ID A0A5B6X107_9ROSI Unreviewed; 285 AA.
AC A0A5B6X107;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 03-MAY-2023, entry version 15.
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=EPI10_031689 {ECO:0000313|EMBL:KAA3487891.1};
OS Gossypium australe.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=47621 {ECO:0000313|EMBL:KAA3487891.1, ECO:0000313|Proteomes:UP000325315};
RN [1] {ECO:0000313|Proteomes:UP000325315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PA1801 {ECO:0000313|Proteomes:UP000325315};
RX PubMed=31479566; DOI=10.1111/pbi.13249;
RA Cai Y., Cai X., Wang Q., Wang P., Zhang Y., Cai C., Xu Y., Wang K.,
RA Zhou Z., Wang C., Geng S., Li B., Dong Q., Hou Y., Wang H., Ai P., Liu Z.,
RA Yi F., Sun M., An G., Cheng J., Zhang Y., Shi Q., Xie Y., Shi X., Chang Y.,
RA Huang F., Chen Y., Hong S., Mi L., Sun Q., Zhang L., Zhou B., Peng R.,
RA Zhang X., Liu F.;
RT "Genome sequencing of the Australian wild diploid species Gossypium
RT australe highlights disease resistance and delayed gland morphogenesis.";
RL Plant Biotechnol. J. 0:0-0(2019).
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. 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:KAA3487891.1}.
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DR EMBL; SMMG02000001; KAA3487891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B6X107; -.
DR Proteomes; UP000325315; Chromosome 13.
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; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR PANTHER; PTHR31235:SF39; PEROXIDASE 39; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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:UP000325315};
KW Secreted {ECO:0000256|RuleBase:RU362060}.
FT DOMAIN 1..284
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 43
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 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 150
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 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 35
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 8..86
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 41..46
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 92..280
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 157..190
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 285 AA; 31251 MW; D14F4C84A46C23E4 CRC64;
MNFYASSCSK AEQIVLDYVK QHIPNAPSLA ASFLRMHFHD CIVRGCDASV LLNSTSGQAE
KNAVPILTLR GFDFIERVKS LLEAECPGVV SCADILTLVA RDSVVTTGGP FWNVPTGRRD
GMISNITEEN TNIPSPFHNF TTLLTLFSGH TIGISLCPAV SRRLYNSTGP GGIDPPMDSK
YAENLKANKC KIVSDSTTIL EMDPGGRKTF DFSYYSLLLK RRGLFQSDAA LTTDLTSLAF
INQLLTSPPQ FFFNEFSKAM EKMGRVNVKT GSEGQIRKQC ALVNN
//
