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Database: UniProt
Entry: A0A0R0KZD9_SOYBN
LinkDB: A0A0R0KZD9_SOYBN
Original site: A0A0R0KZD9_SOYBN 
ID   A0A0R0KZD9_SOYBN        Unreviewed;       176 AA.
AC   A0A0R0KZD9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE            EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN   ORFNames=GLYMA_02G079800 {ECO:0000313|EMBL:KRH70265.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH70265.1};
RN   [1] {ECO:0000313|EMBL:KRH70265.1, ECO:0000313|EnsemblPlants:KRH70265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH70265};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH70265.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH70265}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH70265};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH70265.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH70265.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|RuleBase:RU004241}.
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DR   EMBL; CM000835; KRH70265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R0KZD9; -.
DR   SMR; A0A0R0KZD9; -.
DR   STRING; 3847.A0A0R0KZD9; -.
DR   PaxDb; 3847-GLYMA02G08780-2; -.
DR   EnsemblPlants; KRH70265; KRH70265; GLYMA_02G079800.
DR   Gramene; KRH70265; KRH70265; GLYMA_02G079800.
DR   InParanoid; A0A0R0KZD9; -.
DR   OMA; MLKAKCA; -.
DR   Proteomes; UP000008827; Chromosome 2.
DR   GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
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:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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   PANTHER; PTHR31517; -; 1.
DR   PANTHER; PTHR31517:SF87; PEROXIDASE; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 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   Iron {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   DOMAIN          31..160
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT   BINDING         48
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         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         88
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   DISULFID        50..76
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   176 AA;  19597 MW;  618F7D006696D1B8 CRC64;
     MEMMMELLSS ALECRDGTRD LPKPFNTTGV FTAKNFDVTD VVALSGTHTC GTFFNRLSPL
     DPNIDKTLAK QLQSTCPDAN SGNTANLDIR TPTLFDNKYY LDLMNRQGVF TSDQDLLSDK
     RTKALTLFFD KFVDATIRLS QLDVLTGNQG EIRAKCNVVN ARKSLLTSVV QLVDQF
//
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