ID   CP176_GIBF5             Reviewed;         550 AA.
AC   S0ENB0;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Cytochrome P450 monooxygenase FFUJ_09176 {ECO:0000303|PubMed:28295904};
DE            EC=1.-.-.- {ECO:0000269|PubMed:28295904};
DE   AltName: Full=DMATS1 biosynthesis cluster protein FFUJ_09176 {ECO:0000303|PubMed:28295904};
DE   Flags: Precursor;
GN   ORFNames=FFUJ_09176;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28295904; DOI=10.1002/cbic.201600691;
RA   Arndt B., Janevska S., Schmid R., Huebner F., Tudzynski B., Humpf H.U.;
RT   "A Fungal N-Dimethylallyltryptophan Metabolite from Fusarium fujikuroi.";
RL   ChemBioChem 18:899-904(2017).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the DMATS1 gene
CC       cluster that mediates the biosynthesis of a reversely N-prenylated
CC       monomeric L-tryptophan (r-N-DMAT) (PubMed:28295904). Seems not to
CC       contribute to the final DMATS1 product (PubMed:28295904).
CC       {ECO:0000269|PubMed:28295904}.
CC   -!- INDUCTION: Expression is negaticely regulated by the global nitrogen
CC       regulator areA. {ECO:0000269|PubMed:28295904}.
CC   -!- DISRUPTION PHENOTYPE: Does not alter the amount of produced r-N-DMAT.
CC       {ECO:0000269|PubMed:28295904}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; HF679031; CCT73988.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0ENB0; -.
DR   SMR; S0ENB0; -.
DR   EnsemblFungi; CCT73988; CCT73988; FFUJ_09176.
DR   VEuPathDB; FungiDB:FFUJ_09176; -.
DR   HOGENOM; CLU_001570_2_1_1; -.
DR   Proteomes; UP000016800; Chromosome 9.
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   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..550
FT                   /note="Cytochrome P450 monooxygenase FFUJ_09176"
FT                   /id="PRO_5004496262"
FT   REGION          430..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         466
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:0000250|UniProtKB:P04798"
SQ   SEQUENCE   550 AA;  62432 MW;  A712F2C798AE6AA3 CRC64;
     MLQTIPMPSR ELTIALAVLS LLMVLVQRAG SRRRETKQLL SLPPSPPCAN IIAGHLPTVL
     KAAKEHRQHL LFQKWAEEYG EVFFVQLGTI QEYFINSDQA VRAIFDKAAA QTSERPRWIV
     SNEQICNRLN LLLLSSSEKA WKSQRKATTF GLTNLNLADA GLPFLHFETL KFLNDIGQNP
     SKGADPQSLW SSIGRYTYST FSSQIFGLDV PEDNSPVIDY IFETGLAQIL GMLPGYYLVD
     TFNILDKLPL FLKPWERDAK SRHKRDYEWC CDKLKKVKSQ IDAGEAPPHM TFIRRVIEDP
     NHLGLDSLED ASYLGMMLII GASDTSRIST WSFLEAMLTF PDVCNKARKV IDSAVGDRVP
     VFEDLERVPY IRQVMKESWR WRPPVALGHP HTTTRDIMYK NYRIPKGARI HLNAWAIHRD
     PTRYPDPENF IPERFEGDTR SSQESAASPD VSKRDHFVFG AGRRICPGYH VADRSFAVSV
     MRILWAFDIS LKPGTKLPLD PQSFPGDMPG NPGLELPVVL TVRSPERLET IQKEFEAAVQ
     SRERMEPLVG