Type | Description |
---|---|
Definition | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase |
Date | Results | Publications |
---|---|---|
2019-06-08 11:48:00 | The non-native-binding site of the inactive 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) intermediate suggests a target for the development of antibiotics. | 30341164 |
2015-07-25 12:05:00 | MenD possesses a characteristic substrate range with respect to Michael acceptor substrates which is distinctly different from the classical stetterases. | 25111035 |
2011-12-17 11:40:00 | The active-Site of MenD are Arg33, Arg107, Lys292, Arg293, Arg395, and Arg413. | 21928762 |
2010-01-21 00:00:00 | the crystal structures of the Vitamin K(2) synthesis protein MenD were described. | 19703421 |
2010-01-21 00:00:00 | the crystal structure of apo MenD with supporting biological assay that reveals its affinity towards ThDP, FAD and oxoglutarate, providing further insight into its function and role as a bifunctional enzyme. | 19338755 |
Type | IDs |
---|---|
Synonymous | ECK2258 |
Gene |
UniProtKB-ID:
MEND_ECOLI
UniprotKB:
P17109
UniParc:
UPI000012EEF1
EMBL:
M21787,
U00096,
L04464,
U54790,
AP009048,
L35030
EnsemblGenome:
BAA16089,
b2264
KO:
ecj:JW5374,
eco:b2264
|
Nucleutide sequences |
EMBL-CDS:
AAA24153.1,
AAB59060.1,
BAA16089.2,
AAC44304.1,
AAA24150.1,
AAC75324.1
EnsemblGenome_TRS:
BAA16089,
AAC75324
|
Protein sequencees |
EnsemblGenome_PRO:
AAC75324,
BAA16089
RefSeq:
NP_416767.1
|
Others |
UniRef100:
UniRef100_C4ZUA7
UniRef90:
UniRef90_Q8XDX8
UniRef50:
UniRef50_Q8XDX8
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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