ID A0A3B5Y5G8_WHEAT Unreviewed; 332 AA.
AC A0A3B5Y5G8;
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};
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:TraesCS1A02G342300.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS1A02G342300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS1A02G342300.1};
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 [2] {ECO:0000313|EnsemblPlants:TraesCS1A02G342300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
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 AlphaFoldDB; A0A3B5Y5G8; -.
DR SMR; A0A3B5Y5G8; -.
DR STRING; 4565.A0A3B5Y5G8; -.
DR PaxDb; 4565-Traes_1AL_A982D9220-1; -.
DR EnsemblPlants; TraesCS1A02G342300.1; TraesCS1A02G342300.1; TraesCS1A02G342300.
DR Gramene; TraesCAD_scaffold_021946_01G000200.1; TraesCAD_scaffold_021946_01G000200.1; TraesCAD_scaffold_021946_01G000200.
DR Gramene; TraesCLE_scaffold_044466_01G000200.1; TraesCLE_scaffold_044466_01G000200.1; TraesCLE_scaffold_044466_01G000200.
DR Gramene; TraesCS1A02G342300.1; TraesCS1A02G342300.1; TraesCS1A02G342300.
DR Gramene; TraesCS1A03G0845000.1; TraesCS1A03G0845000.1.CDS; TraesCS1A03G0845000.
DR Gramene; TraesKAR1A01G0334640.1; cds.TraesKAR1A01G0334640.1; TraesKAR1A01G0334640.
DR Gramene; TraesPAR_scaffold_042009_01G000200.1; TraesPAR_scaffold_042009_01G000200.1; TraesPAR_scaffold_042009_01G000200.
DR Gramene; TraesROB_scaffold_036613_01G000200.1; TraesROB_scaffold_036613_01G000200.1; TraesROB_scaffold_036613_01G000200.
DR Gramene; TraesWEE_scaffold_033953_01G000200.1; TraesWEE_scaffold_033953_01G000200.1; TraesWEE_scaffold_033953_01G000200.
DR OrthoDB; 337848at2759; -.
DR Proteomes; UP000019116; Chromosome 1A.
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:SF231; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..25
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT CHAIN 26..332
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT /id="PRO_5017097884"
FT DOMAIN 30..330
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
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 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 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 201
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 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 40..121
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 73..78
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 127..326
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 208..234
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 332 AA; 35635 MW; 6C8E1C5E66F7CA96 CRC64;
MAAVAAKPQV LVACAMLLLA VGCQASPFWP LEIGYYHDKC PQAEAVVKGV MEKAISQNPG
NGAAMIRMLF HDCFVEGCDA SVLLDPTPFS PTPEKLSPPN DPTLRGFELI DAIKDALEVA
CPGVVSCADI VAFAARDASS ILSRGKINFQ MPSGRRDGTF SNASEPLKFL VPPTSNLSDL
VASFVIKGLN AEDLVVLSGA HTIGRSHCSS FVSDRLNTPS DINGGLAAFL RGQCPADATP
GGNDPTVMQD VVTPNKLDRQ YYKNVLSHTV LFTSDAALMT SAETARMVVE NAKIPGWWED
RFEKAMVKMA GIEVKTGYQG QIRKNCRAIN HY
//
