ID A0A0S3R4S1_PHAAN Unreviewed; 329 AA. AC A0A0S3R4S1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 13-NOV-2019, entry version 18. 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.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; 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:BAT75668.1, ECO:0000313|Proteomes:UP000291084}; RN [1] {ECO:0000313|EMBL:BAT75668.1, 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; BAT75668.1; -; 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; 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|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 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}. FT ACT_SITE 68 68 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR600823-1}. FT METAL 69 69 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 72 72 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 74 74 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 76 76 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 78 78 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 90 90 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 198 198 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 199 199 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 168 168 Substrate; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-2}. FT SITE 64 64 Transition state stabilizer. FT {ECO:0000256|PIRSR:PIRSR600823-4}. 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 //