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P83686

- NB5R3_PIG

UniProt

P83686 - NB5R3_PIG

Protein

NADH-cytochrome b5 reductase 3

Gene

CYB5R3

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.Curated

    Catalytic activityi

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

    Cofactori

    FAD.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi103 – 11816FADBy similarityAdd
    BLAST
    Nucleotide bindingi142 – 17736FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: UniProtKB

    GO - Biological processi

    1. cholesterol biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    SABIO-RKP83686.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH-cytochrome b5 reductase 3 (EC:1.6.2.2)
    Short name:
    B5R
    Short name:
    Cytochrome b5 reductase
    Alternative name(s):
    Diaphorase-1
    Gene namesi
    Name:CYB5R3
    Synonyms:DIA1
    OrganismiSus scrofa (Pig)Imported
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Mitochondrion outer membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cytoplasm By similarity
    Note: The enzyme exists in two forms, a membrane-bound form on the cytoplasmic side of the endoplasmic reticulum and also on the mitochondrial outer membrane and in soluble form in erythrocytes. NADH-cytochrome b5 reductase 3 membrane-bound form: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side. NADH-cytochrome b5 reductase 3 soluble form: Cytoplasm.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. mitochondrial outer membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491H → A: Similar properties to wild-type. 1 Publication
    Mutagenesisi49 – 491H → E: Decreased Kcat values for PB5, ferricyanide and NADH. Increased Km values for all three substrates. 1 Publication
    Mutagenesisi49 – 491H → K: Decreased Kcat and Km values for PB5 and ferricyanide. Increased values for NADH. 1 Publication
    Mutagenesisi49 – 491H → Y: Similar properties to wild-type. 1 Publication
    Mutagenesisi63 – 631R → A or Q: Increased Km values for NADH and increased dissociation constant for NAD(+). 1 Publication
    Mutagenesisi63 – 631R → K: Little effect on Km and KD values. 1 Publication
    Mutagenesisi65 – 651Y → A or F: Protein destabilized, release of FAD accelerated, and Kcat values decreased. 1 Publication
    Mutagenesisi66 – 661T → A: Similar properties to wild-type. 1 Publication
    Mutagenesisi66 – 661T → S: Similar properties to wild-type. 1 Publication
    Mutagenesisi66 – 661T → V: 10% of wild-type Kcat values. 1 Publication
    Mutagenesisi97 – 971K → A: Little effect on absorption or CD spectra. 1 Publication
    Mutagenesisi97 – 971K → R: Little effect on absorption or CD spectra. 1 Publication
    Mutagenesisi99 – 991S → A or V: Increased Km values for NADH and increased dissociation constant for NAD(+). 1 Publication
    Mutagenesisi99 – 991S → T: Little effect on Km and KD values. 1 Publication
    Mutagenesisi272 – 2721F → FG: 10% of wild-type Kcat values. 1 Publication
    Mutagenesisi272 – 2721Missing: 54% of wild-type Kcat values. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 272›272NADH-cytochrome b5 reductase 3PRO_0000167625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131N6-acetyllysineBy similarity
    Modified residuei14 – 141PhosphotyrosineBy similarity
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei91 – 911N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP83686.
    PRIDEiP83686.

    Interactioni

    Subunit structurei

    Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2.1 Publication

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000000040.

    Structurei

    Secondary structure

    1
    272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 2512
    Beta strandi28 – 347
    Beta strandi49 – 568
    Beta strandi59 – 657
    Beta strandi67 – 693
    Beta strandi75 – 828
    Turni86 – 883
    Beta strandi89 – 913
    Helixi97 – 1048
    Beta strandi110 – 1178
    Beta strandi119 – 1246
    Beta strandi127 – 1304
    Beta strandi132 – 1354
    Beta strandi139 – 1424
    Beta strandi144 – 1518
    Helixi152 – 1543
    Helixi155 – 16612
    Beta strandi174 – 18310
    Helixi184 – 1863
    Helixi190 – 20011
    Turni201 – 2033
    Beta strandi204 – 2129
    Beta strandi218 – 2236
    Helixi226 – 2327
    Helixi236 – 2383
    Beta strandi241 – 2466
    Helixi248 – 2536
    Helixi256 – 2627
    Helixi266 – 2683
    Beta strandi269 – 2713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NDHX-ray2.10A1-272[»]
    3W2EX-ray2.10A2-272[»]
    3W2FX-ray1.76A2-272[»]
    3W2GX-ray1.68A2-272[»]
    3W2HX-ray1.75A2-272[»]
    3W2IX-ray1.81A2-272[»]
    3W5HX-ray0.78A1-272[»]
    ProteinModelPortaliP83686.
    SMRiP83686. Positions 3-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP83686.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 123113FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0543.
    HOGENOMiHOG000175005.
    HOVERGENiHBG052580.

    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: Fragment.

