFDP LGFKQQANIH
CAYCNGAYKI GGKELQVHFS WLFFPFHRWY LYFYERILGS LINDPTFGLP YWNWDHPKGM
RIPPMFDREG SSLYDARRNQ SHRNGTIIDL GFFGTEVQTT QLQQMTNNLT IMYRQMITNA
PCPLLFFGQP YPLGTDPSPG MGTIENIPHT PVHIWVGSRP DENNVKHGED MGNFYSAGLD
PLFYSHHANV DRMWSEWKAL GGKRRDLTHK DWLNSEFFFY DENRNPFRVK VRDCLDSKKM
GFDYAPMPTP WRNFKPIRKS NAGKVNLSSV PPASKVFPLS KLDRAISFSI DRPSSSRTQQ
EKNEQEEMLT FNNIKYDDSK YIRFDVFLNV DKTVNADELD KAEYAGSYTS LPHVHGDNVS
HVTSVTFQLA ITELLEDIGL EDEDTIAVTV VPKTGGEEIS IEGVEIKLVD C
//
