Type | Description |
---|---|
Definition | adenylosuccinate lyase |
Date | Results | Publications |
---|---|---|
2010-01-21 00:00:00 | Kinetic data reveal that human Ser(289) and B. subtilis Ser(262) and Ser(263) are essential for catalysis, while the ability of these Ser mutants to bind APBADP suggests that they do not contribute to substrate affinity | 18469177 |
2010-01-21 00:00:00 | Data conclude that both hydrophobic and electrostatic interactions play roles in maintaining the adenylosuccinate lyase tetramer and this structure is essential for adenylosuccinate lyase activity. | 18237141 |
Type | IDs |
---|---|
Synonymous | BSU06440 |
Gene |
UniProtKB-ID:
PUR8_BACSU,
A0A6M3ZBB6_BACSU
UniprotKB:
P12047,
A0A6M3ZBB6
UniParc:
UPI000006001E
EMBL:
CP053102,
AL009126,
CP052842,
J02732
EnsemblGenome:
BSU06440
KO:
bsu:BSU06440
|
Nucleutide sequences |
EMBL-CDS:
AAA22676.1,
CAB12464.1,
QJR45103.1,
QJP87180.1
Gene_ORFName:
HIR78_03685,
HIR77_03665
EnsemblGenome_TRS:
CAB12464
|
Protein sequencees |
EnsemblGenome_PRO:
CAB12464
RefSeq:
NP_388526.1
|
Others |
UniRef100:
UniRef100_P12047
UniRef90:
UniRef90_P12047
UniRef50:
UniRef50_P12047
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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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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