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Database: UniProt/TrEMBL
Entry: B3N5I0_DROER
LinkDB: B3N5I0_DROER
Original site: B3N5I0_DROER 
ID   B3N5I0_DROER            Unreviewed;       679 AA.
AC   B3N5I0;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   13-APR-2016, entry version 46.
DE   RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000208};
DE            EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000208};
GN   Name=Dere\GG10405 {ECO:0000313|EMBL:EDV59059.1};
GN   ORFNames=Dere_GG10405 {ECO:0000313|EMBL:EDV59059.1}, GG10405
GN   {ECO:0000313|FlyBase:FBgn0102714};
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220 {ECO:0000313|EMBL:EDV59059.1, ECO:0000313|Proteomes:UP000008711};
RN   [1] {ECO:0000313|EMBL:EDV59059.1, ECO:0000313|Proteomes:UP000008711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV59059.1}, and Tucson
RC   14021-0224.01 {ECO:0000313|Proteomes:UP000008711};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2] {ECO:0000313|EMBL:EDV59059.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV59059.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:EDV59059.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV59059.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KQS70615.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:KQS70615.1};
RG   FlyBase;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP
CC       to cytochrome P450. {ECO:0000256|PIRNR:PIRNR000208}.
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein. {ECO:0000256|PIRNR:PIRNR000208}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR000208}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|PIRNR:PIRNR000208}.
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DR   EMBL; CH954177; EDV59059.1; -; Genomic_DNA.
DR   EMBL; CH954177; KQS70615.1; -; Genomic_DNA.
DR   RefSeq; XP_001970000.1; XM_001969964.2.
DR   RefSeq; XP_015014488.1; XM_015159002.1.
DR   ProteinModelPortal; B3N5I0; -.
DR   EnsemblMetazoa; FBtr0130459; FBpp0128951; FBgn0102714.
DR   GeneID; 6542407; -.
DR   KEGG; der:Dere_GG10405; -.
DR   FlyBase; FBgn0102714; Dere\GG10405.
DR   KO; K00327; -.
DR   OMA; YEWITSG; -.
DR   OrthoDB; EOG7HQN7J; -.
DR   Proteomes; UP000008711; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_dom.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR023208; P450R.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008711};
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000208};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000208, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|PIRNR:PIRNR000208};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000208,
KW   ECO:0000313|EMBL:EDV59059.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     22     43       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       84    228       Flavodoxin-like. {ECO:0000259|PROSITE:
FT                                PS50902}.
FT   DOMAIN      283    523       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
SQ   SEQUENCE   679 AA;  76375 MW;  BD4AA0555A05A1AD CRC64;
     MASEQTIDGA AAIPSGGGDE PFLGLLDVAL LAVLIGGAAF YFLRSRKKEE EPTRSYSIQP
     TTVCTTSASD NSFIKKLKAS GRSLVVFYGS QTGTGEEFAG RLAKEGIRYR LKGMVADPEE
     CDMEELLQLK DIDNSLAVFC LATYGEGDPT DNAMEFYEWI TSGDVDLTGL NYAVFGLGNK
     TYEHYNKVAI YVDKRLEELG ANRVFELGLG DDDANIEDDF ITWKDRFWPA VCDHFGIEGG
     GEEVLIRQYR LLEQPEVQPD RIYTGEIARL HSIQNQRPPF DAKNPFLAPI KVNRELHKGG
     GRSCMHIELS IDGSKMRYDA GDHVAMFPVN DKSLVEKLGQ LCKADLDTVF SLINTDTDSS
     KKHPFPCPTT YRTALTHYLE ITAIPRTHIL KELAEYCTDE KEKELLRSMA SISPEGKEKY
     QSWIQDACRN IVHILEDIKS CRPPIDHVCE LLPRLQPRYY SISSSAKLHP TDVHVTAVLV
     EYKTPTGRIN KGVATTYLKN KQPQGSEEVK VPVFIRKSQF RLPTKPETPI IMVGPGTGLA
     PFRGFIQERQ FLRDEGKTVG ESILYFGCRK RSEDYIYESE LEEWVKKGTL NLKAAFSRDQ
     GKKVYVQHLL EQDADLIWNV IGENKGHFYI CGDAKNMAVD VRNILVKILS TKGNMSEADA
     VQYIKKMEAQ KRYSADVWS
//
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