ID A0A6A6M2E5_HEVBR Unreviewed; 503 AA.
AC A0A6A6M2E5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN ORFNames=GH714_019035 {ECO:0000313|EMBL:KAF2306523.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981 {ECO:0000313|EMBL:KAF2306523.1, ECO:0000313|Proteomes:UP000467840};
RN [1] {ECO:0000313|EMBL:KAF2306523.1, ECO:0000313|Proteomes:UP000467840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GT1 {ECO:0000313|Proteomes:UP000467840};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF2306523.1};
RX PubMed=31838037; DOI=10.1016/j.molp.2019.10.017;
RA Liu J., Shi C., Shi C.C., Li W., Zhang Q.J., Zhang Y., Li K., Lu H.F.,
RA Shi C., Zhu S.T., Xiao Z.Y., Nan H., Yue Y., Zhu X.G., Wu Y., Hong X.N.,
RA Fan G.Y., Tong Y., Zhang D., Mao C.L., Liu Y.L., Hao S.J., Liu W.Q.,
RA Lv M.Q., Zhang H.B., Liu Y., Hu-Tang G.R., Wang J.P., Wang J.H., Sun Y.H.,
RA Ni S.B., Chen W.B., Zhang X.C., Jiao Y.N., Eichler E.E., Li G.H., Liu X.,
RA Gao L.Z.;
RT "The Chromosome-Based Rubber Tree Genome Provides New Insights into Spurge
RT Genome Evolution and Rubber Biosynthesis.";
RL Mol. Plant 13:336-350(2020).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR600823-3};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF2306523.1}.
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DR EMBL; JAAGAX010000008; KAF2306523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A6M2E5; -.
DR Proteomes; UP000467840; Chromosome 9.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 2.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388:SF271; PEROXIDASE; 1.
DR PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 2.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|PIRSR:PIRSR600823-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000467840};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..503
FT /note="peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025454123"
FT DOMAIN 35..503
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 379
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT DISULFID 307..499
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 386..411
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 503 AA; 54123 MW; 5DB40647C7834CCB CRC64;
MASGGSVFYL SALIILAAAA ATVASSSLSP YYYDRGCDAS ILLDPSPTID SEKNARPNLN
SARGFEVIDQ IKQAVDEVCG RPVVSCADIL AVVARDSVVA LGGPTWKVKL GRRDSTTASR
TKADSDIPSP FMDLPALINN FKNQGLNERD LVALSGGHSI GFAQCFVFRN RIYSETNIDP
KFAQQRRSTC PRNGGNSTLS PLDPTPARFD TAYFTNLIKK KGLLHSDQQL FNGGSTDGIV
KTYSSNAKAF SADFARAVML QFFWILLPPL TVKRNALPNA NSARGFEVID QIKSEVDKAC
GGAVVSCADI LAVVARDSVV ALGGPTWAVQ LGRRDSTTAS RTAAETDLPS PFADLPELIN
GFKKQGLDEK DLVVLSGAHT LGFSKCGAFK NRIYNETNID PNFAQKRRST CPPNGGDGNL
APLDPTPARF DLAYFTNLKN KKGLLHSDQQ LFNGGSTDNL VNTYSSNAPA FWNDFANSMV
KMGNIKPLTG NQGQVRLNCK MVN
//