ID A0A0S3R4I5_PHAAN Unreviewed; 331 AA. AC A0A0S3R4I5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 13-NOV-2019, entry version 17. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; 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; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC 50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade; OC 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., RA Kaga A., Tomooka N.; RT "The power of single molecule real-time sequencing technology in the RT de 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 CC catabolism, response to environmental stresses such as wounding, CC pathogen attack and oxidative stress. CC {ECO:0000256|RuleBase:RU362060}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + CC 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; CC EC=1.11.1.7; Evidence={ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215718}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant CC (class III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215721}. 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 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. 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 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 Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 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, KW ECO:0000256|RuleBase:RU362060}; KW Complete proteome {ECO:0000313|Proteomes:UP000291084}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00449210}; KW Heme {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215736}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215715}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215733}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215720}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215725}; KW Reference proteome {ECO:0000313|Proteomes:UP000291084}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1 22 {ECO:0000256|RuleBase:RU362060}. FT CHAIN 23 331 Peroxidase. {ECO:0000256|RuleBase: FT RU362060}. FT /FTId=PRO_5006519988. FT DOMAIN 29 330 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT ACT_SITE 70 70 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR600823-1}. FT METAL 71 71 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 74 74 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 76 76 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 78 78 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 80 80 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 92 92 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 197 197 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 198 198 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 250 250 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 253 253 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 258 258 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT BINDING 167 167 Substrate; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-2}. FT SITE 66 66 Transition state stabilizer. FT {ECO:0000256|PIRSR:PIRSR600823-4}. 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 //