LipidDB ID

LipidDB-9606-00195

Entry Name

UniProt Accession

P00387; B1AHF2; B7Z7L3; O75675; Q8TDL8; Q8WTS8; Q9UEN4; Q9UEN5; Q9UL55; Q9UL56;

Theoretical PI

7.18

Molecular Weight

34234.86

Genbank Protein ID

AAA59900.1; AAA59900.1; AAA59900.1; AAA59900.1; AAA59900.1; AAA59900.1; AAA59900.1; AAA59900.1; CAA70696.1; AAL87744.1; CAA09006.1; CAA09007.1; CAA09008.1; AAP88936.1; AAP88823.1; CAG30321.1; AAF06818.1; AAF06819.1; BAH13649.1; CAB42843.1; CAQ08414.1; AAH04821.1; CAC84523.1; CAC84524.1; AAA52306.1; AAA52307.1;

Genbank Nucleotide ID

M28713; M28705; M28706; M28707; M28708; M28709; M28710; M28711; Y09501; AF361370; AJ010116; AJ010117; AJ010118; AY341030; BT009821; CR456435; AF061830; AF061831; AK302204; Z93241; Z93241; BC004821; AJ310899; AJ310900; M16461; M16462;

Protein Name

NADH-cytochrome b5 reductase 3 soluble form

Protein Synonyms/Alias

B5R; Cytochrome b5 reductase; 1.6.2.2; Diaphorase-1;

Gene Name

CYB5R3

Gene Synonyms/Alias

DIA1;

Created Date

21-JUL-1986

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Murakami K, Yubisui T, Takeshita M, Miyata T. The NH2-terminal structures ofhuman and rat liver microsomal NADH-cytochrome b5 reductases. J Biochem. 1989Feb;105(2):312-7.[PMID:2498303]
[2] Strittmatter P, Kittler JM, Coghill JE, Ozols J. Interaction ofnon-myristoylated NADH-cytochrome b5 reductase with cytochromeb5-dimyristoylphosphatidylcholine vesicles. J Biol Chem. 1993 Nov5;268(31):23168-71.[PMID:8226835]

Functional Description

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

Sequence Annotation

Domain: 40 152 FAD-binding FR-type.
Nucleotide-binding: 132 147 FAD.
Nucleotide-binding: 171 206 FAD.
Modified residue: 42 42 N6-acetyllysine.
Modified residue: 43 43 Phosphotyrosine.
Modified residue: 120 120 N6-acetyllysine.

Protein Length

301 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0005783; C:endoplasmic reticulum; IDA:HPA
GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005833; C:hemoglobin complex; TAS:ProtInc
GO:0005811; C:lipid particle; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl
GO:0005741; C:mitochondrial outer membrane; TAS:Reactome
GO:0005739; C:mitochondrion; IDA:UniProt
GO:0043531; F:ADP binding; IEA:Ensembl
GO:0016208; F:AMP binding; IEA:Ensembl
GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:Reactome
GO:0071949; F:FAD binding; IDA:UniProtKB
GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl
GO:0051287; F:NAD binding; IEA:Ensembl
GO:0008015; P:blood circulation; TAS:ProtInc
GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW
GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0006766; P:vitamin metabolic process; TAS:Reactome
GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome

Interpro

InterPro; IPR017927; Fd_Rdtase_FAD-bd
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase
InterPro; IPR001834; NADH-Cyt_B5_reductase
InterPro; IPR008333; OxRdtase_FAD-bd_dom
InterPro; IPR001433; OxRdtase_FAD/NAD-bd
InterPro; IPR017938; Riboflavin_synthase-like_b-brl

Pfam

Pfam; PF00970; FAD_binding_6;
Pfam; PF00175; NAD_binding_1;

SMART

PROSITE

PROSITE; PS51384; FAD_FR;

PRINTS

PRINTS; PR00406; CYTB5RDTASE;
PRINTS; PR00371; FPNCR;