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Database: UniProt
Entry: D2JM38_GIBPU
LinkDB: D2JM38_GIBPU
Original site: D2JM38_GIBPU 
ID   D2JM38_GIBPU            Unreviewed;       368 AA.
AC   D2JM38;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cytochrome P450 monooxygenase {ECO:0000313|EMBL:ACZ56413.1};
DE   Flags: Fragment;
GN   Name=TRI4 {ECO:0000313|EMBL:ACZ56413.1};
OS   Gibberella pulicaris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5128 {ECO:0000313|EMBL:ACZ56413.1};
RN   [1] {ECO:0000313|EMBL:ACZ56413.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FRC R-07843 {ECO:0000313|EMBL:ACZ56413.1};
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}.
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DR   EMBL; GQ915539; ACZ56413.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2JM38; -.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Monooxygenase {ECO:0000313|EMBL:ACZ56413.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ACZ56413.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACZ56413.1"
FT   NON_TER         368
FT                   /evidence="ECO:0000313|EMBL:ACZ56413.1"
SQ   SEQUENCE   368 AA;  41934 MW;  644E5561A7ED4623 CRC64;
     LWEIAKMHDK YGPIVRVNAH EVHIRDSSYY STIYTAGARK TNKDPATVGA FDVPTATAAT
     VDHDQHRARR GYLNPYFSKR TITNLEPFIH ERVTKLLSRF QEHLDNNQIL SLDGAFCALT
     ADVITSRFYG KHYNYLDLPD FHFVVRDGFL GLTKVYHLAR FLPFLVTILK RLPYSCLRMI
     APSVSDLLQM RNEIQDRGAG EFLSNKTTEA KSSILFGALA DTHIPLAERT VERMLDEGTV
     ILFAGTETTS RTLAITLFYL LTHPECLKKL REELSNLPKV EDDKFTLATL ENLPYLNGVV
     HEGFRLAFGP ISRSGRVATQ ENLKYKDHII PAGTPISQST YFMHTDPKIF PEPSKFRPER
     WIEAAEKQ
//
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