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NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4)

 NCPR_YEAST              Reviewed;         691 AA.
P16603; D3DKZ0;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 197.
RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
Name=NCP1 {ECO:0000255|HAMAP-Rule:MF_03212};
Synonyms=CPR1, NCPR1, PRD1;
OrderedLocusNames=YHR042W {ECO:0000312|SGD:S000001084};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13 AND
45-62.
PubMed=3139648; DOI=10.1093/oxfordjournals.jbchem.a122370;
Yabusaki Y., Murakami H., Ohkawa H.;
"Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450
reductase deduced from nucleotide sequence of its cloned gene.";
J. Biochem. 103:1004-1010(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=1730736;
Turi T.G., Loper J.C.;
"Multiple regulatory elements control expression of the gene encoding
the Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-
demethylase (ERG11).";
J. Biol. Chem. 267:2046-2056(1992).
[6]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=9368374; DOI=10.1111/j.1574-6968.1997.tb12720.x;
Lesuisse E., Casteras-Simon M., Labbe P.;
"Cytochrome P-450 reductase is responsible for the ferrireductase
activity associated with isolated plasma membranes of Saccharomyces
cerevisiae.";
FEMS Microbiol. Lett. 156:147-152(1997).
[7]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION,
TOPOLOGY, AND DISRUPTION PHENOTYPE.
PubMed=9468503; DOI=10.1074/jbc.273.8.4492;
Venkateswarlu K., Lamb D.C., Kelly D.E., Manning N.J., Kelly S.L.;
"The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP)
oxidoreductase is not required for catalytic activity in sterol
biosynthesis or in reconstitution of CYP activity.";
J. Biol. Chem. 273:4492-4496(1998).
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
TOPOLOGY.
PubMed=11485306; DOI=10.1006/bbrc.2001.5338;
Lamb D.C., Warrilow A.G., Venkateswarlu K., Kelly D.E., Kelly S.L.;
"Activities and kinetic mechanisms of native and soluble NADPH-
cytochrome P450 reductase.";
Biochem. Biophys. Res. Commun. 286:48-54(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=14557538; DOI=10.1073/pnas.2135500100;
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response
to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[13]
PHOSPHORYLATION, AND INTERACTION WITH PCL1.
PubMed=15082539; DOI=10.1534/genetics.166.3.1177;
Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
"The identification of Pcl1-interacting proteins that genetically
interact with Cla4 may indicate a link between G1 progression and
mitotic exit.";
Genetics 166:1177-1186(2004).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823961; DOI=10.1021/pr050477f;
Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
"Toward the complete yeast mitochondrial proteome: multidimensional
separation techniques for mitochondrial proteomics.";
J. Proteome Res. 5:1543-1554(2006).
[15]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16407407; DOI=10.1091/mbc.E05-08-0740;
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
"Proteomic analysis of the yeast mitochondrial outer membrane reveals
accumulation of a subclass of preproteins.";
Mol. Biol. Cell 17:1436-1450(2006).
[16]
FMN-BINDING AND FAD-BINDING.
PubMed=20557022; DOI=10.1021/cb100055v;
Ivanov A.S., Gnedenko O.V., Molnar A.A., Archakov A.I., Podust L.M.;
"FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at
the surface is highly specific.";
ACS Chem. Biol. 5:767-776(2010).
[17]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[18]
X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD;
FMN AND NADP.
PubMed=16407065; DOI=10.1016/j.str.2005.09.015;
Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N.,
Lepesheva G.I., Kelly S.L., Waterman M.R., Podust L.M.;
"A second FMN binding site in yeast NADPH-cytochrome P450 reductase
suggests a mechanism of electron transfer by diflavin reductases.";
Structure 14:51-61(2006).
[19]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 44-211 IN COMPLEX WITH FMN.
PubMed=19483672; DOI=10.1038/embor.2009.82;
Aigrain L., Pompon D., Morera S., Truan G.;
"Structure of the open conformation of a functional chimeric NADPH
cytochrome P450 reductase.";
EMBO Rep. 10:742-747(2009).
