ID   D5G516_TUBMM            Unreviewed;      1119 AA.
AC   D5G516;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ79609.1};
GN   ORFNames=GSTUM_00000322001 {ECO:0000313|EMBL:CAZ79609.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ79609.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ79609.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ79609.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
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DR   EMBL; FN429995; CAZ79609.1; -; Genomic_DNA.
DR   RefSeq; XP_002835452.1; XM_002835406.1.
DR   AlphaFoldDB; D5G516; -.
DR   STRING; 656061.D5G516; -.
DR   EnsemblFungi; CAZ79609; CAZ79609; GSTUM_00000322001.
DR   GeneID; 9186307; -.
DR   KEGG; tml:GSTUM_00000322001; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   InParanoid; D5G516; -.
DR   OMA; NTEYART; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd20612; CYP_LDS-like_C; 1.
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; IPR034812; Ppo-like_N.
DR   PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 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   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         421
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"
SQ   SEQUENCE   1119 AA;  126528 MW;  052125122A9DC643 CRC64;
     MASNGDGTNG ATNGDSKYAT QSKPPPPVAK PTRAAVDSTF EQFSNLLHAS NRPLPNRFGD
     GKDQRPPELK PTGVLTDINT LRRGGFFWES VGTLWDFLKQ KAKGGAVDDK TMIMERVIQL
     TSRLPPTSKA RVALTTLQVD QLWDSLQHPP LSYLGDEFSY RQADGGYNNI MYPQLGRAGS
     AYARSVKPMT KMPGAPPDAY TLFDRIFSRG PNDEHFREHD NNVSSMLFYT ATIIIHDLFR
     TNRENQNISD TSSYLDLAPL YGSSVEDQSK IRTFQDGKIK PDSYSEKRLL AFPPGVSVLL
     IMFGRFHNYV VENLKAINEG GRFNLKFPRY PNGDDEVTRQ AKALRQQDED LFQTGRLVTC
     GLYINFILND YLRTIVNLNR VDTTWTLDPR FEASKVYNPD GTPAGIGNMV SAEFNLIYRW
     HSCISKRDDQ WTKDFYQGLF PGRDASDIEM PEFTRGVGRW ERSLSDDPIQ RNIAGLERKA
     DGSYHDDDLV KILTESVEDV AGAFGARNVP HVLRLVEVLG IEQSRKWMVG SLNELREFFG
     LKPHATFEDI NPDPAVANTL RQLYDHPDFV EMYAGLVAEA DKKPMVPGVG IGPTYTISRA
     ILSDAVTLVR GDRFYTADYT ASHLTNWGLQ EASSDLATVY GCVGYKLILK AFPNHFKFNS
     IYAHYPLTIP QENHKIHTAL NSVDQFDFER PVYTPPRIPI SSYNATKQIL CDAENFKVTW
     GAGFDFIMRA DFMLSGDKPS NSEQKQFVRD RLYLGGVDWK QQIRQFYEEA TEKLIRKKAY
     SLGDTYQVDA VRDIGNIAQT IFAASIFNLP MKSEDHPKGI YTEQELYMIL CVMFIVIFFD
     IDSSKSFPLR QAGFKVVRQY GTLVEAQVKA IKNWSWLQGV WDPLNIRGRN KSSPLKSYGW
     TMIKRLLDTG KSPYDVTWSY IVPTAGASAP NQGQIFAQVL DFYLEDRNSH HLAEIQRLAQ
     SGAVDAWETI KKYALEGGRL AGTFGLYRRV EPDNITIEDN GRNIELRKGD MVFVNFITAS
     RDPVVFPDPL EIKLDRPEAS YMQYGDGPHE CLGKAANIIG LTTMLMQFGK LKGLRRAPGP
     QGALKYIPKP GGFKVYMKED WSAYWPFPTS MKVRFDDII
//