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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: 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.UniRule annotation4 Publications

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.UniRule annotation3 Publications

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotation1 PublicationNote: Binds 1 FAD per monomer.UniRule annotation1 Publication
  • FMNUniRule annotation1 PublicationNote: Binds 1 FMN per monomer.UniRule annotation1 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 Publication

Manual assertion based on experiment ini

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei78FMN; alternate1 Publication1
    Binding sitei187FMNUniRule annotation1
    Binding sitei187FMN; alternate1 Publication1
    Binding sitei285NADPUniRule annotation1 Publication1
    Binding sitei543NADPUniRule annotation1 Publication1
    Binding sitei646NADP1 Publication1
    Binding sitei691FADUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi67 – 72FMNUniRule annotation2 Publications6
    Nucleotide bindingi116 – 119FMNUniRule annotation2 Publications4
    Nucleotide bindingi152 – 161FMNUniRule annotation2 Publications10
    Nucleotide bindingi439 – 442FADUniRule annotation1 Publication4
    Nucleotide bindingi457 – 459FADUniRule annotation1 Publication3
    Nucleotide bindingi476 – 479FADUniRule annotation1 Publication4
    Nucleotide bindingi610 – 611NADPUniRule annotation1 Publication2
    Nucleotide bindingi617 – 621NADPUniRule annotation1 Publication5

    GO - Molecular functioni

    • electron carrier activity Source: SGD
    • flavin adenine dinucleotide binding Source: UniProtKB-HAMAP
    • FMN binding Source: UniProtKB-HAMAP
    • NADP binding Source: UniProtKB-HAMAP
    • NADPH-hemoprotein reductase activity Source: SGD

    GO - Biological processi

    • 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.
    BRENDAi1.6.2.4. 984.
    ReactomeiR-SCE-211897. Cytochrome P450 - arranged by substrate type.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation)
    Short name:
    CPRUniRule annotation
    Short name:
    P450RUniRule annotation
    Gene namesi
    Name:NCP1UniRule annotation
    Synonyms:CPR1, NCPR1, PRD1
    Ordered Locus Names:YHR042WImported
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VIII

    Organism-specific databases

    EuPathDBiFungiDB:YHR042W.
    SGDiS000001084. NCP1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini2 – 7LumenalCurated6
    Transmembranei8 – 24HelicalSequence analysisAdd BLAST17
    Topological domaini25 – 691CytoplasmicCuratedAdd BLAST667

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    Accumulates 20% of ergosterol of wild type.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001676082 – 691NADPH--cytochrome P450 reductaseAdd BLAST690

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki666Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP16603.
    PRIDEiP16603.

    PTM databases

    iPTMnetiP16603.

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Interacts with PCL1.2 Publications

    Protein-protein interaction databases

    BioGridi36474. 61 interactors.
    DIPiDIP-8294N.
    IntActiP16603. 8 interactors.
    MINTiMINT-2782506.

    Structurei

    Secondary structure

    1691
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi50 – 56Combined sources7
    Beta strandi60 – 66Combined sources7
    Beta strandi68 – 70Combined sources3
    Helixi71 – 87Combined sources17
    Beta strandi91 – 95Combined sources5
    Helixi96 – 98Combined sources3
    Helixi104 – 106Combined sources3
    Beta strandi109 – 116Combined sources8
    Beta strandi119 – 121Combined sources3
    Helixi125 – 127Combined sources3
    Helixi128 – 136Combined sources9
    Turni139 – 144Combined sources6
    Beta strandi146 – 153Combined sources8
    Beta strandi157 – 159Combined sources3
    Helixi162 – 173Combined sources12
    Beta strandi183 – 186Combined sources4
    Turni187 – 190Combined sources4
    Helixi192 – 210Combined sources19
    Beta strandi223 – 226Combined sources4
    Beta strandi234 – 239Combined sources6
    Helixi243 – 245Combined sources3
    Beta strandi271 – 278Combined sources8
    Beta strandi287 – 293Combined sources7
    Beta strandi306 – 309Combined sources4
    Helixi315 – 325Combined sources11
    Beta strandi332 – 334Combined sources3
    Beta strandi337 – 339Combined sources3
    Beta strandi348 – 351Combined sources4
    Helixi352 – 358Combined sources7
    Helixi368 – 374Combined sources7
    Helixi375 – 377Combined sources3
    Helixi381 – 390Combined sources10
    Helixi394 – 400Combined sources7
    Helixi402 – 404Combined sources3
    Helixi408 – 416Combined sources9
    Helixi426 – 432Combined sources7
    Beta strandi439 – 443Combined sources5
    Turni447 – 449Combined sources3
    Beta strandi453 – 459Combined sources7
    Beta strandi469 – 471Combined sources3
    Helixi477 – 489Combined sources13
    Turni494 – 496Combined sources3
    Helixi508 – 510Combined sources3
    Turni511 – 515Combined sources5
    Beta strandi519 – 522Combined sources4
    Beta strandi536 – 541Combined sources6
    Helixi542 – 545Combined sources4
    Helixi546 – 560Combined sources15
    Turni564 – 566Combined sources3
    Beta strandi574 – 585Combined sources12
    Turni587 – 591Combined sources5
    Helixi592 – 599Combined sources8
    Helixi600 – 602Combined sources3
    Beta strandi603 – 610Combined sources8
    Helixi620 – 626Combined sources7
    Helixi628 – 635Combined sources8
    Turni636 – 638Combined sources3
    Beta strandi640 – 645Combined sources6
    Helixi650 – 665Combined sources16
    Helixi670 – 682Combined sources13
    Beta strandi685 – 690Combined sources6

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP16603.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini61 – 204Flavodoxin-likeUniRule annotationAdd BLAST144
    Domaini266 – 529FAD-binding FR-typeUniRule annotationAdd BLAST264

    Sequence similaritiesi

    Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation
    In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
    Contains 1 FAD-binding FR-type domain.UniRule annotation
    Contains 1 flavodoxin-like domain.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00840000129757.
    HOGENOMiHOG000282027.
    InParanoidiP16603.
    KOiK00327.
    OMAiTDEDYMA.
    OrthoDBiEOG092C1RRH.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03212. NCPR. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti423T → N in BAA02936 (PubMed:3139648).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti474V → G.1

    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.
    PIRiS46735.
    RefSeqiNP_011908.1. NM_001179172.1.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi36474. 61 interactors.
    DIPiDIP-8294N.
    IntActiP16603. 8 interactors.
    MINTiMINT-2782506.

    PTM databases

    iPTMnetiP16603.

    Proteomic databases

    MaxQBiP16603.
    PRIDEiP16603.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:YHR042W.
    SGDiS000001084. NCP1.

    Phylogenomic databases

    GeneTreeiENSGT00840000129757.
    HOGENOMiHOG000282027.
    InParanoidiP16603.
    KOiK00327.
    OMAiTDEDYMA.
    OrthoDBiEOG092C1RRH.

    Enzyme and pathway databases

    BioCyciYEAST:YHR042W-MONOMER.
    BRENDAi1.6.2.4. 984.
    ReactomeiR-SCE-211897. Cytochrome P450 - arranged by substrate type.

    Miscellaneous databases

    EvolutionaryTraceiP16603.
    PROiP16603.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03212. NCPR. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin-like.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like_dom.
    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]
    ProtoNetiSearch...

    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 30, 2016
    This is version 183 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.