ID A0A654EWP8_ARATH Unreviewed; 329 AA. AC A0A654EWP8; A0A5S9X0K1; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 02-JUN-2021, entry version 8. 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 ORFNames=AN1_LOCUS8619 {ECO:0000313|EMBL:VYS53158.1}, AT9943_LOCUS7391 GN {ECO:0000313|EMBL:CAD5319201.1}, C24_LOCUS8472 GN {ECO:0000313|EMBL:CAA0369522.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:VYS53158.1, ECO:0000313|Proteomes:UP000426265}; RN [1] {ECO:0000313|EMBL:VYS53158.1, ECO:0000313|Proteomes:UP000426265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. An-1 {ECO:0000313|Proteomes:UP000426265}, and cv. C24 RC {ECO:0000313|Proteomes:UP000434276}; RA Jiao W.-B., Schneeberger K.; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAD5319201.1, ECO:0000313|Proteomes:UP000516314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ashkenazy H.; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. 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 -!- 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. 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; CACSHJ010000088; CAA0369522.1; -; Genomic_DNA. DR EMBL; LR881467; CAD5319201.1; -; Genomic_DNA. DR EMBL; CACRSJ010000105; VYS53158.1; -; Genomic_DNA. DR RefSeq; NP_179828.1; NM_127806.4. DR SMR; A0A654EWP8; -. DR GeneID; 816773; -. DR KEGG; ath:AT2G22420; -. DR OMA; CRVANSR; -. DR Proteomes; UP000426265; Unassembled WGS sequence. DR Proteomes; UP000434276; Unassembled WGS sequence. DR Proteomes; UP000516314; Chromosome 2. 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; IPR033905; Secretory_peroxidase. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 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}; Heme {ECO:0000256|RuleBase:RU362060}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060}; KW Peroxidase {ECO:0000256|RuleBase:RU362060}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 21..329 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5028498820" FT DOMAIN 39..285 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|Pfam:PF00141" FT ACT_SITE 63 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 64 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 67 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 69 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 71 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 73 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 85 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 190 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 242 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 244 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 249 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 160 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 59 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 32..112 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 65..70 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 118..315 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 197..229 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" SQ SEQUENCE 329 AA; 36670 MW; 6BF861DE592968BA CRC64; MSLLPHLILY LTLLTVVVTG ETLRPRFYSE TCPEAESIVR REMKKAMIKE ARSVASVMRF QFHDCFVNGC DASLLLDDTP NMLGEKLSLS NIDSLRSFEV VDDIKEALEK ACPATVSCAD IVIMAARDAV ALTGGPDWEV KLGRKDSLTA SQQDSDDIMP SPRANATFLI DLFERFNLSV KDMVALSGSH SIGQGRCFSI MFRLYNQSGS GKPDPALEPS YRKKLDKLCP LGGDENVTGD LDATPQVFDN QYFKDLVSGR GFLNSDQTLY TNLVTREYVK MFSEDQDEFF RAFAEGMVKL GDLQSGRPGE IRFNCRVVNR RPIDVLLVS //