ID B2VRC1_PYRTR Unreviewed; 293 AA.
AC B2VRC1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=PTRG_00102 {ECO:0000313|EMBL:EDU39540.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU39540.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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:PIRSR601621-2,
CC ECO:0000256|RuleBase:RU363051};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR601621-
CC 2, ECO:0000256|RuleBase:RU363051};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR601621-2};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000256|ARBA:ARBA00006089, ECO:0000256|RuleBase:RU363051}.
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DR EMBL; DS231615; EDU39540.1; -; Genomic_DNA.
DR RefSeq; XP_001930435.1; XM_001930400.1.
DR AlphaFoldDB; B2VRC1; -.
DR STRING; 426418.B2VRC1; -.
DR EnsemblFungi; EDU39540; EDU39540; PTRG_00102.
DR GeneID; 6340453; -.
DR eggNOG; ENOG502QT8W; Eukaryota.
DR HOGENOM; CLU_041038_0_1_1; -.
DR InParanoid; B2VRC1; -.
DR OMA; HACAETP; -.
DR OrthoDB; 1010072at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31517; -; 1.
DR PANTHER; PTHR31517:SF73; PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
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:PIRSR601621-2, ECO:0000256|RuleBase:RU363051};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601621-4};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRSR:PIRSR601621-2};
KW Iron {ECO:0000256|PIRSR:PIRSR601621-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601621-2,
KW ECO:0000256|RuleBase:RU363051};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Signal {ECO:0000256|RuleBase:RU363051}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT CHAIN 19..293
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT /id="PRO_5006990941"
FT DOMAIN 16..267
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
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:PIRSR601621-2"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT SITE 55
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT DISULFID 46..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ SEQUENCE 293 AA; 31238 MW; 6B14F5EAB0978160 CRC64;
MRFSPASFLA LATAPTFALN IWPRASSCPA VWTKVAAELQ ADFAGCTADA HQSIRSSFHD
CINNGCDGSL VLTDECGRAE NMGLSKICTK IQGWATKYDV GVADMLQFAA AQGISACPLG
PKVPILIGRK DSSVAAPLHS VPGSRDPLDS ILAAFSAKGF DGKDVVALMG THSVAFQFFD
DPSQAGKTLD STPNVYDTTF YKETKDGTAP YTLQSDKLLS NSSQTENAWN SFIDNGNAWA
TAFVDAWARF AVIGNDPSQM VDCSSLVPAS RASKKRQAAV AAFTKKMSAK WRL
//
