Type | Description |
---|---|
Definition | NADH:quinone oxidoreductase subunit F |
Date | Results | Publications |
---|---|---|
2015-05-02 10:42:00 | Data indicate that the NADH:ubiquinone oxidoreductase chain F (NuoF) E95Q variant of Complex I shows that the single amino acid replacement in the catalytic site caused a strong decrease of NADH binding. | 25283488 |
2011-04-30 10:35:00 | Data show that both NuoF mutations E183A and E183G having NADH and NADPH oxidizing ability. | 21205901 |
2011-03-12 10:21:00 | Study determined the distance between a MTSL labeled complex I variant and the bound quinone by continuous-wave (cw) EPR allowing an inference on the location of the quinone binding site. | 20959113 |
2010-01-21 00:00:00 | two distinct Electron Spin Resonance Spectroscopy, arising from a [4Fe-4S] cluster (g(x,y,z)=1.90, 1.95, and 2.05) in NuoF | 15922336 |
2007-11-05 21:38:00 | N-terminus verified by Edman degradation on complete protein | 11416161 |
Type | IDs |
---|---|
Synonymous | ECK2278 |
Gene |
UniProtKB-ID:
NUOF_ECOLI
UniprotKB:
P31979
UniParc:
UPI00001309EC
EMBL:
U00096,
AP009048,
L19569,
X68301,
L25055
EnsemblGenome:
BAA16113,
b2284
KO:
eco:b2284,
ecj:JW2279
|
Nucleutide sequences |
EMBL-CDS:
BAA16113.1,
AAA03537.1,
AAC75344.1,
AAA53584.1,
CAA48365.1
EnsemblGenome_TRS:
AAC75344,
BAA16113
|
Protein sequencees |
EnsemblGenome_PRO:
BAA16113,
AAC75344
RefSeq:
NP_416787.1
|
Others |
UniRef100:
UniRef100_P31979
UniRef90:
UniRef90_P31979
UniRef50:
UniRef50_P31979
|
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