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Protein

NADH-cytochrome b5 reductase 3

Gene

CYB5R3

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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.Curated

Catalytic activityi

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

Cofactori

FAD1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi103 – 118FADBy similarityAdd BLAST16
Nucleotide bindingi142 – 177FADBy similarityAdd BLAST36

GO - Molecular functioni

  • cytochrome-b5 reductase activity, acting on NAD(P)H Source: UniProtKB
  • FAD binding Source: GO_Central
  • flavin adenine dinucleotide binding Source: UniProtKB

GO - Biological processi

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

BRENDAi1.6.2.2. 6170.
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
Proteomesi
  • UP000008227 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49H → A: Similar properties to wild-type. 1 Publication1
Mutagenesisi49H → E: Decreased Kcat values for PB5, ferricyanide and NADH. Increased Km values for all three substrates. 1 Publication1
Mutagenesisi49H → K: Decreased Kcat and Km values for PB5 and ferricyanide. Increased values for NADH. 1 Publication1
Mutagenesisi49H → Y: Similar properties to wild-type. 1 Publication1
Mutagenesisi63R → A or Q: Increased Km values for NADH and increased dissociation constant for NAD(+). 1 Publication1
Mutagenesisi63R → K: Little effect on Km and KD values. 1 Publication1
Mutagenesisi65Y → A or F: Protein destabilized, release of FAD accelerated, and Kcat values decreased. 1 Publication1
Mutagenesisi66T → A: Similar properties to wild-type. 1 Publication1
Mutagenesisi66T → S: Similar properties to wild-type. 1 Publication1
Mutagenesisi66T → V: 10% of wild-type Kcat values. 1 Publication1
Mutagenesisi97K → A: Little effect on absorption or CD spectra. 1 Publication1
Mutagenesisi97K → R: Little effect on absorption or CD spectra. 1 Publication1
Mutagenesisi99S → A or V: Increased Km values for NADH and increased dissociation constant for NAD(+). 1 Publication1
Mutagenesisi99S → T: Little effect on Km and KD values. 1 Publication1
Mutagenesisi272F → FG: 10% of wild-type Kcat values. 1 Publication1
Mutagenesisi272Missing : 54% of wild-type Kcat values. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000167625‹1 – 272NADH-cytochrome b5 reductase 3Add BLAST›272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei14PhosphotyrosineBy similarity1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei91N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

PaxDbiP83686.
PeptideAtlasiP83686.
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

1272
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 25Combined sources12
Beta strandi28 – 34Combined sources7
Beta strandi49 – 56Combined sources8
Beta strandi59 – 65Combined sources7
Beta strandi67 – 69Combined sources3
Beta strandi75 – 82Combined sources8
Turni86 – 88Combined sources3
Beta strandi89 – 91Combined sources3
Helixi97 – 104Combined sources8
Beta strandi110 – 117Combined sources8
Beta strandi119 – 124Combined sources6
Beta strandi127 – 130Combined sources4
Beta strandi132 – 135Combined sources4
Beta strandi139 – 142Combined sources4
Beta strandi144 – 151Combined sources8
Helixi152 – 154Combined sources3
Helixi155 – 166Combined sources12
Beta strandi174 – 183Combined sources10
Helixi184 – 186Combined sources3
Helixi190 – 200Combined sources11
Turni201 – 203Combined sources3
Beta strandi204 – 212Combined sources9
Beta strandi218 – 223Combined sources6
Helixi226 – 232Combined sources7
Helixi236 – 238Combined sources3
Beta strandi241 – 246Combined sources6
Helixi248 – 253Combined sources6
Helixi256 – 262Combined sources7
Helixi266 – 268Combined sources3
Beta strandi269 – 271Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83686.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 123FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP83686.

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

        10         20         30         40         50
STPAITLENP DIKYPLRLID KEVVNHDTRR FRFALPSPEH ILGLPVGQHI
60 70 80 90 100
YLSARIDGNL VIRPYTPVSS DDDKGFVDLV IKVYFKDTHP KFPAGGKMSQ
110 120 130 140 150
YLESMKIGDT IEFRGPNGLL VYQGKGKFAI RPDKKSSPVI KTVKSVGMIA
160 170 180 190 200
GGTGITPMLQ VIRAIMKDPD DHTVCHLLFA NQTEKDILLR PELEELRNEH
210 220 230 240 250
SARFKLWYTV DRAPEAWDYS QGFVNEEMIR DHLPPPEEEP LVLMCGPPPM
260 270
IQYACLPNLE RVGHPKERCF AF
Length:272
Mass (Da):30,831
Last modified:December 15, 2003 - v1
Checksum:i16B08682FC365090
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti39E → Q (PubMed:10082957).Curated1

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000040.

Proteomic databases

PaxDbiP83686.
PeptideAtlasiP83686.
PRIDEiP83686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP83686.

Enzyme and pathway databases

BRENDAi1.6.2.2. 6170.
SABIO-RKP83686.

Miscellaneous databases

EvolutionaryTraceiP83686.

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 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: November 2, 2016
This is version 97 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

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.