-!- FUNCTION: This enzyme is required for electron transfer from NADP
to cytochrome P450 in microsomes. It can also provide electron
transfer to heme oxygenase and cytochrome B5. Involved in
ergosterol biosynthesis. Has NADPH-dependent ferrireductase
activity on the plasma membrane. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11485306, ECO:0000269|PubMed:1730736,
ECO:0000269|PubMed:9368374, ECO:0000269|PubMed:9468503}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11485306, ECO:0000269|PubMed:9368374,
ECO:0000269|PubMed:9468503}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9468503};
Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9468503};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9468503};
Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9468503};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.59 uM for cytochrome c {ECO:0000269|PubMed:11485306};
KM=1.46 uM for NADPH {ECO:0000269|PubMed:11485306};
Note=The Vmax of the reaction is 721 pmol/min/pmol enzyme
towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.
{ECO:0000269|PubMed:11485306};
-!- SUBUNIT: Interacts with PCL1. {ECO:0000269|PubMed:15082539,
ECO:0000269|PubMed:16407065}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:9468503}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306,
ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-
Rule:MF_03212, ECO:0000305|PubMed:11485306,
ECO:0000305|PubMed:9468503}. Mitochondrion outer membrane
{ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961}; Single-
pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503};
Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}. Cell
membrane {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9368374}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306,
ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-
Rule:MF_03212, ECO:0000305|PubMed:11485306,
ECO:0000305|PubMed:9468503}.
-!- INDUCTION: By galactose and on the plasma membrane by iron or
copper deficiency. Repressed by glucose.
{ECO:0000269|PubMed:9368374}.
-!- PTM: Phosphorylated by the cyclin-CDK PCL1-PHO85.
{ECO:0000269|PubMed:15082539}.
-!- DISRUPTION PHENOTYPE: Accumulates 20% of ergosterol of wild type.
{ECO:0000269|PubMed:9468503}.
-!- MISCELLANEOUS: Present with 46600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family.
{ECO:0000255|HAMAP-Rule:MF_03212}.
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EMBL; D13788; BAA02936.1; -; Genomic_DNA.
EMBL; U00062; AAB68904.1; -; Genomic_DNA.
EMBL; AY693091; AAT93110.1; -; Genomic_DNA.
EMBL; BK006934; DAA06734.1; -; Genomic_DNA.
PIR; S46735; S46735.
RefSeq; NP_011908.1; NM_001179172.1.
PDB; 2BF4; X-ray; 3.00 A; A/B=47-691.
PDB; 2BN4; X-ray; 2.91 A; A/B=47-691.
PDB; 2BPO; X-ray; 2.90 A; A/B=47-691.
PDB; 3FJO; X-ray; 2.50 A; A=44-211.
PDBsum; 2BF4; -.
PDBsum; 2BN4; -.
PDBsum; 2BPO; -.
PDBsum; 3FJO; -.
ProteinModelPortal; P16603; -.
SMR; P16603; -.
BioGrid; 36474; 64.
DIP; DIP-8294N; -.
IntAct; P16603; 9.
MINT; P16603; -.
STRING; 4932.YHR042W; -.
iPTMnet; P16603; -.
MaxQB; P16603; -.
PaxDb; P16603; -.
PRIDE; P16603; -.
EnsemblFungi; YHR042W; YHR042W; YHR042W.
GeneID; 856438; -.
KEGG; sce:YHR042W; -.
EuPathDB; FungiDB:YHR042W; -.
SGD; S000001084; NCP1.
GeneTree; ENSGT00840000129757; -.
HOGENOM; HOG000282027; -.
InParanoid; P16603; -.
KO; K00327; -.
OMA; TKMDVAF; -.
OrthoDB; EOG092C1RRH; -.
BioCyc; YEAST:YHR042W-MONOMER; -.
BRENDA; 1.6.2.4; 984.
