ID   A0A3B6ATT5_WHEAT        Unreviewed;       363 AA.
AC   A0A3B6ATT5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060};
DE            EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060};
GN   ORFNames=CFC21_015837 {ECO:0000313|EMBL:KAF6999861.1};
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:TraesCS2A02G149400.1};
RN   [1] {ECO:0000313|EMBL:KAF6999861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF6999861.1};
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:TraesCS2A02G149400.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS2A02G149400.1};
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:TraesCS2A02G149400.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF6999861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF6999861.1};
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; CM022214; KAF6999861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6ATT5; -.
DR   SMR; A0A3B6ATT5; -.
DR   STRING; 4565.A0A3B6ATT5; -.
DR   PaxDb; 4565-Traes_2AS_C24F72BD8-1; -.
DR   EnsemblPlants; TraesCS2A02G149400.1; TraesCS2A02G149400.1; TraesCS2A02G149400.
DR   Gramene; TraesCAD_scaffold_072676_01G000100.1; TraesCAD_scaffold_072676_01G000100.1; TraesCAD_scaffold_072676_01G000100.
DR   Gramene; TraesCLE_scaffold_199769_01G000100.1; TraesCLE_scaffold_199769_01G000100.1; TraesCLE_scaffold_199769_01G000100.
DR   Gramene; TraesCS2A02G149400.1; TraesCS2A02G149400.1; TraesCS2A02G149400.
DR   Gramene; TraesCS2A03G0307600.1; TraesCS2A03G0307600.1.CDS; TraesCS2A03G0307600.
DR   Gramene; TraesKAR2A01G0070490.1; cds.TraesKAR2A01G0070490.1; TraesKAR2A01G0070490.
DR   Gramene; TraesPAR_scaffold_188974_01G000100.1; TraesPAR_scaffold_188974_01G000100.1; TraesPAR_scaffold_188974_01G000100.
DR   Gramene; TraesWEE_scaffold_157589_01G000100.1; TraesWEE_scaffold_157589_01G000100.1; TraesWEE_scaffold_157589_01G000100.
DR   OMA; CTSNLLM; -.
DR   OrthoDB; 357890at2759; -.
DR   Proteomes; UP000019116; Chromosome 2A.
DR   Proteomes; UP000815260; Chromosome 2A.
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; IPR019793; Peroxidases_heam-ligand_BS.
DR   InterPro; IPR033905; Secretory_peroxidase.
DR   PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR   PANTHER; PTHR31235:SF374; PLANT HEME PEROXIDASE FAMILY PROFILE DOMAIN-CONTAINING PROTEIN; 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; 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|RuleBase:RU362060};
KW   Hydrogen peroxide {ECO:0000256|RuleBase:RU362060};
KW   Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3,
KW   ECO:0000256|RuleBase:RU362060};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362060};
KW   Peroxidase {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..23
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT   CHAIN           24..363
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT                   /id="PRO_5040519234"
FT   DOMAIN          64..361
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          24..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         108
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         110
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         112
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         125
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="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT   BINDING         231
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         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   SITE            98
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT   DISULFID        74..151
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        157..357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        238..268
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   363 AA;  39026 MW;  180DF6299C9A76E5 CRC64;
     MAKLAAALTV LALLGCMARE GQADYGHPSP PPSTPCSPGH PSTPPSTATP PPPAPVPSPP
     ASAELVVGYY QKTCHRAEDI VRETVRGANA GIMAGLVRLF FHDCFIRGCD ASVLLDLADP
     SSATEKFGLP NLSLRGFEVI DAAKARIEKE CGNVVSCADV LAFAGRDATY FLSNKKVYFE
     MPAGRYDGRV SLINETLIHL PPPFATVEQL KANFASKGLS ADEMVTLSGA HTIGVSHCSS
     FDDDFSDRLN ASTSDMDPKL MASLEKQCRS DTGNDNTVVQ DIKTPNKLDN KYYKNVLSHE
     VLFASDAALL TADDTSAAVR AYAEDNNVWE EKFKAAMVRM GAIEVKTSAD GEIRRSCRIL
     NTY
//