LMPD Database

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LMP007028

UniProt Annotations

Entry Information
Gene NameNcp1p
Protein EntryNCPR_YEAST
UniProt IDP16603
SpeciesYeast (S288c)
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic 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.;
Catalytic ActivityNADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein. {ECO:0000269|PubMed:11485306, ECO:0000269|PubMed:9368374, ECO:0000269|PubMed:9468503}.
CofactorName=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:9468503}; Note=Binds 1 FAD per monomer. {ECO:0000269|PubMed:9468503};
CofactorName=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:9468503}; Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:9468503};
Disruption PhenotypeAccumulates 20% of ergosterol of wild type. {ECO:0000269|PubMed:9468503}.
FunctionThis 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:0000269|PubMed:11485306, ECO:0000269|PubMed:1730736, ECO:0000269|PubMed:9368374, ECO:0000269|PubMed:9468503}.
InductionBy galactose and on the plasma membrane by iron or copper deficiency. Repressed by glucose. {ECO:0000269|PubMed:9368374}.
MiscellaneousPresent with 46600 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
PtmPhosphorylated by the cyclin-CDK PCL1-PHO85. {ECO:0000269|PubMed:15082539}.
SimilarityContains 1 FAD-binding FR-type domain. {ECO:0000255|PROSITE-ProRule:PRU00716}.
SimilarityContains 1 flavodoxin-like domain. {ECO:0000255|PROSITE-ProRule:PRU00088}.
SimilarityIn the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. {ECO:0000305}.
Subcellular LocationEndoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein. Cell membrane; Single-pass membrane protein. Microsome.
SubunitInteracts with PCL1. {ECO:0000269|PubMed:15082539, ECO:0000269|PubMed:16407065}.