ID S8DK87_9LAMI Unreviewed; 298 AA.
AC S8DK87;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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};
DE Flags: Fragment;
GN ORFNames=M569_14928 {ECO:0000313|EMBL:EPS59877.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS59877.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS59877.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
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|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|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. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}.
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:EPS59877.1}.
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DR EMBL; AUSU01008006; EPS59877.1; -; Genomic_DNA.
DR AlphaFoldDB; S8DK87; -.
DR OrthoDB; 1010072at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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 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; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31517; -; 1.
DR PANTHER; PTHR31517:SF81; PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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}; 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 Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Secreted {ECO:0000256|RuleBase:RU362060}.
FT DOMAIN 1..298
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 170
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 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 37
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 10..91
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 43..48
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 97..294
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 177..204
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS59877.1"
SQ SEQUENCE 298 AA; 32549 MW; 28461F659BEA017F CRC64;
LSVGFYDQSC PQMGSVVRAH VQSLAITDPT SPPAFLRLLF HDCQVQGCDA SILLDSDGGR
IRSPEMDSSR NFAVRNRGAI ETIKTELENL CPRRVSCSDI IVLAAREAVA ITGGPRISVP
LGRRDSTAVP SSGLADASLP PADSGVDAML RIFDRKDMTR EESVAILGAH TLGRTHCFNL
RNRLYNFTDD PSNSPFELIL RANCPPYAAA SSTITVQNDV TSSFFDSQYY LDSISGRGVL
KIDAEMAVDP RTQPIVERFA RDQDEFFRAF SSAFVKLSYS GVLTGDNGAI RRRCNSLD
//
