ID A0A5N5J6M3_9PEZI Unreviewed; 443 AA. AC A0A5N5J6M3; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 24-JAN-2024, entry version 12. DE SubName: Full=Putative P450 monooxygenase {ECO:0000313|EMBL:KAB5513113.1}; GN ORFNames=GE09DRAFT_1163523 {ECO:0000313|EMBL:KAB5513113.1}; OS Coniochaeta sp. 2T2.1. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta. OX NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5513113.1, ECO:0000313|Proteomes:UP000325492}; RN [1] {ECO:0000313|EMBL:KAB5513113.1, ECO:0000313|Proteomes:UP000325492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5513113.1, RC ECO:0000313|Proteomes:UP000325492}; RX PubMed=31572496; RA Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K., RA Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.; RT "Genome expansion by allopolyploidization in the fungal strain Coniochaeta RT 2T2.1 and its exceptional lignocellulolytic machinery."; RL Biotechnol. Biofuels 12:229-229(2019). CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971, CC ECO:0000256|PIRSR:PIRSR602403-1}; CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}. 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:KAB5513113.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VSMA01000056; KAB5513113.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5N5J6M3; -. DR Proteomes; UP000325492; 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:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR CDD; cd11062; CYP58-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR InterPro; IPR036396; Cyt_P450_sf. DR PANTHER; PTHR24305; CYTOCHROME P450; 1. DR PANTHER; PTHR24305:SF157; N-ACETYLTRYPTOPHAN 6-HYDROXYLASE IVOC-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00465; EP450IV. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1, KW ECO:0000256|RuleBase:RU000461}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461, KW ECO:0000313|EMBL:KAB5513113.1}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Reference proteome {ECO:0000313|Proteomes:UP000325492}. FT BINDING 386 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1" SQ SEQUENCE 443 AA; 49772 MW; B64FB958C1314361 CRC64; MTDVLVRLHA KYGDVVRVGP NELHFAKPSA FNEIYNASLR WDKEKTLYES FGEDHSSFGL LKYAEAKQRK DVLQPLFSRR SIINMQWLVR KNMDHLAETL ARNNQKGRSA DLLFAFRCFA IDTITTYCFA KSVDAIDEPG WQAPIVLAMD NSLPTFHLFK HFPLFRKLIF SLPPWLAIKA SPDTAGLTRL QIILGEQVRD VHAHPERLSE SPHPTIYHRL LDPDAHKGCP VPDATALYEE AQTMIFAGGV TVGDALAVGF FHILDQPELL QRLRAETHAA WPDLDSPPKL EELEKLPLLT ATIKESLRMS PGASSPLLRI VPPTGATISG SVIPPGTIVG MSTVLVHMSP EIFEEPTKLN PNRWLAPGAE SLEPWLVAFS KGPRSCLGIN LAWSELYIVF ATMLRRFEMS LDGTTAEDMV WRDCFTPHFP RRHLHAWCSP VTV //