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P83686 (NB5R3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-cytochrome b5 reductase 3

Short name=B5R
Short name=Cytochrome b5 reductase
EC=1.6.2.2
Alternative name(s):
Diaphorase-1
Gene names
Name:CYB5R3
Synonyms:DIA1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length272 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

FAD. Ref.4

Subunit structure

Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2. Ref.9

Subcellular location

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.

Sequence similarities

Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 272›272NADH-cytochrome b5 reductase 3
PRO_0000167625

Regions

Domain11 – 123113FAD-binding FR-type
Nucleotide binding103 – 11816FAD By similarity
Nucleotide binding142 – 17736FAD By similarity UniProtKB P07514

Amino acid modifications

Modified residue131N6-acetyllysine By similarity
Modified residue141Phosphotyrosine By similarity
Modified residue211N6-acetyllysine By similarity
Modified residue911N6-acetyllysine By similarity

Experimental info

Mutagenesis491H → A: Similar properties to wild-type. Ref.1
Mutagenesis491H → E: Decreased Kcat values for PB5, ferricyanide and NADH. Increased Km values for all three substrates. Ref.1
Mutagenesis491H → K: Decreased Kcat and Km values for PB5 and ferricyanide. Increased values for NADH. Ref.1
Mutagenesis491H → Y: Similar properties to wild-type. Ref.1
Mutagenesis631R → A or Q: Increased Km values for NADH and increased dissociation constant for NAD(+). Ref.7
Mutagenesis631R → K: Little effect on Km and KD values. Ref.7
Mutagenesis651Y → A or F: Protein destabilized, release of FAD accelerated, and Kcat values decreased. Ref.7
Mutagenesis661T → A: Similar properties to wild-type. Ref.8
Mutagenesis661T → S: Similar properties to wild-type. Ref.8
Mutagenesis661T → V: 10% of wild-type Kcat values. Ref.8
Mutagenesis971K → A: Little effect on absorption or CD spectra. Ref.7
Mutagenesis971K → R: Little effect on absorption or CD spectra. Ref.7
Mutagenesis991S → A or V: Increased Km values for NADH and increased dissociation constant for NAD(+). Ref.7
Mutagenesis991S → T: Little effect on Km and KD values. Ref.7
Mutagenesis2721F → FG: 10% of wild-type Kcat values. Ref.1
Mutagenesis2721Missing: 54% of wild-type Kcat values. Ref.1
Sequence conflict391E → Q Ref.1
Non-terminal residue11

Secondary structure

...................................................... 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P83686 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 16B08682FC365090

FASTA27230,831
        10         20         30         40         50         60 
STPAITLENP DIKYPLRLID KEVVNHDTRR FRFALPSPEH ILGLPVGQHI YLSARIDGNL 

        70         80         90        100        110        120 
VIRPYTPVSS DDDKGFVDLV IKVYFKDTHP KFPAGGKMSQ YLESMKIGDT IEFRGPNGLL 

       130        140        150        160        170        180 
VYQGKGKFAI RPDKKSSPVI KTVKSVGMIA GGTGITPMLQ VIRAIMKDPD DHTVCHLLFA 

       190        200        210        220        230        240 
NQTEKDILLR PELEELRNEH SARFKLWYTV DRAPEAWDYS QGFVNEEMIR DHLPPPEEEP 

       250        260        270 
LVLMCGPPPM IQYACLPNLE RVGHPKERCF AF 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP83686.
SMRP83686. Positions 3-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000000040.

Proteomic databases

PaxDbP83686.
PRIDEP83686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0543.
HOGENOMHOG000175005.
HOVERGENHBG052580.

Enzyme and pathway databases

SABIO-RKP83686.

Family and domain databases

InterProIPR017927. 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]
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP83686.

Entry information

Entry nameNB5R3_PIG
AccessionPrimary (citable) accession number: P83686
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references