ID A0A0S3R4S1_PHAAN Unreviewed; 329 AA. AC A0A0S3R4S1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 10-MAY-2017, entry version 9. 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.01G357100 {ECO:0000313|EMBL:BAT75668.1}; GN ORFNames=VIGAN_01357100 {ECO:0000313|EMBL:BAT75668.1}; 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:BAT75668.1}; RN [1] {ECO:0000313|EMBL:BAT75668.1} 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 -!- 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; BAT75668.1; -; 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; IPR019794; Peroxidases_AS. 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; PS00436; PEROXIDASE_2; 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 26 {ECO:0000256|RuleBase:RU362060}. FT CHAIN 27 329 Peroxidase. {ECO:0000256|RuleBase: FT RU362060}. FT /FTId=PRO_5006519983. FT DOMAIN 27 329 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. SQ SEQUENCE 329 AA; 36077 MW; 7618CC8998506B48 CRC64; MGRLNLILVW SLSLTLSLYN LHPTSAQLSP NHYANVCPNL ETIVRQVVTT KFQQTFVTVP ATLRLFFHDC FVQGCDASVL VASTGNNQAE KDHPDNLSLA GDGFDTVIKA KAAVDAVPQC RNKVSCADIL ALATRDVIVL SGGPSYTVEL GRFDGLVSRA SDVNGRLPHP TFDLNQLNSL FAANGLTQTD MIALSGAHTL GFSHCSKFAN RIYNFNGQTP VDPSLNRQYA IQLQQMCPRN VDPRIAINMD PTTPRRFDNV YYQNLQQGKG LFTSDQILFT DQRSRNTVNS FASNANVFNS NFIAAMTKLG RVGVKTARNG KIRTDCSVL //