NADPH--cytochrome P450 reductase - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
    NADPH--cytochrome P450 reductase
      Short name=CPR
      Short name=P450R
    EC=1.6.2.4

Gene names

Name:	NCP1
Synonyms:	NCPR1, PRD1
Ordered Locus Names:	YHR042W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	691 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
Catalytic activity	NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein.
Cofactor	Binds 1 FAD per monomer. Binds 1 FMN per monomer.
Subunit structure	Interacts with PCL1. Ref.6
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein.
Post-translational modification	Phosphorylated by the cyclin-CDK PCL1-PHO85. Ref.6
Miscellaneous	Present with 46600 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Inferred from mutant phenotype. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from direct assay. Source: SGD mitochondrial outer membrane Inferred from direct assay. Source: SGD
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from direct assay. Source: SGD iron ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	Q12164	1	EBI-11940,EBI-30000
AGP1	P25376	1	EBI-11940,EBI-2357
ERG11	P10614	1	EBI-11940,EBI-5127
PHO84	P25297	1	EBI-11940,EBI-13320
PIS1	P06197	1	EBI-11940,EBI-13458
PMP2	P40975	1	EBI-11940,EBI-2043041
RPN3	P40016	1	EBI-11940,EBI-15927
RPT2	P40327	1	EBI-11940,EBI-13901
STE24	P47154	1	EBI-11940,EBI-18298

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.1

Chain

2 – 691

690

NADPH--cytochrome P450 reductase

PRO_0000167608

Regions

Transmembrane

8 – 24

17

Potential

Domain

61 – 204

144

Flavodoxin-like

Domain

266 – 529

264

FAD-binding FR-type

Nucleotide binding

71 – 78

8

FMN; alternate

Nucleotide binding

116 – 119

4

FMN

Nucleotide binding

610 – 621

12

NADP

Sites

Binding site

67

1

FMN

Binding site

187

1

FMN; alternate

Binding site

441

1

FAD

Binding site

478

1

FAD

Binding site

646

1

NADP

Amino acid modifications

Cross-link

666

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Natural variations

Natural variant

474

1

V → G

Experimental info

Sequence conflict

423

1

T → N in BAA02936. Ref.1

Secondary structure

1

.

691

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P16603-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 82BB847701E5438B
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FASTA

691

76,772

        10         20         30         40         50         60 
MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI AQVVTENNKN 

        70         80         90        100        110        120 
YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD FESLNDVPVI VSIFISTYGE 

       130        140        150        160        170        180 
GDFPDGAVNF EDFICNAEAG ALSNLRYNMF GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG 

       190        200        210        220        230        240 
KLGEADDGAG TTDEDYMAWK DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE 

       250        260        270        280        290        300 
PSAHYLPSHQ LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK 

       310        320        330        340        350        360 
YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT TIGAAIKHYL 

       370        380        390        400        410        420 
EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE ITSKYFNIAD ALKYLSDGAK 

       430        440        450        460        470        480 
WDTVPMQFLV ESVPQMTPRY YSISSSSLSE KQTVHVTSIV ENFPNPELPD APPVVGVTTN 

       490        500        510        520        530        540 
LLRNIQLAQN NVNIAETNLP VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG 

       550        560        570        580        590        600 
PGTGVAPFRG FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD 

       610        620        630        640        650        660 
GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM AKGVSTALVG 

       670        680        690 
ILSRGKSITT DEATELIKML KTSGRYQEDV W

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene." Yabusaki Y., Murakami H., Ohkawa H. J. Biochem. 103:1004-1010(1988) [PubMed: 3139648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13 AND 45-62.
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." 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. Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Hitchcock A.L., Auld K., Gygi S.P., Silver P.A. Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, MASS SPECTROMETRY.
[6]	"The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit." Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr. Genetics 166:1177-1186(2004) [PubMed: 15082539] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH PCL1.
[7]	"A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases." Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N., Lepesheva G.I., Kelly S.L., Waterman M.R., Podust L.M. Structure 14:51-61(2006) [PubMed: 16407065] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN AND NADP.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

D13788 Genomic DNA. Translation: BAA02936.1.
U00062 Genomic DNA. Translation: AAB68904.1.
AY693091 Genomic DNA. Translation: AAT93110.1.

PIR

S46735.

RefSeq

NP_011908.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BF4	X-ray	3.00	A/B	34-691	[»]
2BN4	X-ray	2.91	A/B	34-691	[»]
2BPO	X-ray	2.90	A/B	34-691	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:8294N.

IntAct

P16603. 19 interactions.

Proteomic databases

PeptideAtlas

P16603.

Genome annotation databases

Ensembl

YHR042W. Saccharomyces cerevisiae. [Contig view]

GeneID

856438.

GenomeReviews

Gene locus YHR042W in contig U00093_GR.

KEGG

sce:YHR042W.

NMPDR

fig|4932.3.peg.3057.

Organism-specific databases

CYGD

YHR042w.

SGD

S000001084. NCP1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P16603.

OMA

P16603. PEECDME.

Enzyme and pathway databases

BRENDA

1.6.2.4. 250.

Gene expression databases

ArrayExpress

P16603.

GermOnline

YHR042W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015702. NADPH_Cyt_P450_Rdtase.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]

PANTHER

PTHR19384:SF17. NADPH_Cyt_Red. 1 hit.

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

PROSITE

PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

982042.

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Entry information

Entry name

NCPR_YEAST

Accession

Primary (citable) accession number: P16603

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents