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P16603

- NCPR_YEAST

UniProt

P16603 - NCPR_YEAST

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Protein

NADPH--cytochrome P450 reductase

Gene

NCP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • FAD1 PublicationNote: Binds 1 FAD per monomer.1 Publication
  • FMN1 PublicationNote: Binds 1 FMN per monomer.1 Publication

Kineticsi

The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.

  1. KM=1.59 µM for cytochrome c1 Publication
  2. KM=1.46 µM for NADPH1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671FMN1 Publication
Binding sitei187 – 1871FMN; alternate1 Publication
Binding sitei441 – 4411FAD1 Publication
Binding sitei478 – 4781FAD1 Publication
Binding sitei646 – 6461NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 788FMN; alternate1 PublicationPROSITE-ProRule annotation
Nucleotide bindingi116 – 1194FMN1 PublicationPROSITE-ProRule annotation
Nucleotide bindingi610 – 62112NADP1 PublicationAdd
BLAST

GO - Molecular functioni

  1. electron carrier activity Source: SGD
  2. FMN binding Source: InterPro
  3. iron ion binding Source: InterPro
  4. NADPH-hemoprotein reductase activity Source: SGD

GO - Biological processi

  1. ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciYEAST:YHR042W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Short name:
CPR
Short name:
P450R
Gene namesi
Name:NCP1
Synonyms:CPR1, NCPR1, PRD1
Ordered Locus Names:YHR042W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

SGDiS000001084. NCP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2417HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Disruption phenotypei

Accumulates 20% of ergosterol of wild type.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 691690NADPH--cytochrome P450 reductasePRO_0000167608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki666 – 666Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Phosphorylated by the cyclin-CDK PCL1-PHO85.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16603.
PaxDbiP16603.
PeptideAtlasiP16603.

Expressioni

Inductioni

By galactose and on the plasma membrane by iron or copper deficiency. Repressed by glucose.1 Publication

Gene expression databases

GenevestigatoriP16603.

Interactioni

Subunit structurei

Interacts with PCL1.2 Publications

Protein-protein interaction databases

BioGridi36474. 62 interactions.
DIPiDIP-8294N.
IntActiP16603. 8 interactions.
MINTiMINT-2782506.
STRINGi4932.YHR042W.

Structurei

Secondary structure

1
691
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 567Combined sources
Beta strandi60 – 667Combined sources
Beta strandi68 – 703Combined sources
Helixi71 – 8717Combined sources
Beta strandi91 – 955Combined sources
Helixi96 – 983Combined sources
Helixi104 – 1063Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi119 – 1213Combined sources
Helixi125 – 1273Combined sources
Helixi128 – 1369Combined sources
Turni139 – 1446Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 17312Combined sources
Beta strandi183 – 1864Combined sources
Turni187 – 1904Combined sources
Helixi192 – 21019Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi234 – 2396Combined sources
Helixi243 – 2453Combined sources
Beta strandi271 – 2788Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi306 – 3094Combined sources
Helixi315 – 32511Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi337 – 3393Combined sources
Beta strandi348 – 3514Combined sources
Helixi352 – 3587Combined sources
Helixi368 – 3747Combined sources
Helixi375 – 3773Combined sources
Helixi381 – 39010Combined sources
Helixi394 – 4007Combined sources
Helixi402 – 4043Combined sources
Helixi408 – 4169Combined sources
Helixi426 – 4327Combined sources
Beta strandi439 – 4435Combined sources
Turni447 – 4493Combined sources
Beta strandi453 – 4597Combined sources
Beta strandi469 – 4713Combined sources
Helixi477 – 48913Combined sources
Turni494 – 4963Combined sources
Helixi508 – 5103Combined sources
Turni511 – 5155Combined sources
Beta strandi519 – 5224Combined sources
Beta strandi536 – 5416Combined sources
Helixi542 – 5454Combined sources
Helixi546 – 56015Combined sources
Turni564 – 5663Combined sources
Beta strandi574 – 58512Combined sources
Turni587 – 5915Combined sources
Helixi592 – 5998Combined sources
Helixi600 – 6023Combined sources
Beta strandi603 – 6108Combined sources
Helixi620 – 6267Combined sources
Helixi628 – 6358Combined sources
Turni636 – 6383Combined sources
Beta strandi640 – 6456Combined sources
Helixi650 – 66516Combined sources
Helixi670 – 68213Combined sources
Beta strandi685 – 6906Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BF4X-ray3.00A/B47-691[»]
2BN4X-ray2.91A/B47-691[»]
2BPOX-ray2.90A/B47-691[»]
3FJOX-ray2.50A44-211[»]
ProteinModelPortaliP16603.
SMRiP16603. Positions 47-691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16603.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 204144Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini266 – 529264FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0369.
GeneTreeiENSGT00620000087711.
HOGENOMiHOG000282027.
InParanoidiP16603.
KOiK00327.
OMAiLGKHILF.
OrthoDBiEOG744TKC.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16603-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI
60 70 80 90 100
AQVVTENNKN YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD
110 120 130 140 150
FESLNDVPVI VSIFISTYGE GDFPDGAVNF EDFICNAEAG ALSNLRYNMF
160 170 180 190 200
GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG KLGEADDGAG TTDEDYMAWK
210 220 230 240 250
DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE PSAHYLPSHQ
260 270 280 290 300
LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK
310 320 330 340 350
YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT
360 370 380 390 400
TIGAAIKHYL EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE
410 420 430 440 450
ITSKYFNIAD ALKYLSDGAK WDTVPMQFLV ESVPQMTPRY YSISSSSLSE
460 470 480 490 500
KQTVHVTSIV ENFPNPELPD APPVVGVTTN LLRNIQLAQN NVNIAETNLP
510 520 530 540 550
VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG PGTGVAPFRG
560 570 580 590 600
FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD
610 620 630 640 650
GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM
660 670 680 690
AKGVSTALVG ILSRGKSITT DEATELIKML KTSGRYQEDV W
Length:691
Mass (Da):76,772
Last modified:January 23, 2007 - v3
Checksum:i82BB847701E5438B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti423 – 4231T → N in BAA02936. (PubMed:3139648)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti474 – 4741V → G.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13788 Genomic DNA. Translation: BAA02936.1.
U00062 Genomic DNA. Translation: AAB68904.1.
AY693091 Genomic DNA. Translation: AAT93110.1.
BK006934 Genomic DNA. Translation: DAA06734.1.
PIRiS46735.
RefSeqiNP_011908.1. NM_001179172.1.

