ID A0A4V3WJJ7_CAMSI Unreviewed; 263 AA.
AC A0A4V3WJJ7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN ORFNames=TEA_016367 {ECO:0000313|EMBL:THF97156.1};
OS Camellia sinensis var. sinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=542762 {ECO:0000313|EMBL:THF97156.1, ECO:0000313|Proteomes:UP000306102};
RN [1] {ECO:0000313|EMBL:THF97156.1, ECO:0000313|Proteomes:UP000306102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shuchazao {ECO:0000313|Proteomes:UP000306102};
RC TISSUE=Leaf {ECO:0000313|EMBL:THF97156.1};
RX PubMed=29678829; DOI=.1073/pnas.1719622115;
RA Wei C., Yang H., Wang S., Zhao J., Liu C., Gao L., Xia E., Lu Y., Tai Y.,
RA She G., Sun J., Cao H., Tong W., Gao Q., Li Y., Deng W., Jiang X., Wang W.,
RA Chen Q., Zhang S., Li H., Wu J., Wang P., Li P., Shi C., Zheng F., Jian J.,
RA Huang B., Shan D., Shi M., Fang C., Yue Y., Li F., Li D., Wei S., Han B.,
RA Jiang C., Yin Y., Xia T., Zhang Z., Bennetzen J.L., Zhao S., Wan X.;
RT "Draft genome sequence of Camellia sinensis var. sinensis provides insights
RT into the evolution of the tea genome and tea quality.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E4151-E4158(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000189};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR600823-3};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THF97156.1}.
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DR EMBL; SDRB02012621; THF97156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3WJJ7; -.
DR STRING; 542762.A0A4V3WJJ7; -.
DR Proteomes; UP000306102; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235:SF399; PEROXIDASE; 1.
DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR600823-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR600823-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000306102};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..263
FT /note="peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020937515"
FT DOMAIN 59..263
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 130
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT DISULFID 137..169
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 263 AA; 28404 MW; 5CF66768DE2FE581 CRC64;
MSSKKLTCVC IAFFLVLCAS VRLEAQLQVG FYTSSCAIAE FVVKDEVRKA YMSDMGLAAG
LVRMHFHDCF VRAGGLGYDV PAGRRDGRVS LASEANTNLP SPASNVNQLT QIFGNKGLTQ
EEMVTLSGAH TIGRAHCTSF SPRLYNFNTT TNQDPTLDSQ YASQLKQKCP QGSTNTNLVV
PMDPSSPNVM DVGYYNDILA NRGLFTSDQT LLTNSATANQ VNQNAMNTFV WGSKFAAAMV
KMGQIGVLTG GAGEVRLNCR KIN
//
