Type | Description |
---|---|
Definition | putative acyl-CoA dehydrogenase AidB |
Date | Results | Publications |
---|---|---|
2015-07-04 14:47:00 | AidB exhibits several discrepancies from ACADs that suggest a novel catalytic mechanism distinct from that of the ACAD family enzymes. | 23443126 |
2011-10-15 10:53:00 | AidB was found to bind to RNA, raising the prospect that the protein may have a role in protection of RNA from chemical alkylation. | 21782785 |
2011-01-01 10:42:00 | The N-terminal region, comprising the first 439 amino acids possesses dehydrogenase activity, while its C-terminal domain, corresponding to residues 440 to 541 displays DNA binding activity and can negatively regulate the expression of its own gene. | 20889740 |
2010-01-21 00:00:00 | AidB is shown to possess flavin adenine dinucleotide (FAD), low levels of isovaleryl-coenzyme A (CoA) dehydrogenase activity, and ability to bind DNA, and is predicted to catalyze the direct repair of alkylated DNA | 16352838 |
2010-01-21 00:00:00 | a 1.7-A crystal structure of AidB, which bears superficial resemblance to the acyl-CoA dehydrogenase superfamily of flavoproteins | 18829440 |
Type | IDs |
---|---|
Synonymous | ECK4183 |
Gene |
UniProtKB-ID:
AIDB_ECOLI
UniprotKB:
P33224
UniParc:
UPI0000125733
EMBL:
AP009048,
U14003,
L20915,
U00096
EnsemblGenome:
BAE78188,
b4187
KO:
ecj:JW5867,
eco:b4187
|
Nucleutide sequences |
EMBL-CDS:
BAE78188.1,
AAC77144.2,
AAC18889.1,
AAC18890.1,
AAA97083.1
EnsemblGenome_TRS:
BAE78188,
AAC77144
|
Protein sequencees |
EnsemblGenome_PRO:
AAC77144,
BAE78188
RefSeq:
NP_418608.6
|
Others |
UniRef100:
UniRef100_P33224
UniRef90:
UniRef90_P33224
UniRef50:
UniRef50_P33224
|
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Refseq |
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