Genome annotation databases

EnsemblFungiiYHR042W; YHR042W; YHR042W.
GeneIDi856438.
KEGGisce:YHR042W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13788 Genomic DNA. Translation: BAA02936.1 .
U00062 Genomic DNA. Translation: AAB68904.1 .
AY693091 Genomic DNA. Translation: AAT93110.1 .
BK006934 Genomic DNA. Translation: DAA06734.1 .
PIRi S46735.
RefSeqi NP_011908.1. NM_001179172.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BF4 X-ray 3.00 A/B 47-691 [» ]
2BN4 X-ray 2.91 A/B 47-691 [» ]
2BPO X-ray 2.90 A/B 47-691 [» ]
3FJO X-ray 2.50 A 44-211 [» ]
ProteinModelPortali P16603.
SMRi P16603. Positions 47-691.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36474. 62 interactions.
DIPi DIP-8294N.
IntActi P16603. 8 interactions.
MINTi MINT-2782506.
STRINGi 4932.YHR042W.

Proteomic databases

MaxQBi P16603.
PaxDbi P16603.
PeptideAtlasi P16603.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHR042W ; YHR042W ; YHR042W .
GeneIDi 856438.
KEGGi sce:YHR042W.

Organism-specific databases

SGDi S000001084. NCP1.

Phylogenomic databases

eggNOGi COG0369.
GeneTreei ENSGT00620000087711.
HOGENOMi HOG000282027.
InParanoidi P16603.
KOi K00327.
OMAi LGKHILF.
OrthoDBi EOG744TKC.

Enzyme and pathway databases

BioCyci YEAST:YHR042W-MONOMER.

Miscellaneous databases

EvolutionaryTracei P16603.
NextBioi 982042.
PROi P16603.

Gene expression databases

Genevestigatori P16603.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000208. P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13 AND 45-62.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Multiple regulatory elements control expression of the gene encoding the Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase (ERG11)."
    Turi T.G., Loper J.C.
    J. Biol. Chem. 267:2046-2056(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Cytochrome P-450 reductase is responsible for the ferrireductase activity associated with isolated plasma membranes of Saccharomyces cerevisiae."
    Lesuisse E., Casteras-Simon M., Labbe P.
    FEMS Microbiol. Lett. 156:147-152(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
  7. "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."
    Venkateswarlu K., Lamb D.C., Kelly D.E., Manning N.J., Kelly S.L.
    J. Biol. Chem. 273:4492-4496(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  8. "Activities and kinetic mechanisms of native and soluble NADPH-cytochrome P450 reductase."
    Lamb D.C., Warrilow A.G., Venkateswarlu K., Kelly D.E., Kelly S.L.
    Biochem. Biophys. Res. Commun. 286:48-54(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "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] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH PCL1.
  13. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
    Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
    J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
    Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
    Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific."
    Ivanov A.S., Gnedenko O.V., Molnar A.A., Archakov A.I., Podust L.M.
    ACS Chem. Biol. 5:767-776(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FMN-BINDING AND FAD-BINDING.
  16. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN AND NADP.

Entry informationi

Entry nameiNCPR_YEAST
AccessioniPrimary (citable) accession number: P16603
Secondary accession number(s): D3DKZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 46600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3