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P83686

- NB5R3_PIG

UniProt

P83686 - NB5R3_PIG

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Protein
NADH-cytochrome b5 reductase 3
Gene
CYB5R3, DIA1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

FAD.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi103 – 11816FAD By similarity
Add
BLAST
Nucleotide bindingi142 – 17736FAD By similarityBy similarity
Add
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
Complete GO annotation...

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)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side By similarity. Mitochondrion outer membrane; Lipid-anchor; 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 By similarity. NADH-cytochrome b5 reductase 3 membrane-bound form: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side By similarity. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side By similarity. 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
Complete GO annotation...

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 3
PRO_0000167625Add
BLAST

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP83686.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 123113FAD-binding FR-type
Add
BLAST

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391E → Q1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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: Liver.
  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: Liver.
  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: July 9, 2014
This is version 85 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

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