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Database: UniProt
Entry: A0A6A3BMQ7_HIBSY
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ID   A0A6A3BMQ7_HIBSY        Unreviewed;       211 AA.
AC   A0A6A3BMQ7;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE            EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN   ORFNames=F3Y22_tig00110015pilonHSYRG00056
GN   {ECO:0000313|EMBL:KAE8718280.1};
OS   Hibiscus syriacus (Rose of Sharon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX   NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8718280.1, ECO:0000313|Proteomes:UP000436088};
RN   [1] {ECO:0000313|EMBL:KAE8718280.1, ECO:0000313|Proteomes:UP000436088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAE8718280.1};
RA   Kim Y.-M.;
RT   "Draft genome information of white flower Hibiscus syriacus.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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:KAE8718280.1}.
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DR   EMBL; VEPZ02000813; KAE8718280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A3BMQ7; -.
DR   OrthoDB; 1010072at2759; -.
DR   Proteomes; UP000436088; Unassembled WGS sequence.
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:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.10.520.10; -; 1.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR000823; Peroxidase_pln.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31388:SF126; PEROXIDASE; 1.
DR   PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR600823-5};
KW   Iron {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3};
KW   Oxidoreductase {ECO:0000313|EMBL:KAE8718280.1};
KW   Peroxidase {ECO:0000313|EMBL:KAE8718280.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000436088}.
FT   DOMAIN          1..211
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT   BINDING         127
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         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   DISULFID        134..159
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   211 AA;  22871 MW;  74E820C93D960732 CRC64;
     MKNPPKTRPT IDSEKNSRPN QNSARGFEVI DEIKAEVDKI CGRPVVSCAD IVAVAARDSV
     VAARDSVVAL GGPSWKVLLG RRDSTTASRT QADTYLPAPF MDLPALINNF KNQGLNERDL
     VALSGGHTIG FAQCFTFRNR IYNATNIDPV FAENRRATCP RTGGDTNLAP LDPTPARFDN
     AYFNNLVKQR GLLISDQALF SGGSTDDLVS T
//
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