| Type | Description |
|---|---|
| Definition | glutamine-dependent NAD(+) synthetase |
| Date | Results | Publications |
|---|---|---|
| 2020-04-25 11:34:00 | Homo sapiens NAD(+) synthetase (hsNadE) lacks substrate specificity for glutamine over ammonia and displays a modest activation of the glutaminase domain compared to tbNadE. | 31911602 |
| 2012-05-19 11:43:00 | results provide new insight into the regulation of ammonia transport in the intermolecular tunnel of NadE | 22280445 |
| 2010-01-21 00:00:00 | The structure, the first of a glutamine-dependent NAD(+) synthetase, reveals a homooctameric subunit organization suggesting a tight dependence of catalysis on the quaternary structure. | 19270703 |
| 2010-01-21 00:00:00 | glutamine-amidotransferase activity is mediated by an N-terminal domain belonging to the superfamily of nitrilases | 15748981 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
NADE_MYCTU
UniprotKB:
P9WJJ3
UniParc:
UPI000012FCD6
EMBL:
AL123456
EnsemblGenome:
Rv2438c
KO:
mtv:RVBD_2438c,
mtu:Rv2438c
|
| Nucleutide sequences |
EMBL-CDS:
CCP45230.1
Gene_ORFName:
MTCY428.08
EnsemblGenome_TRS:
CCP45230
|
| Protein sequencees |
EnsemblGenome_PRO:
CCP45230
|
| Others |
UniRef100:
UniRef100_P0A5L7
UniRef90:
UniRef90_P0A5L7
UniRef50:
UniRef50_P0A5L7
|
| {{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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