ID   B0DZX3_LACBS            Unreviewed;      1120 AA.
AC   B0DZX3;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 74.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ99796.1};
GN   ORFNames=LACBIDRAFT_315146 {ECO:0000313|EMBL:EDQ99796.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDQ99796.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
CC   -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00298}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00298}.
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DR   EMBL; DS547158; EDQ99796.1; -; Genomic_DNA.
DR   RefSeq; XP_001889488.1; XM_001889453.1.
DR   AlphaFoldDB; B0DZX3; -.
DR   GeneID; 6085191; -.
DR   KEGG; lbc:LACBIDRAFT_315146; -.
DR   HOGENOM; CLU_002329_0_0_1; -.
DR   InParanoid; B0DZX3; -.
DR   OrthoDB; 823504at2759; -.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR050783; Oxylipin_biosynth_metab.
DR   InterPro; IPR034812; Ppo-like_N.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   PANTHER; PTHR11903:SF37; PSI-PRODUCING OXYGENASE A; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT   ACT_SITE        219
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00298"
FT   BINDING         394
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:PIRSR619791-2"
FT   SITE            272
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00298"
SQ   SEQUENCE   1120 AA;  125225 MW;  2CC164A56F85244D CRC64;
     MSLRYIRDRI VKRVDFIAES RAPLDTDGAH PQSHVFEKTV TEIHELLVKP AFQVSDLGAY
     WDAIQNLSTV GLNDRDLLLE KVLVLMSRLQ HTKISLKVQQ FVINLLYKDL PHPPSGYLGL
     SPSSTLCHHH KTLEDASTHA LVKYAYRAAD GSNYNPLFPT LGKAGSPYAR SVPSANIVPS
     SALPDPELVF DTLLRRQKFV PHPGGISSLF FAFADLVIHS IFNTNHFDWS INDASSYLDL
     SVLYGSSESQ VNSVRRRDGT GKLFDDVFAD SRLLFMPPAS CALLVLLNRN HNYIAEKILN
     INENGNLSSP PPEDEKLRLA QDDEIFHRAR LVNCGYFMHI ILGDYVGAIL GLVRDESDWR
     LDPLMTMREI SHEFVPQGEG NVVSIEFNLL YRWHATLSAQ DEKWTEGEFN KLFKGKNPND
     VTIEDFKNAA HEFMLPPKDP RVWTFKDLKR DDKGRFNDAD LAQILQDATE WRAGAYGARG
     TPEVLRVIEI MGMKQARSWG TCSLNEFRKF LGLRPYETFA EWNPDREIHT AAAALYRDID
     NLELHVGLQA EQTKKPGPGA GLCPGYTISR SILADAVCLT RGDRFLTVDF NPFNLTSWGY
     QDCQYDKKDG SYGGLLTKLL FRTLPEHYQR GSAYAHFPFL DPVFMREENL AKTNPSLVDK
     YIWTRPRQDS PTVPFDTLES VKKVLKDPHF VSAYDHRLYN VVKPFLPKKR PSAFTTVSKR
     LSIIKKSTPT TAVTPTKENE VPEAIRHLHE GVSQVSSLIH GESTADWVAF FSKATEDLIK
     AKAFEPVSKG VKYVDIVKDV INILPIHWIS HSIAGLPLKT SANPGGVWYE QDTYHKFAVI
     ASYVYLNFDP VNDWHLRESS QRYSAEILDI IHAHIEKLTG IQLSIPDALN HLSIGASNKS
     HDFLKKVIDA NGKNNTRHEL AAQVFSATIP TAPLYSQAIA KVVDFYLARE QAVARQEIVN
     LANSKDKDAP SKILAYVREA LRLNPTVAGV YRTAAQDVLV GSKRVNATEH AFASIVKANL
     DPEVFGPHPS VASYSRPADK AGITTIGDFG LLSPVFFDAT APVILGKILS LKNLKPAPGK
     SGTLLSFKEN WNGTPSTQYI NTEGIVGPFP DSLLVQFTPA
//