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Protein

NADH--cytochrome b5 reductase 1

Gene

CBR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reductase transferring electrons from NADH to cytochrome b5. Required for the NADH-dependent electron transfer involved in the desaturation and hydroxylation of fatty acids and in the desaturation of sterol precursors. No activity with NADPH as electron donor.2 Publications

Catalytic activityi

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

Cofactori

FADBy similarity

Kineticsi

  1. KM=1.5 µM for NADH1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi129 – 14416FADBy similarityAdd
    BLAST
    Nucleotide bindingi155 – 18733FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    • cytochrome-b5 reductase activity, acting on NAD(P)H Source: TAIR
    • FAD binding Source: GO_Central

    GO - Biological processi

    • electron transport chain Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciARA:AT5G17770-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH--cytochrome b5 reductase 1 (EC:1.6.2.2)
    Gene namesi
    Name:CBR1
    Synonyms:CBR
    Ordered Locus Names:At5g17770
    ORF Names:MVA3.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G17770.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum Source: TAIR
    • integral component of membrane Source: UniProtKB-KW
    • mitochondrial outer membrane Source: UniProtKB-SubCell
    • plant-type cell wall Source: TAIR
    • plasma membrane Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781L → F in cbr1-1; decreased stability and decreased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281NADH--cytochrome b5 reductase 1PRO_0000419622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei166 – 1661PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9ZNT1.
    PRIDEiQ9ZNT1.

    Expressioni

    Tissue specificityi

    Expressed in roots, stems, flowers and siliques. Detected in leaves.1 Publication

    Gene expression databases

    GenevisibleiQ9ZNT1. AT.

    Interactioni

    Subunit structurei

    Monomer. Interacts with AKR2A (PubMed:20215589).By similarity1 Publication

    Protein-protein interaction databases

    BioGridi16921. 2 interactions.
    STRINGi3702.AT5G17770.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZNT1.
    SMRiQ9ZNT1. Positions 37-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 149105FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi34 – 407AKR2A-binding sequence (ABS) required for mitochondrion outer membrane targeting1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG0534. Eukaryota.
    COG0543. LUCA.
    HOGENOMiHOG000175005.
    InParanoidiQ9ZNT1.
    KOiK00326.
    OMAiTHNTAIY.
    PhylomeDBiQ9ZNT1.

    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.

    Q9ZNT1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDTEFLRTLD RQILLGVFVA FVAVGAGAAY FLTSSKKRRV CLDPENFKEF
    60 70 80 90 100
    KLVKRHQLSH NVAKFVFELP TSTSVLGLPI GQHISCRGKD GQGEDVIKPY
    110 120 130 140 150
    TPTTLDSDVG RFELVIKMYP QGRMSHHFRE MRVGDHLAVK GPKGRFKYQP
    160 170 180 190 200
    GQFRAFGMLA GGSGITPMFQ VARAILENPT DKTKVHLIYA NVTYDDILLK
    210 220 230 240 250
    EELEGLTTNY PEQFKIFYVL NQPPEVWDGG VGFVSKEMIQ THCPAPASDI
    260 270 280
    QILRCGPPPM NKAMAANLEA LGYSPEMQFQ F
    Length:281
    Mass (Da):31,490
    Last modified:May 1, 1999 - v1
    Checksum:iE6654D95FEA2BCD2
    GO

    Sequence cautioni

    The sequence AAL24304.1 differs from that shown. Reason: Frameshift at position 39. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB007799 mRNA. Translation: BAA74837.1.
    AB007800 Genomic DNA. Translation: BAA74838.1.
    AB006706 Genomic DNA. Translation: BAB09576.1.
    CP002688 Genomic DNA. Translation: AED92466.1.
    AY059822 mRNA. Translation: AAL24304.1. Frameshift.
    AY072482 mRNA. Translation: AAL66897.1.
    AK316787 mRNA. Translation: BAH19505.1.
    AY085728 mRNA. Translation: AAM62946.1.
    PIRiT52470.
    RefSeqiNP_197279.1. NM_121783.4.
    UniGeneiAt.43640.

    Genome annotation databases

    EnsemblPlantsiAT5G17770.1; AT5G17770.1; AT5G17770.
    GeneIDi831645.
    GrameneiAT5G17770.1; AT5G17770.1; AT5G17770.
    KEGGiath:AT5G17770.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB007799 mRNA. Translation: BAA74837.1.
    AB007800 Genomic DNA. Translation: BAA74838.1.
    AB006706 Genomic DNA. Translation: BAB09576.1.
    CP002688 Genomic DNA. Translation: AED92466.1.
    AY059822 mRNA. Translation: AAL24304.1. Frameshift.
    AY072482 mRNA. Translation: AAL66897.1.
    AK316787 mRNA. Translation: BAH19505.1.
    AY085728 mRNA. Translation: AAM62946.1.
    PIRiT52470.
    RefSeqiNP_197279.1. NM_121783.4.
    UniGeneiAt.43640.

    3D structure databases

    ProteinModelPortaliQ9ZNT1.
    SMRiQ9ZNT1. Positions 37-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi16921. 2 interactions.
    STRINGi3702.AT5G17770.1.

    Proteomic databases

    PaxDbiQ9ZNT1.
    PRIDEiQ9ZNT1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G17770.1; AT5G17770.1; AT5G17770.
    GeneIDi831645.
    GrameneiAT5G17770.1; AT5G17770.1; AT5G17770.
    KEGGiath:AT5G17770.

    Organism-specific databases

    TAIRiAT5G17770.

    Phylogenomic databases

    eggNOGiKOG0534. Eukaryota.
    COG0543. LUCA.
    HOGENOMiHOG000175005.
    InParanoidiQ9ZNT1.
    KOiK00326.
    OMAiTHNTAIY.
    PhylomeDBiQ9ZNT1.

    Enzyme and pathway databases

    BioCyciARA:AT5G17770-MONOMER.

    Miscellaneous databases

    PROiQ9ZNT1.

    Gene expression databases

    GenevisibleiQ9ZNT1. AT.

    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis."
      Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.
      Plant Physiol. 119:353-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
      Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
      Tissue: Rosette leaf.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "A mutation in Arabidopsis cytochrome b5 reductase identified by high-throughput screening differentially affects hydroxylation and desaturation."
      Kumar R., Wallis J.G., Skidmore C., Browse J.
      Plant J. 48:920-932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LEU-78, NOMENCLATURE.
    8. "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis."
      Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.
      Plant Cell 22:811-831(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKR2A.
      Strain: cv. C24 and cv. Columbia.
    9. "Is AKR2A an essential molecular chaperone for a class of membrane-bound proteins in plants?"
      Zhang H., Li X., Zhang Y., Kuppu S., Shen G.
      Plant Signal. Behav. 5:1520-1522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: AKR2A-BINDING SEQUENCE, REVIEW.
    10. "Multiple lines of evidence localize signaling, morphology, and lipid biosynthesis machinery to the mitochondrial outer membrane of Arabidopsis."
      Duncan O., Taylor N.L., Carrie C., Eubel H., Kubiszewski-Jakubiak S., Zhang B., Narsai R., Millar A.H., Whelan J.
      Plant Physiol. 157:1093-1113(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiNB5R1_ARATH
    AccessioniPrimary (citable) accession number: Q9ZNT1
    Secondary accession number(s): Q93YQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: May 1, 1999
    Last modified: July 6, 2016
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    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.