ID NCPR_MUSDO Reviewed; 671 AA. AC Q07994; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212}; DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212}; OS Musca domestica (House fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea; OC Muscidae; Musca. OX NCBI_TaxID=7370; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Rutgers; TISSUE=Abdomen; RX PubMed=8508186; DOI=10.1016/0965-1748(93)90051-s; RA Koener J.F., Carino F.A., Feyereisen R.; RT "The cDNA and deduced protein sequence of house fly NADPH-cytochrome P450 RT reductase."; RL Insect Biochem. Mol. Biol. 23:439-447(1993). CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to CC cytochrome P450 in microsomes. It can also provide electron transfer to CC heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP-Rule:MF_03212}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_03212}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with high levels CC before metamorphosis and low levels in pupae. CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family. CC {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP- CC Rule:MF_03212}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L19897; AAA29295.1; -; mRNA. DR PIR; A56592; A56592. DR RefSeq; NP_001273818.1; NM_001286889.1. DR RefSeq; XP_011294253.1; XM_011295951.2. DR AlphaFoldDB; Q07994; -. DR SMR; Q07994; -. DR STRING; 7370.Q07994; -. DR EnsemblMetazoa; MDOA011246-RC; MDOA011246-PC; MDOA011246. DR EnsemblMetazoa; MDOA011246-RD; MDOA011246-PD; MDOA011246. DR GeneID; 101890161; -. DR KEGG; mde:101890161; -. DR CTD; 33883; -. DR VEuPathDB; VectorBase:MDOA011246; -. DR eggNOG; KOG1158; Eukaryota. DR OrthoDB; 276396at2759; -. DR BioCyc; MetaCyc:MONOMER-18499; -. DR SABIO-RK; Q07994; -. DR Proteomes; UP000095301; Unassembled WGS sequence. DR Proteomes; UP000694905; Unplaced. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule. DR CDD; cd06204; CYPOR; 1. 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 HAMAP; MF_03212; NCPR; 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; IPR023208; P450R. 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; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000208; P450R; 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 Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..671 FT /note="NADPH--cytochrome P450 reductase" FT /id="PRO_0000167603" FT TOPO_DOM 1..14 FT /note="Lumenal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT TRANSMEM 15..35 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT TOPO_DOM 36..671 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 77..221 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 276..515 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 83..88 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 135..138 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 170..179 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 205 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 295 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 451..454 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 469..471 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 475 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 485..488 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 529 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 589..590 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 595..599 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 632 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 670 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" SQ SEQUENCE 671 AA; 76358 MW; A00A2C35DFD8D129 CRC64; MSAEHVEEVV SEEPFLGTLD IALLVVLLVG ATWYFMRSRK KEEAPIRSYS IQPTTVSTVS TTENSFIKKL KASGRSLVVF YGSQTGTAEE FAGRLAKEGL RYRMKGMVAD PEECDMEELL QMKDIPNSLA VFCLATYGEG DPTDNAMEFY EWITNGEVDL TGLNYAVFGL GNKTYEHYNK VAIYVDKRLE ELGATRVFEL GLGDDDANIE DDFITWKDRF WPSVCDFFGI EGSGEEVLMR QFRLLEQPDV QPDRIYTGEI ARLHSMQNQR PPFDAKNPFL ASVIVNRELH KGGGRSCMHI ELDIDGSKMR YDAGDHIAMY PINDKILVEK LGKLCDANLD TVFSLINTDT DSSKKHPFPC PTTYRTALTH YLEITAIPRT HILKELAEYC SDEKDKEFLR NMASITPEGK EKYQNWIQNS SRNIVHILED IKSCRPPIDH ICELLPRLQP RYYSISSSSK LYPTNVHITA VLVQYETPTG RVNKGVATSY MKEKNPSVGE VKVPVFIRKS QFRLPTKSEI PIIMVGPGTG LAPFRGFIQE RQFLRDGGKV VGDTILYFGC RKKDEDFIYR EELEQYVQNG TLTLKTAFSR DQQEKIYVTH LIEQDADLIW KVIGEQKGHF YICGDAKNMA VDVRNILVKI LSTKGNMNES DAVQYIKKME AQKRYSADVW S //