ID D5GFH1_TUBMM Unreviewed; 1079 AA.
AC D5GFH1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83264.1};
GN ORFNames=GSTUM_00006891001 {ECO:0000313|EMBL:CAZ83264.1};
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:CAZ83264.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ83264.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83264.1,
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; FN430208; CAZ83264.1; -; Genomic_DNA.
DR RefSeq; XP_002839073.1; XM_002839027.1.
DR AlphaFoldDB; D5GFH1; -.
DR EnsemblFungi; CAZ83264; CAZ83264; GSTUM_00006891001.
DR GeneID; 9188212; -.
DR KEGG; tml:GSTUM_00006891001; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR InParanoid; D5GFH1; -.
DR OMA; YEIMEFF; -.
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 BINDING 373
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 1079 AA; 120668 MW; 75E4D9E9D9542926 CRC64;
MSFLGLFGGG SSANPNSEYG DESAATKEIT YTGIAEDIKA SGGKIPEDLK LLLETGAQKV
SKGPVDDKQL VMERLIGLVA SLPQNSANRK KLTSTIIDTL WDSLQHPPLS YVGDKYQYRQ
ADGSYNNILY PDLGKAGTEY ARTIRQDKKL YGAKPDAGLL FDLLMARGDN FKQNQAGISS
VLFYHASIII HDIFHTNRKD FSKSDASSYL DLAPLYGSNQ EEQNLIRTMQ DGLIKPDTFS
DKRLLGLPPG ICVLLVMYSR FHNYAAKTIK AINENGRFSL PASHATASPE DQAKNLAKLD
NNLFQTARLI TNGLYVNISL HDYIRGIANL NHSESTWTLD PRVEIDKSFD GEGTPRGVGN
QVSCEFNLLY RFHSAVSKRD DAWTKDFFGK IFPGQDPASI GISQLLQGLI VFEKSISEDP
AKRTFGGLKR TGADGSGAFN DDELVKILKE SIEDPAGAFG ANTVPEILKP VEVLGILQAR
KWQVASLNEF RAFFNLKKHK TFEDINPDPY VANTLRKLYD HPDMVEMYPG MFLEDTKPRM
DPGMGLCAPY TVTRAVFSDA VTLVRSDRHL TLDYTPANLT NWGITEVAQD YDTLGGAKMF
HLILNAFPSY FKYNSVYAMQ PFYTPTESRK IFDKFGKSYL YSFDPPAKTA SPIPILTHAG
LKRVLNDQKN FKVPWGEAME ALNNEHDFML AGDLSSHTQQ RNLVGDAIYD VTGSRKQFKD
YTEEITLKLL KREVYQLGKD PFNQVDIVRD IGNLAALHFA ASLLYLPLKS DENPNGQYSE
QELYKTLTDL TWFVFSDSDP TKSWEHRREA KKSIDKLGEI MVEEVKKFKT PIGIWDKLTG
GTGVRPPPPS LKDYGSNLVK RLLGSGKSAE DVAWMLLWSG CAFVANSACA FAQLIDFYLQ
DDNRKHWAEI QRLSSLNTPE ADKLLTKYTL EGTRLSNSLG IFRTVDPVDT QTITIKQLGQ
DVVLKKGDKV FVSFVYASKD ASVFPDPLDI KLDRPAELYV THGEGQHQCL GKDINIIQNT
YMLKTLAKLR NFRRAPGDEG KLKFISKPGG IKLYMNADWS KFTPYPTTMR VQFDGPIVA
//