Reactome; R-SCE-1222556; ROS, RNS production in phagocytes.
Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-SCE-203615; eNOS activation.
Reactome; R-SCE-211897; Cytochrome P450 - arranged by substrate type.
Reactome; R-SCE-392154; Nitric oxide stimulates guanylate cyclase.
Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-SCE-5578775; Ion homeostasis.
Reactome; R-SCE-9033241; Peroxisomal protein import.
EvolutionaryTrace; P16603; -.
PRO; PR:P16603; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009055; F:electron transfer activity; IDA:SGD.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:SGD.
GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD.
Gene3D; 1.20.990.10; -; 1.
Gene3D; 3.40.50.360; -; 1.
HAMAP; MF_03212; NCPR; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR023208; P450R.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PIRSF; PIRSF000208; P450R; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein;
FMN; Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Membrane;
Mitochondrion; Mitochondrion outer membrane; NADP; Oxidoreductase;
Phosphoprotein; Reference proteome; Steroid biosynthesis;
Steroid metabolism; Sterol biosynthesis; Sterol metabolism;
Transmembrane; Transmembrane helix; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3139648}.
CHAIN 2 691 NADPH--cytochrome P450 reductase.
/FTId=PRO_0000167608.
TOPO_DOM 2 7 Lumenal. {ECO:0000305}.
TRANSMEM 8 24 Helical. {ECO:0000255}.
TOPO_DOM 25 691 Cytoplasmic. {ECO:0000305}.
DOMAIN 61 204 Flavodoxin-like. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 266 529 FAD-binding FR-type. {ECO:0000255|HAMAP-
Rule:MF_03212}.
NP_BIND 67 72 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065,
ECO:0000269|PubMed:19483672}.
NP_BIND 116 119 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065,
ECO:0000269|PubMed:19483672}.
NP_BIND 152 161 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065,
ECO:0000269|PubMed:19483672}.
NP_BIND 439 442 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
NP_BIND 457 459 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
NP_BIND 476 479 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
NP_BIND 610 611 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
NP_BIND 617 621 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
BINDING 78 78 FMN; alternate.
{ECO:0000269|PubMed:16407065}.
BINDING 187 187 FMN. {ECO:0000255|HAMAP-Rule:MF_03212}.
BINDING 187 187 FMN; alternate.
{ECO:0000269|PubMed:16407065}.
BINDING 285 285 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
BINDING 543 543 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
BINDING 646 646 NADP. {ECO:0000269|PubMed:16407065}.
BINDING 691 691 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:16407065}.
CROSSLNK 666 666 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
VARIANT 474 474 V -> G.
CONFLICT 423 423 T -> N (in Ref. 1; BAA02936).
{ECO:0000305}.
HELIX 50 56 {ECO:0000244|PDB:3FJO}.
STRAND 60 66 {ECO:0000244|PDB:3FJO}.
STRAND 68 70 {ECO:0000244|PDB:3FJO}.
HELIX 71 87 {ECO:0000244|PDB:3FJO}.
STRAND 91 95 {ECO:0000244|PDB:3FJO}.
HELIX 96 98 {ECO:0000244|PDB:3FJO}.
HELIX 104 106 {ECO:0000244|PDB:3FJO}.
STRAND 109 116 {ECO:0000244|PDB:3FJO}.
STRAND 119 121 {ECO:0000244|PDB:3FJO}.
HELIX 125 127 {ECO:0000244|PDB:3FJO}.
HELIX 128 136 {ECO:0000244|PDB:3FJO}.
TURN 139 144 {ECO:0000244|PDB:3FJO}.
STRAND 146 153 {ECO:0000244|PDB:3FJO}.
STRAND 157 159 {ECO:0000244|PDB:3FJO}.
HELIX 162 173 {ECO:0000244|PDB:3FJO}.
STRAND 183 186 {ECO:0000244|PDB:3FJO}.
TURN 187 190 {ECO:0000244|PDB:3FJO}.
HELIX 192 210 {ECO:0000244|PDB:3FJO}.
