ID A0A0S3R4I5_PHAAN Unreviewed; 331 AA. AC A0A0S3R4I5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 10-MAY-2017, entry version 8. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00709852}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00709852}; 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Vigna. OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT75441.1}; RN [1] {ECO:0000313|EMBL:BAT75441.1} RP NUCLEOTIDE SEQUENCE. 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: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS00709881}. 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 --------------------------------------------------------------------------- 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 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; IPR010255; Haem_peroxidase. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. 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|RuleBase:RU362060}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00506910}; KW Heme {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00709882}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00709895}; KW Metal-binding {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS00709843}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS00709839}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS00709844}; 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}. 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 //