    P83686-1 [UniParc]FASTAAdd to Basket

    « Hide

    STPAITLENP DIKYPLRLID KEVVNHDTRR FRFALPSPEH ILGLPVGQHI    50
    YLSARIDGNL VIRPYTPVSS DDDKGFVDLV IKVYFKDTHP KFPAGGKMSQ 100
    YLESMKIGDT IEFRGPNGLL VYQGKGKFAI RPDKKSSPVI KTVKSVGMIA 150
    GGTGITPMLQ VIRAIMKDPD DHTVCHLLFA NQTEKDILLR PELEELRNEH 200
    SARFKLWYTV DRAPEAWDYS QGFVNEEMIR DHLPPPEEEP LVLMCGPPPM 250
    IQYACLPNLE RVGHPKERCF AF 272
    Length:272
    Mass (Da):30,831
    Last modified:December 15, 2003 - v1
    Checksum:i16B08682FC365090
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti39 – 391E → Q(PubMed:10082957)Curated

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NDH X-ray 2.10 A 1-272 [» ]
    3W2E X-ray 2.10 A 2-272 [» ]
    3W2F X-ray 1.76 A 2-272 [» ]
    3W2G X-ray 1.68 A 2-272 [» ]
    3W2H X-ray 1.75 A 2-272 [» ]
    3W2I X-ray 1.81 A 2-272 [» ]
    3W5H X-ray 0.78 A 1-272 [» ]
    ProteinModelPortali P83686.
    SMRi P83686. Positions 3-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000000040.

    Proteomic databases

    PaxDbi P83686.
    PRIDEi P83686.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0543.
    HOGENOMi HOG000175005.
    HOVERGENi HBG052580.

    Enzyme and pathway databases

    SABIO-RK P83686.

    Miscellaneous databases

    EvolutionaryTracei P83686.

    Family and domain databases

    InterProi IPR017927. 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 ]
    Pfami PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00406. CYTB5RDTASE.
    PR00371. FPNCR.
    SUPFAMi SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Systematic mutations of highly conserved His49 and carboxyl-terminal of recombinant porcine liver NADH-cytochrome b5 reductase solubilized domain."
      Kimura S., Emi Y., Ikushiro S., Iyanagi T.
      Biochim. Biophys. Acta 1430:290-301(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 1-5, MUTAGENESIS OF HIS-49 AND PHE-272, CIRCULAR DICHROISM ANALYSIS.
      Tissue: Liver1 Publication.
    2. "Terminal sequences of lysosome solubilized pig liver cytochrome b5 reductase."
      Crabb J.W., Tarr G.E., Yasunobu K.T., Iyanagi T., Coon M.J.
      Biochem. Biophys. Res. Commun. 95:1650-1655(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-20.
      Tissue: Liver1 Publication.
    3. "Gastric microsomal NADH-cytochrome b5 reductase: characterization and solubilization."
      Ghesquier D., Robert J.C., Soumarmon A., Abastado M., Grelac F., Lewin M.J.M.
      Comp. Biochem. Physiol. 80B:165-169(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b5 reductase and the other flavin-dependent reductases."
      Nishida H., Inaka K., Miki K.
      FEBS Lett. 361:97-100(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FAD-BINDING.
    5. "Redox properties of microsomal reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5."
      Iyanagi T.
      Biochemistry 16:2725-2730(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: POTENTIOMETRIC TITRATION, EPR SPECTROSCOPY.
    6. "One-electron reduction of hepatic NADH-cytochrome b5 reductase as studied by pulse radiolysis."
      Kobayashi K., Iyanagi T., Ohara H., Hayashi K.
      J. Biol. Chem. 263:7493-7499(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME KINETICS.
    7. "Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis."
      Kimura S., Nishida H., Iyanagi T.
      J. Biochem. 130:481-490(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-63; TYR-65; LYS-97 AND SER-99, CIRCULAR DICHROISM ANALYSIS.
    8. "Role of Thr(66) in porcine NADH-cytochrome b5 reductase in catalysis and control of the rate-limiting step in electron transfer."
      Kimura S., Kawamura M., Iyanagi T.
      J. Biol. Chem. 278:3580-3589(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-66, ENZYME KINETICS, CIRCULAR DICHROISM ANALYSIS.
    9. "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."
      Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.
      J. Biol. Chem. 281:34796-34802(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CYTOCHROME B5 AND MOSC2.
    10. "Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution."
      Nishida H., Inaka K., Yamanaka M., Kaida S., Kobayashi K., Miki K.
      Biochemistry 34:2763-2767(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-273.
    11. "Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner."
      Nishida H., Miki K.
      Proteins 26:32-41(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), 3D-STRUCTURE MODELING OF COMPLEX WITH CYTOCHROME B5.

    Entry informationi

    Entry nameiNB5R3_PIG
    AccessioniPrimary (citable) accession number: P83686
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3