STRAND 223 226 {ECO:0000244|PDB:2BN4}.
STRAND 234 239 {ECO:0000244|PDB:2BN4}.
HELIX 243 245 {ECO:0000244|PDB:2BPO}.
STRAND 271 278 {ECO:0000244|PDB:2BPO}.
STRAND 287 293 {ECO:0000244|PDB:2BPO}.
STRAND 306 309 {ECO:0000244|PDB:2BPO}.
HELIX 315 325 {ECO:0000244|PDB:2BPO}.
STRAND 332 334 {ECO:0000244|PDB:2BPO}.
STRAND 337 339 {ECO:0000244|PDB:2BPO}.
STRAND 348 351 {ECO:0000244|PDB:2BPO}.
HELIX 352 358 {ECO:0000244|PDB:2BPO}.
HELIX 368 374 {ECO:0000244|PDB:2BPO}.
HELIX 375 377 {ECO:0000244|PDB:2BN4}.
HELIX 381 390 {ECO:0000244|PDB:2BPO}.
HELIX 394 400 {ECO:0000244|PDB:2BPO}.
HELIX 402 404 {ECO:0000244|PDB:2BPO}.
HELIX 408 416 {ECO:0000244|PDB:2BPO}.
HELIX 426 432 {ECO:0000244|PDB:2BPO}.
STRAND 439 443 {ECO:0000244|PDB:2BPO}.
TURN 447 449 {ECO:0000244|PDB:2BPO}.
STRAND 453 459 {ECO:0000244|PDB:2BPO}.
STRAND 469 471 {ECO:0000244|PDB:2BF4}.
HELIX 477 489 {ECO:0000244|PDB:2BPO}.
TURN 494 496 {ECO:0000244|PDB:2BPO}.
HELIX 508 510 {ECO:0000244|PDB:2BPO}.
TURN 511 515 {ECO:0000244|PDB:2BPO}.
STRAND 519 522 {ECO:0000244|PDB:2BPO}.
STRAND 536 541 {ECO:0000244|PDB:2BPO}.
HELIX 542 545 {ECO:0000244|PDB:2BPO}.
HELIX 546 560 {ECO:0000244|PDB:2BPO}.
TURN 564 566 {ECO:0000244|PDB:2BN4}.
STRAND 574 585 {ECO:0000244|PDB:2BPO}.
TURN 587 591 {ECO:0000244|PDB:2BPO}.
HELIX 592 599 {ECO:0000244|PDB:2BPO}.
HELIX 600 602 {ECO:0000244|PDB:2BPO}.
STRAND 603 610 {ECO:0000244|PDB:2BPO}.
HELIX 620 626 {ECO:0000244|PDB:2BPO}.
HELIX 628 635 {ECO:0000244|PDB:2BPO}.
TURN 636 638 {ECO:0000244|PDB:2BPO}.
STRAND 640 645 {ECO:0000244|PDB:2BPO}.
HELIX 650 665 {ECO:0000244|PDB:2BPO}.
HELIX 670 682 {ECO:0000244|PDB:2BPO}.
STRAND 685 690 {ECO:0000244|PDB:2BPO}.
SEQUENCE 691 AA; 76772 MW; 82BB847701E5438B CRC64;
MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI AQVVTENNKN
YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD FESLNDVPVI VSIFISTYGE
GDFPDGAVNF EDFICNAEAG ALSNLRYNMF GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG
KLGEADDGAG TTDEDYMAWK DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE
PSAHYLPSHQ LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK
YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT TIGAAIKHYL
EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE ITSKYFNIAD ALKYLSDGAK
WDTVPMQFLV ESVPQMTPRY YSISSSSLSE KQTVHVTSIV ENFPNPELPD APPVVGVTTN
LLRNIQLAQN NVNIAETNLP VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG
PGTGVAPFRG FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD
GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM AKGVSTALVG
ILSRGKSITT DEATELIKML KTSGRYQEDV W


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