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Database: UniProt
Entry: D2JM58_FUSCE
LinkDB: D2JM58_FUSCE
Original site: D2JM58_FUSCE 
ID   D2JM58_FUSCE            Unreviewed;       376 AA.
AC   D2JM58;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cytochrome P450 monooxygenase {ECO:0000313|EMBL:ACZ56381.1};
DE   Flags: Fragment;
GN   Name=TRI11 {ECO:0000313|EMBL:ACZ56381.1};
OS   Fusarium cerealis (Fusarium crookwellense).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56641 {ECO:0000313|EMBL:ACZ56381.1};
RN   [1] {ECO:0000313|EMBL:ACZ56381.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FRC R-09624 {ECO:0000313|EMBL:ACZ56381.1};
RX   PubMed=19843228; DOI=10.1111/j.1365-2958.2009.06927.x;
RA   Proctor R.H., McCormick S.P., Alexander N.J., Desjardins A.E.;
RT   "Evidence that a secondary metabolic biosynthetic gene cluster has grown by
RT   gene relocation during evolution of the filamentous fungus Fusarium.";
RL   Mol. Microbiol. 74:1128-1142(2009).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; GQ915559; ACZ56381.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2JM58; -.
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; cd11058; CYP60B-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305:SF29; BENZOATE-PARA-HYDROXYLASE; 1.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461, ECO:0000313|EMBL:ACZ56381.1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACZ56381.1"
SQ   SEQUENCE   376 AA;  42016 MW;  715C125033737B8D CRC64;
     HMKYGPVVRI GPNMLSFNHP DAMKDVRGHR KSGEAEHGKD PIIVLSNGDN IVGSDRENHT
     RFRRALAYGF SAQAMLEQEP TFKAYVNQLF QRLHEESSNG TKTVDISKWY TFTTFDMIGD
     LAFGESFGCL DNSTYHPWVA LAFESLKSLA FMAEMGRYPR IAPYIGFLLP RGLLNKFAEN
     KELASMKVRK RLDTETDRPD FVGKITQGLK AKGSSMEFNE LASNASVLIV AGSETTATLL
     SAAVYFLCSN PRTLELLAEE VRSTYTQADA IDLVSTQGLR YMQAVLDEAL RMYPPVAGGG
     SPRKIAKGGS FVAGYFVPEN TLVENDMWAM HYDPKYFTQP HDFIPERWLG DARFSSDRLD
     AVKPFSIGPR NCIGMK
//
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