NCPR_DICDI
ID NCPR_DICDI Reviewed; 667 AA.
AC Q55CT1;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
DE AltName: Full=NADPH oxidoreductase B;
GN Name=redB; ORFNames=DDB_G0269912;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=18218133; DOI=10.1186/1471-213x-8-8;
RA Gonzalez-Kristeller D.C., Farage L., Fiorini L.C., Loomis W.F.,
RA da Silva A.M.;
RT "The P450 oxidoreductase, RedA, controls development beyond the mound stage
RT in Dictyostelium discoideum.";
RL BMC Dev. Biol. 8:8-8(2008).
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;
CC Evidence={ECO:0000255|HAMAP-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;
CC Evidence={ECO:0000255|HAMAP-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: Present during growth and development.
CC {ECO:0000269|PubMed:18218133}.
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}.
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DR EMBL; AAFI02000005; EAL72306.1; -; Genomic_DNA.
DR RefSeq; XP_646400.1; XM_641308.1.
DR AlphaFoldDB; Q55CT1; -.
DR SMR; Q55CT1; -.
DR STRING; 44689.DDB0266665; -.
DR PaxDb; Q55CT1; -.
DR EnsemblProtists; EAL72306; EAL72306; DDB_G0269912.
DR GeneID; 8617355; -.
DR KEGG; ddi:DDB_G0269912; -.
DR dictyBase; DDB_G0269912; redB.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; Q55CT1; -.
DR OMA; QKRYQRD; -.
DR PhylomeDB; Q55CT1; -.
DR Reactome; R-DDI-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DDI-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DDI-203615; eNOS activation.
DR Reactome; R-DDI-203754; NOSIP mediated eNOS trafficking.
DR Reactome; R-DDI-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DDI-5578775; Ion homeostasis.
DR Reactome; R-DDI-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR PRO; PR:Q55CT1; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:dictyBase.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 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 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; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 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..667
FT /note="NADPH--cytochrome P450 reductase"
FT /id="PRO_0000351223"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TOPO_DOM 30..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 72..215
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 277..511
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 164..173
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 199
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 468..470
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 484..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 527
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 586..587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 592..596
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 666
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
SQ SEQUENCE 667 AA; 76193 MW; F16028B0BBD08BBB CRC64;
MEILESIDFI EVLILDNLGA IIIVAVIVGT YLYMNKPPPP PPVFNKPNNK INKEAQKPKK
TITKNEDGKK VMKIFFGTQT RTAEDFSRII EKECKKIGIP CEVVDLESYE HEQELHSESF
VMFLVATHGE GDPTDNAKEF YLWLTNDERP TDLLNGVPFT VFGLGNKTYE HYNAVARVID
RRMEELGGKR VFERGEGDDD ATLEEDFNRW KKDMWPVVCK FLGYELKSTE DDKFVPRFRM
VTLNQDSKDI NDPFIKIVST PLKPKLSTDN KVIYDMKNPY YAEVLENREL HSNESDRSCR
HIEFKLGDEV SYTTGDHLGV FPINDSKLVE QLIKRLGVNG DDMIALVPID QEGSVIKASF
GPMTIRRAFS EHLDITNPVR KSVLRALAES TTNEEEKKRL LYLATEEANE EYNKYIKNDF
RGVVDLLESF PGLQPLIAHF LEFTPRLPAR MYSISSSPHN KNGVVSITSV VVNFTTGNQR
AHNGVASTWL SHLKVGDKVP LFVRESHFKL PSAATEQKPV IMVGPGTGLA PFRGFLQELQ
HRNHSQQQQS LLFFGCRSDT VDYIYREELE QYHQSSVLGD LVVAFSRKTS QKVYVQNKLL
EHKEKVWELL NKGAYFYVCG DGRNMSKAVQ QALLSIIKEF GSKDDNSAQQ FIDDMSSHGR
YLQDVWF
