ID A0A3B6TJ52_WHEAT Unreviewed; 330 AA.
AC A0A3B6TJ52;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060};
DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060};
GN ORFNames=CFC21_107284 {ECO:0000313|EMBL:KAF7106564.1}, CFC21_107291
GN {ECO:0000313|EMBL:KAF7106571.1}, CFC21_107292
GN {ECO:0000313|EMBL:KAF7106572.1}, CFC21_107293
GN {ECO:0000313|EMBL:KAF7106573.1}, CFC21_107294
GN {ECO:0000313|EMBL:KAF7106574.1}, CFC21_107295
GN {ECO:0000313|EMBL:KAF7106575.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7D02G090500.1};
RN [1] {ECO:0000313|EMBL:KAF7106564.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7106564.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7D02G090500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7D02G090500.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7D02G090500.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7106564.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7106564.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue. {ECO:0000256|ARBA:ARBA00002322}.
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 ECO:0000256|RuleBase:RU362060};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC ECO:0000256|RuleBase:RU362060};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3, ECO:0000256|RuleBase:RU362060};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC ECO:0000256|RuleBase:RU362060};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}.
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DR EMBL; CM022231; KAF7106564.1; -; Genomic_DNA.
DR EMBL; CM022231; KAF7106571.1; -; Genomic_DNA.
DR EMBL; CM022231; KAF7106572.1; -; Genomic_DNA.
DR EMBL; CM022231; KAF7106573.1; -; Genomic_DNA.
DR EMBL; CM022231; KAF7106574.1; -; Genomic_DNA.
DR EMBL; CM022231; KAF7106575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6TJ52; -.
DR SMR; A0A3B6TJ52; -.
DR STRING; 4565.A0A3B6TJ52; -.
DR EnsemblPlants; TraesCS7D02G090500.1; TraesCS7D02G090500.1; TraesCS7D02G090500.
DR Gramene; TraesCAD_scaffold_182980_01G000100.1; TraesCAD_scaffold_182980_01G000100.1; TraesCAD_scaffold_182980_01G000100.
DR Gramene; TraesCLE_scaffold_088677_01G000100.1; TraesCLE_scaffold_088677_01G000100.1; TraesCLE_scaffold_088677_01G000100.
DR Gramene; TraesCS7D02G090500.1; TraesCS7D02G090500.1; TraesCS7D02G090500.
DR Gramene; TraesCS7D03G0207000.1; TraesCS7D03G0207000.1.CDS; TraesCS7D03G0207000.
DR Gramene; TraesKAR7D01G0042080.1; cds.TraesKAR7D01G0042080.1; TraesKAR7D01G0042080.
DR Gramene; TraesPAR_scaffold_201457_01G000100.1; TraesPAR_scaffold_201457_01G000100.1; TraesPAR_scaffold_201457_01G000100.
DR Gramene; TraesROB_scaffold_070891_01G000600.1; TraesROB_scaffold_070891_01G000600.1; TraesROB_scaffold_070891_01G000600.
DR Gramene; TraesWEE_scaffold_219538_01G000100.1; TraesWEE_scaffold_219538_01G000100.1; TraesWEE_scaffold_219538_01G000100.
DR OMA; AVGCQAI; -.
DR OrthoDB; 337848at2759; -.
DR Proteomes; UP000019116; Chromosome 7D.
DR Proteomes; UP000815260; Chromosome 7D.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR CDD; cd00693; secretory_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 1.
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:SF277; 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|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362060};
KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060};
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 ECO:0000256|RuleBase:RU362060};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Secreted {ECO:0000256|RuleBase:RU362060};
KW Signal {ECO:0000256|RuleBase:RU362060}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT CHAIN 27..330
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT /id="PRO_5040520038"
FT DOMAIN 28..328
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
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 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 199
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 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 65
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 38..119
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 71..76
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 125..324
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 206..232
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 330 AA; 35228 MW; C09C4CDB1A86FF38 CRC64;
MAAAGAEKLY LLVACALLLL AVGCQAIPLQ IGFYHDRCPQ AEAIVKGVMM EAISQNPGNG
AAMIRMLFHD CFVEGCDASV LLDPTLFSPT PEKLSAPNNP SLRGFELIDA IKDALEAACP
GVVSCADIIA FSARDASCIL SGGKVDFEVP SGRRDGTFSN ASEPVKFLVP PTSNLSDLVD
SFVVKGLDAE DLVILSGAHT IGRSHCSAFV PDRLNVSSDI DSGLAAFLRG QCPADATPGG
NDPTVMQDVV TPNDLDRQYY NNVLSHTVLF TSDAALLTSE GTVRMVVDNA HIPGWWEDRF
EKAMVKMAGI EVKTGDQGQI RKNCRAINYY
//
