ID D2JLR2_9HYPO Unreviewed; 310 AA.
AC D2JLR2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NADPH-cytochrome P450 reductase {ECO:0000313|EMBL:ACZ56044.1};
DE Flags: Fragment;
GN Name=CPR1 {ECO:0000313|EMBL:ACZ56044.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:ACZ56044.1};
RN [1] {ECO:0000313|EMBL:ACZ56044.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:ACZ56044.1};
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=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};
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DR EMBL; GQ915466; ACZ56044.1; -; Genomic_DNA.
DR AlphaFoldDB; D2JLR2; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..257
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACZ56044.1"
FT NON_TER 310
FT /evidence="ECO:0000313|EMBL:ACZ56044.1"
SQ SEQUENCE 310 AA; 34589 MW; CCF18680E31DAEB4 CRC64;
PIAESYELFS AKDRNCLHME VDISGSNLKY ETGDHIAIWP TNPGEEVNRF LDILDLSGKQ
HTVITVKALE PTAKVPFPNP TTYDAILRYH LEICAPVSRQ FVSTLAAFAP NDDIKAEMNR
LGSDKDYFHE KTGPHYYNIA RFLSSVSKGE KWSKIPFSAF VEGLTKLQPR YYSISSSSLV
QPKKISITAV VESQQIPGRD DPFRGVATNY LFALKQKQNG DPNPAPFGQT YELTGPRNKY
DGIHVPVHVR HSNFKLPSDP GKPIIMIGPG TGVAPFRGFV QERAKLARDG VEVGKTLLFF
GCRKPSEDFM
//