ID   B6SVQ7_MAIZE            Unreviewed;       665 AA.
AC   B6SVQ7;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   03-MAY-2023, entry version 67.
DE   SubName: Full=NADPH--cytochrome P450 reductase {ECO:0000313|EMBL:ACG28940.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG28940.1};
RN   [1] {ECO:0000313|EMBL:ACG28940.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(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; EU956822; ACG28940.1; -; mRNA.
DR   AlphaFoldDB; B6SVQ7; -.
DR   ExpressionAtlas; B6SVQ7; baseline and differential.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 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; 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:SF126; NADPH--CYTOCHROME P450 REDUCTASE 2; 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   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
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; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
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}.
FT   DOMAIN          97..247
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          304..546
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          59..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  72858 MW;  4D653573D27D0D00 CRC64;
     MDSATSGAME LVAALLRGRV PPELGGEGAE GRAVVATLAA AVLGAALFVL RRRAAAGNKR
     KTEGAAATEA TRAKARGVKV SAEEEEEKPA DDGRKKVTVF FGTQTGTAEG FAKALAEEAK
     ARYDKAIFKV VDLDDYAAED EEYEEKLKKE KLALFFVATY GDGEPTDNAA RFYKWFTEGN
     ERGIWLHDFE YAVFGLGNRQ YEHFNKVAKV VDEILTEQGG KRLVPVGLGD DDQCIEDDFN
     TWKETLWPEL DRLLGDGNDI STGTTYTAAI PEYRVEFMGP EEAAHLERNS SLANGHAVHD
     AQHPCKFRAD VAVRRELHTP ASDRSCTHLE FDIAGTGLTY ETGDHVGVCT ENCPEVVEEA
     ERLLGYSPDT SFTIHADRDD GSPPPFPSPT TLRNALARYA DLLNSPKKAS LVALATYASD
     PAEADRLTFL ASAAGKDEYA QWVVASQRSL LEVMAEFPSA KPPLGVFFAA VAPRLQPRYY
     SISSSPSMAP TRIHVTCALV HETTPAGRVH KGVCSTWIKN AVPSEGSEDC SSWAPIFVRK
     SNFKLPADPS VPIIMIGPGT GLAPFRGFLQ ERLAWKESGA ELGRSVFFFG CRNSKMDFIY
     EDELSNFLEQ GALFELVLAF SRQGPTKEYV QHKMAQKASE IWDMISQGAY IYVCGDARRH
     GQRCT
//