ID A0A0S3R4S1_PHAAN Unreviewed; 329 AA. AC A0A0S3R4S1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 02-JUN-2021, entry version 25. 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.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; 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: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., 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 -!- 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. These functions might be dependent on each CC isozyme/isoform in each plant tissue. {ECO:0000256|ARBA:ARBA00002322}. 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|ARBA:ARBA00001913}; 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|ARBA:ARBA00001970}; 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. CC {ECO:0000256|RuleBase:RU004241}. 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; 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, ECO:0000256|RuleBase:RU362060}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600823-5}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362060}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR600823-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600823-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362060}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, 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..26 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 27..329 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5006519983" FT DOMAIN 27..329 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 68 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 69 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 72 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 74 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 76 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 78 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 90 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 198 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 199 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 250 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 253 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 258 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 168 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 64 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 37..120 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 70..75 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 126..326 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 205..237 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" 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 //