ID A0A397Z0P1_BRACM Unreviewed; 333 AA.
AC A0A397Z0P1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, 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=BRARA_F02292 {ECO:0000313|EMBL:RID59041.1};
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID59041.1, ECO:0000313|Proteomes:UP000264353};
RN [1] {ECO:0000313|EMBL:RID59041.1, ECO:0000313|Proteomes:UP000264353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA Yotsui I., Zachgo S., Schmutz J.;
RT "WGS assembly of Brassica rapa FPsc.";
RL Submitted (JUN-2018) 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}.
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DR EMBL; CM010633; RID59041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397Z0P1; -.
DR Proteomes; UP000264353; Chromosome a6.
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:SF268; PEROXIDASE 70; 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 Secreted {ECO:0000256|RuleBase:RU362060};
KW Signal {ECO:0000256|RuleBase:RU362060}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT CHAIN 27..333
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU362060"
FT /id="PRO_5017098849"
FT DOMAIN 36..333
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 198
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 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 73
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 46..122
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 79..84
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 128..329
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 205..237
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 333 AA; 36398 MW; 192D753F4BFC3EDB CRC64;
MASVTNFNPH GVFLPLFLVL AATATATTRP YTSLPRPRVG YYSSACWNVE SIVRSVVQSN
YFTNPANAPG ILRMHFHDCF VRGCDGSILL DGPNSEKTAI PNQSLRGFNV IEEAKTQLEI
ACPLTVSCAD ILALAARDFV VLTGGPWWPV PLGRLDGRVS LASNVDLPEP TDSVAVQKQR
FAAKYLNTQD LVVLAAGHTI GTVGCGVFRD RFFNYKNTGS PDPTINPNFV PQIQSQCPLN
GNAATRVALD LGSEGQFDTS YLNNLRFGRG VLESDQVLWN DPETRPIVER LLGLRFPFLL
FGPEFARSMS KMSLTEVKTG LDGEIRRVCS AIN
//
