ID W7MHK7_GIBM7 Unreviewed; 951 AA.
AC W7MHK7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Bifunctional P-450:NADPH-P450 reductase {ECO:0000313|EMBL:EWG47020.1};
GN ORFNames=FVEG_07269 {ECO:0000313|EMBL:EWG47020.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG47020.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG47020.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; DS022250; EWG47020.1; -; Genomic_DNA.
DR RefSeq; XP_018753211.1; XM_018895861.1.
DR AlphaFoldDB; W7MHK7; -.
DR GeneID; 30065090; -.
DR VEuPathDB; FungiDB:FVEG_07269; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000009096; Chromosome 8.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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 CDD; cd06206; bifunctional_CYPOR; 1.
DR CDD; cd11068; CYP120A1; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF127; BIFUNCTIONAL CYTOCHROME P450_NADPH--P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 385..526
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 561..789
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 951 AA; 105076 MW; 7FF1A19156F1DE54 CRC64;
MFPEMHDIAT QLCMKFARHG PRTPIDASDN FTRLALDTLA LCAMDFRFNS YYKEELHPFI
EAMGDFLTES GNRNRRPPFA PNFLYRAANE KFYNDIALMK SVADEVVAAR KASPSDRKDL
LAAMLNGVDP QTGEKLSDEN ITNQLITFLI AGHETTSGTL SFAMYQLLKN PEAYSKVQKE
VDEVVGRGPV LVEHLTKLPY ISAVLRETLR INSPISAFGL EAIDDTFLGG KYLVKKGEIV
TALLSRGHVD PAVYGSDADK FIPERMLDDE FARLNKEYPN CWKPFGNGKR ACIGRPFAWQ
ESLLAMVVLF QNFNFTMTDP NYALEIQQTL TIKPVHFYIN ATLRHGMTPT ELEHVLAGSG
GTSSSNHNIK SAANSDVKAG SGKPMAIFYG SNSGTCEALA NRLASDAPSH GFSATTVGPL
DQAKQSLPED RPVVIVTASY EGQPPSNAAH FIKWMEDLDG NEMEKVSYAV FACGHHDWVE
TFHRIPKLVD STLEKRGGTR LVPMGSADAA TSDMFSDFEA WEDTVLWPGL KEKYKISDEE
SGGQKGLLVE VSTPRKTSLR QDVEEALVVA EKTLTKSGPA KKHIEIQLPS AMTYKAGDYL
AILPLNPKST VARVFRRFSL AWDSFLKIQS EGPTTLPTNV AISAFDVFSA YVELSQPATK
RNILALAEAT EDKATIQELE RLAGDAYQAE ISPKRVSVLD LLEKFPAVAL PISSYLAMLP
PMRVRQYSIS SSPFADPSKL TLTYSLLDAP SLSGQGRHVG VATNFLSQLT AGDKLHVSVR
ASSEAFHLPS DAEKTPIICV AAGTGLAPFR GFIQERAAML AAGRTLAPAL LFFGCRNPEV
DDLYAEEFER WEKMGAVDVR RAYSRAADKS EGCKYVQDRV YHDRADVFKV WDQGAKVFIC
GSREIGKAVE DVCVRLAIEK AQQNGKDVTE EMARAWFERS RNERFATDVF D
//
