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P16603

- NCPR_YEAST

UniProt

P16603 - NCPR_YEAST

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
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Binds 1 FAD per monomer.1 Publication
    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

    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

    GO - Cellular componenti

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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Transmembrane

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

    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.
    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

    MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI    50
    AQVVTENNKN YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD 100
    FESLNDVPVI VSIFISTYGE GDFPDGAVNF EDFICNAEAG ALSNLRYNMF 150
    GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG KLGEADDGAG TTDEDYMAWK 200
    DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE PSAHYLPSHQ 250
    LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK 300
    YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT 350
    TIGAAIKHYL EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE 400
    ITSKYFNIAD ALKYLSDGAK WDTVPMQFLV ESVPQMTPRY YSISSSSLSE 450
    KQTVHVTSIV ENFPNPELPD APPVVGVTTN LLRNIQLAQN NVNIAETNLP 500
    VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG PGTGVAPFRG 550
    FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD 600
    GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM 650
    AKGVSTALVG ILSRGKSITT DEATELIKML KTSGRYQEDV W 691
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 161 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