ID A0A4S4CZS6_CAMSI Unreviewed; 160 AA.
AC A0A4S4CZS6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN ORFNames=TEA_009895 {ECO:0000313|EMBL:THF95258.1};
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:THF95258.1, ECO:0000313|Proteomes:UP000306102};
RN [1] {ECO:0000313|EMBL:THF95258.1, 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:THF95258.1};
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|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the peroxidase family.
CC {ECO:0000256|RuleBase:RU004241}.
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:THF95258.1}.
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DR EMBL; SDRB02013304; THF95258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S4CZS6; -.
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:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.520.10; -; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
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; 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|PIRSR:PIRSR600823-5};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..160
FT /note="peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020667408"
FT DOMAIN 25..143
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 62
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 35..115
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 68..73
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 160 AA; 17670 MW; 8D9B0751EEE6F764 CRC64;
MVLPIVVLFI VLLSMSFQIL EAQAQLQVGF YRDKCIAAEL IVKEEVEKAF ARDKGIAPGL
IRMHFHDCFV RGCDCSIGID STPNNLSEKD GPPNGFTLRG FEVIENAKTR LEAQCKGVVS
CADILAFAAR DSAHGRPFLG CPSRKAGWED FACCKDHRHL
//
