ID A0A4R0RWI2_9APHY Unreviewed; 358 AA.
AC A0A4R0RWI2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN Name=MNP3_3 {ECO:0000313|EMBL:TCD71225.1};
GN ORFNames=EIP91_011703 {ECO:0000313|EMBL:TCD71225.1};
OS Steccherinum ochraceum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Steccherinaceae; Steccherinum.
OX NCBI_TaxID=92696 {ECO:0000313|EMBL:TCD71225.1, ECO:0000313|Proteomes:UP000292702};
RN [1] {ECO:0000313|EMBL:TCD71225.1, ECO:0000313|Proteomes:UP000292702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LE-BIN_3174 {ECO:0000313|EMBL:TCD71225.1,
RC ECO:0000313|Proteomes:UP000292702};
RA Fedorova T.V., Glazunova O.A., Landesman E.O., Moiseenko K.V.,
RA Psurtseva N.V., Savinova O.S., Shakhova N.V., Tyazhelova T.V., Vasina D.V.;
RT "Genome assembly of Steccherinum ochraceum LE-BIN_3174, the white-rot
RT fungus of the Steccherinaceae family (The Residual Polyporoid clade,
RT Polyporales, Basidiomycota).";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:TCD71225.1}.
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DR EMBL; RWJN01000008; TCD71225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R0RWI2; -.
DR STRING; 92696.A0A4R0RWI2; -.
DR Proteomes; UP000292702; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00692; ligninase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356:SF8; L-ASCORBATE PEROXIDASE 6-RELATED; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 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; PS00436; PEROXIDASE_2; 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|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR601621-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601621-2};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601621-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000292702};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363051}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT CHAIN 22..358
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT /id="PRO_5021036238"
FT DOMAIN 69..338
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 196
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 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT SITE 70
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT DISULFID 29..42
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 41..305
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 61..140
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 269..334
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ SEQUENCE 358 AA; 37444 MW; 8FA02F49EDA2AE1C CRC64;
MAFKTLAALL SVVGALQVAN AAITKRVACP DGVNTATNAA CCSLFAIRDD IQENLFDGGE
CGEEVHESLR LTFHDAIGIG SNGGGGADGS MIVFDDIETN FHANNGVDEI VDAQKPFIAR
HNITPGDFIQ FAGAIGVSNC PGAPQLDFFL GRPAPIAPAP DLTVPEPFDT VDSILARFAD
AGNFSPQEVV ALLGSHTIAA ADHVDPSIPG TPFDSTPFTF DTQFFVETQL RGTLFPGTGG
NQGEVESPLH GEIRLQSDSE LARDERTACE WQSFVNNLPK LQNAFKAAML KLSVLGHNVN
DMVDCSELIP VPKGFTGAAT FPAGLSHADV EQACATTPFP TLASDPGPAT SVAPVPPS
//
