| Type | Description |
|---|---|
| Definition | D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase |
| Date | Results | Publications |
|---|---|---|
| 2010-04-19 12:01:00 | E. coli GmhB is characterized as a D-dlycero-D-manno-heptose-1,7-bisphosphate (HAD) phosphatase with a narrow substrate range and a high catalytic efficiency toward its physiological substrate. | 20050615 |
| 2010-04-19 12:01:00 | GmhB and the histidinol-phosphate phosphatase domain use the same design of three substrate recognition loops inserted into the cap domain yet have achieved unique substrate specificity and thus novel biochemical function. | 20050614 |
| 2010-03-15 11:42:00 | GmhB functions through a phosphoaspartate intermediate catalyzing the third essential step of lipopolysaccharide/heptose biosynthesis. | 20050699 |
| Type | IDs |
|---|---|
| Synonymous | ECK0200, yaeD |
| Gene |
UniProtKB-ID:
GMHBB_ECOLI
UniprotKB:
P63228
UniParc:
UPI000013A05D
EMBL:
AP009048,
U70214,
U00096,
D15061
EnsemblGenome:
BAA77877,
b0200
KO:
ecj:JW0196,
eco:b0200
|
| Nucleutide sequences |
EMBL-CDS:
BAA03661.1,
AAC73311.1,
AAB08628.1,
BAA77877.1
EnsemblGenome_TRS:
AAC73311,
BAA77877
|
| Protein sequencees |
EnsemblGenome_PRO:
BAA77877,
AAC73311
RefSeq:
NP_414742.1
|
| Others |
UniRef100:
UniRef100_P63229
UniRef90:
UniRef90_Q8ZRM8
UniRef50:
UniRef50_Q8Z989
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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