ID F0ZAP9_DICPU Unreviewed; 708 AA.
AC F0ZAP9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000208};
DE EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000208};
GN ORFNames=DICPUDRAFT_148280 {ECO:0000313|EMBL:EGC38958.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC38958.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC cytochrome P450. {ECO:0000256|PIRNR:PIRNR000208}.
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|PIRNR:PIRNR000208};
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 -!- 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}.
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; GL870966; EGC38958.1; -; Genomic_DNA.
DR RefSeq; XP_003284523.1; XM_003284475.1.
DR AlphaFoldDB; F0ZAP9; -.
DR STRING; 5786.F0ZAP9; -.
DR EnsemblProtists; EGC38958; EGC38958; DICPUDRAFT_148280.
DR GeneID; 10506248; -.
DR KEGG; dpp:DICPUDRAFT_148280; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; F0ZAP9; -.
DR OMA; QKRYQRD; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
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; IPR036291; NAD(P)-bd_dom_sf.
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 InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00106; adh_short; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000208}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000208};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000208};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000208};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..216
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 278..512
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 40..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 80445 MW; 0606D4791128A829 CRC64;
MEMVLEYVDL IESLIIDNLG AIIIVVVIVG TYLYMNKPPP PPPIPQNKKA PIKPQRTESN
KGGKKENKEK EKVMKIFFGT QTRTAEDFSR IIEKESKKIG IPCEVVDLES YDVEDLANEW
FVMFLVSTHG EGDPTDNAKE FYLWLTNDER PTDLLTGVPF TVFGLGNKTY EHYNAVARVI
DRRMEELGAK RAFERGEGDD DATLEEDFNH WKKRMWPVIC PFLGYELKAT DEDKFVPRFR
MVTLDSENKD ITNPFLKVVP TISKPKTSVD GKTIYDIKNP YYATITENRE LHSSESDRSC
RHIEFALGGA VTYQTGDHLG IYPINDGELV EKLIQRLGVN GEEIISLIPA DQEGNIIKAS
FGPMSIRKAL SEHFDITNPP RKSVLRTLSE YTTDEQEKKK LLRLASEEAS EEYNQFIKHD
FRSIGELLDN FPNLKPNIAH FLEFIPRLPA RYYSISSSPN HKKDTVSITS VVVNFTTPTS
RFHNGVASTW LSNLKVGDKV PLFVRESHFR LPSNTNKPVI MVGPGTGLAP FRGFLQEMQH
KSVNSSESLL FFGCRSDTID YLYKEELEQY KSTGVIGDLI VAFSRKTNEK VYVQNKIMEH
KHKVWDLIHN KGAHFYICGD ARNMAKSVQQ SLVSLIKELG SKDDNSAQQY IEDMESVKKI
INISSIVGFY SRQCGFSIYS STKFAVEAIT EGLQEDVIHV SSILPGYF
//
