ID A0A0S3R4I5_PHAAN Unreviewed; 331 AA. AC A0A0S3R4I5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 27-MAR-2024, entry version 38. DE RecName: Full=Peroxidase {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060}; DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060}; GN Name=Vigan.01G330600 {ECO:0000313|EMBL:BAT75441.1}; GN ORFNames=VIGAN_01330600 {ECO:0000313|EMBL:BAT75441.1}; OS Vigna angularis var. angularis. 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; Vigna. OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT75441.1, ECO:0000313|Proteomes:UP000291084}; RN [1] {ECO:0000313|EMBL:BAT75441.1, ECO:0000313|Proteomes:UP000291084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084}; RX PubMed=26616024; DOI=10.1038/srep16780; RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C., RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A., RA Tomooka N.; RT "The power of single molecule real-time sequencing technology in the de RT novo assembly of a eukaryotic genome."; RL Sci. Rep. 5:16780-16780(2015). 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. {ECO:0000256|RuleBase:RU362060}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP015034; BAT75441.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0S3R4I5; -. DR Proteomes; UP000291084; Chromosome 1. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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: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; PTHR31388:SF150; PEROXIDASE; 1. DR PANTHER; PTHR31388; PEROXIDASE 72-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; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600823-5}; 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 Reference proteome {ECO:0000313|Proteomes:UP000291084}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 23..331 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5006519988" FT DOMAIN 29..330 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 70 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT BINDING 71 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 78 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 80 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 167 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT BINDING 197 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 198 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 66 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 39..119 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 72..77 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 125..326 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 204..237 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" SQ SEQUENCE 331 AA; 36780 MW; 274ACE7A5CCF833D CRC64; MATSMSFFLL LSLLAFAPLC FCNYYQEGKL YPQFYDYSCP QAQNIVKSIL AKYVQQQPRL PASILRLHFH DCFVKGCDAS LLLDSSESII SEKGSNPNRN SARGFEVIDA IKAALERECP STVSCADILT LAARDSVVLS GGPSWEVPLG RRDSRDASIS GSNNNIPAPN NTFQTILTKF RLHGLDLVDL VALSGGHTIG NARCTTFRQR LYSQISGNGK PDSTLDQYYA AALRNRCPRS GGDQNLFFLD YATPYKFDNT YFKNLLAYKG LLSSDQILLT DQESAELVKS YAESNDIFFE QFAKSMIKMG NISPLTNSRG EIRENCRKIN A //