ID A0A1R3KP84_9ROSI Unreviewed; 307 AA.
AC A0A1R3KP84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
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=COLO4_06024 {ECO:0000313|EMBL:OMP08886.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMP08886.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) 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. 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|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. 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 -!- 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:OMP08886.1}.
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DR EMBL; AWUE01012569; OMP08886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3KP84; -.
DR STRING; 93759.A0A1R3KP84; -.
DR OrthoDB; 1010072at2759; -.
DR Proteomes; UP000187203; 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; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR PANTHER; PTHR31235:SF338; PEROXIDASE 62; 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; 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:UP000187203};
KW Secreted {ECO:0000256|RuleBase:RU362060}.
FT DOMAIN 10..307
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 172
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 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 47
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 20..95
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 53..58
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 101..303
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 179..210
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 307 AA; 33127 MW; 80F8675CCAF732BC CRC64;
MASTLVQGQG TRVGFYSATC PNAESIVKST VQSHFRSNPA IAPGLLRMHF HDCFVHGCDA
SILIDGPNTE KTAPPNRIQG YNVIDDAKTQ LEAACPGVVS CADILALAAR DSVVLTSGRS
WQVPTGRRDG RVSLASDTSN LPGFTESIDS QKRKFADFGL NTQDLVTLVG AHTIGTTACQ
LFSYRLYNFT ANGPDPTIDS RFVSQLQALC PQNGNGGSRV DLDTGSANRF DTTFFTNLRN
GRGILESDQK LWTDASTRPI VQQFLGVRGL RAINFNVEFG RSMVKMGNIG VKTGTEGEIR
RVCTAIN
//
