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Protein

NADH-cytochrome b5 reductase 1

Gene

CBR1

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

Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology.1 Publication

Catalytic activityi

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactori

Enzyme regulationi

Competitively inhibited by NAD+. Inhibited by mercurials such as p-chloromercuribenzoate (PCMB) and HgCl2. Enzymatic activity increases under anaerobic conditions.2 Publications

Kineticsi

  1. KM=6.3 µM for NADH1 Publication
  2. KM=0.8 µM for cytochrome b51 Publication

    pH dependencei

    Optimum pH is 5.6. Active from pH 5 to 7.5.1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi122 – 137FADBy similarityAdd BLAST16
    Nucleotide bindingi148 – 180FADBy similarityAdd BLAST33

    GO - Molecular functioni

    • cytochrome-b5 reductase activity, acting on NAD(P)H Source: SGD
    • FAD binding Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciYEAST:YIL043C-MONOMER.
    ReactomeiR-SCE-114608. Platelet degranulation.
    R-SCE-1237044. Erythrocytes take up carbon dioxide and release oxygen.
    R-SCE-196836. Vitamin C (ascorbate) metabolism.
    R-SCE-6798695. Neutrophil degranulation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH-cytochrome b5 reductase 1 (EC:1.6.2.2)
    Alternative name(s):
    Microsomal cytochrome b reductase
    P35
    Gene namesi
    Name:CBR1
    Synonyms:CBR, CBR5
    Ordered Locus Names:YIL043C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IX

    Organism-specific databases

    EuPathDBiFungiDB:YIL043C.
    SGDiS000001305. CBR1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transmembranei7 – 27HelicalSequence analysisAdd BLAST21

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001676271 – 284NADH-cytochrome b5 reductase 1Add BLAST284

    Proteomic databases

    MaxQBiP38626.
    PRIDEiP38626.

    Expressioni

    Inductioni

    Protein levels are highest during exponential growth phase and lowest in stationary phase.1 Publication

    Interactioni

    Subunit structurei

    Monomer. Interacts with STE20.2 Publications

    Protein-protein interaction databases

    BioGridi34947. 56 interactors.
    IntActiP38626. 5 interactors.
    MINTiMINT-1324688.

    Structurei

    3D structure databases

    ProteinModelPortaliP38626.
    SMRiP38626.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini38 – 142FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST105

    Sequence similaritiesi

    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00390000008881.
    HOGENOMiHOG000175005.
    InParanoidiP38626.
    KOiK00326.
    OMAiVYTPNMA.
    OrthoDBiEOG092C43G8.

    Family and domain databases

    InterProiIPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR001834. NADH-Cyt_B5_reductase.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00406. CYTB5RDTASE.
    PR00371. FPNCR.
    SUPFAMiSSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38626-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAIDAQKLVV VIVIVVVPLL FKFIIGPKTK PVLDPKRNDF QSFPLVEKTI
    60 70 80 90 100
    LTHNTSMYKF GLPHADDVLG LPIGQHIVIK ANINGKDITR SYTPTSLDGD
    110 120 130 140 150
    TKGNFELLVK SYPTGNVSKM IGELKIGDSI QIKGPRGNYH YERNCRSHLG
    160 170 180 190 200
    MIAGGTGIAP MYQIMKAIAM DPHDTTKVSL VFGNVHEEDI LLKKELEALV
    210 220 230 240 250
    AMKPSQFKIV YYLDSPDRED WTGGVGYITK DVIKEHLPAA TMDNVQILIC
    260 270 280
    GPPAMVASVR RSTVDLGFRR SKPLSKMEDQ VFVF
    Length:284
    Mass (Da):31,494
    Last modified:April 29, 2008 - v2
    Checksum:i0E71E7AB083BB623
    GO

    Sequence cautioni

    The sequence CAA82214 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence CAA86908 differs from that shown. Reason: Erroneous initiation.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z28365 Genomic DNA. Translation: CAA82214.1. Different initiation.
    Z46861 Genomic DNA. Translation: CAA86908.1. Different initiation.
    BK006942 Genomic DNA. Translation: DAA08505.1.
    PIRiS49935.
    RefSeqiNP_012221.2. NM_001179393.1.

    Genome annotation databases

    EnsemblFungiiYIL043C; YIL043C; YIL043C.
    GeneIDi854768.
    KEGGisce:YIL043C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z28365 Genomic DNA. Translation: CAA82214.1. Different initiation.
    Z46861 Genomic DNA. Translation: CAA86908.1. Different initiation.
    BK006942 Genomic DNA. Translation: DAA08505.1.
    PIRiS49935.
    RefSeqiNP_012221.2. NM_001179393.1.

    3D structure databases

    ProteinModelPortaliP38626.
    SMRiP38626.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi34947. 56 interactors.
    IntActiP38626. 5 interactors.
    MINTiMINT-1324688.

    Proteomic databases

    MaxQBiP38626.
    PRIDEiP38626.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYIL043C; YIL043C; YIL043C.
    GeneIDi854768.
    KEGGisce:YIL043C.

    Organism-specific databases

    EuPathDBiFungiDB:YIL043C.
    SGDiS000001305. CBR1.

    Phylogenomic databases

    GeneTreeiENSGT00390000008881.
    HOGENOMiHOG000175005.
    InParanoidiP38626.
    KOiK00326.
    OMAiVYTPNMA.
    OrthoDBiEOG092C43G8.

    Enzyme and pathway databases

    BioCyciYEAST:YIL043C-MONOMER.
    ReactomeiR-SCE-114608. Platelet degranulation.
    R-SCE-1237044. Erythrocytes take up carbon dioxide and release oxygen.
    R-SCE-196836. Vitamin C (ascorbate) metabolism.
    R-SCE-6798695. Neutrophil degranulation.

    Miscellaneous databases

    PROiP38626.

    Family and domain databases

    InterProiIPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR001834. NADH-Cyt_B5_reductase.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00406. CYTB5RDTASE.
    PR00371. FPNCR.
    SUPFAMiSSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiNCB5R_YEAST
    AccessioniPrimary (citable) accession number: P38626
    Secondary accession number(s): D6VVN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: April 29, 2008
    Last modified: November 30, 2016
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4820 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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