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Sequence of NB5R3_RAT

EC Number:1.6.2.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
cytochrome-b5 reductase
P20070
Rattus norvegicus
301
34175
Reaction
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
Other sequences found for EC No. 1.6.2.2

General information:

Sequence
show sequence in fasta format
  0 MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK EIISHDTRRF
 60 RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK
120 FPAGGKMSQY LENMNIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG
180 GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD
240 KAPDAWDYSQ GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT
300 F
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
193798
Zenno S.,Hattori M.,Misumi Y.,Yubisui T.,Sakaki Y.
Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase and the corresponding gene.
J. Biochem.
107
810-816
1990
193799
Pietrini G.,Carrera P.,Borgese N.
Two transcripts encode rat cytochrome b5 reductase.
Proc. Natl. Acad. Sci. U.S.A.
85
7246-7250
1988
193800
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
193801
Pietrini G.,Aggujaro D.,Carrera P.,Malyszko J.,Vitale A.,Borgese N.
A single mRNA, transcribed from an alternative, erythroid-specific, promoter, codes for two non-myristylated forms of NADH-cytochrome b5 reductase.
J. Cell Biol.
117
975-986
1992
193802
Murakami K.,Yubisui T.,Takeshita M.,Miyata T.
The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases.
J. Biochem.
105
312-317
1989
193803
Mota Vieira L.,Kaplan J.-C.,Kahn A.,Leroux A.
Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts resulting from multiple alternative first exons.
Eur. J. Biochem.
220
729-737
1994
193804
Borgese N.,Aggujaro D.,Carrera P.,Pietrini G.,Bassetti M.
A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes.
J. Cell Biol.
135
1501-1513
1996
193805
Barber M.J.,Quinn G.B.
High-level expression in Escherichia coli of the soluble, catalytic domain of rat hepatic cytochrome b5 reductase.
Protein Expr. Purif.
8
41-47
1996
193806
Bewley M.C.,Marohnic C.C.,Barber M.J.
The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent.
Biochemistry
40
13574-13582
2001