| Type | Description |
|---|---|
| Definition | acetyl-CoA C-acetyltransferase |
| Date | Results | Publications |
|---|---|---|
| 2019-02-02 11:27:00 | Crystal structures of apo ERG10 and its Cys91Ala variant were solved at resolutions of 2.2 and 1.95 A, respectively. ERG10 shares the characteristic thiolase superfamily fold, with a similar active-site architecture to those of type II thiolases and a similar binding pocket, apart from Ala159 at the entrance to the pantetheine-binding cavity, which appears to be a determinant of the poor binding ability of the substrate. | 29372902 |
| 2018-05-26 11:53:00 | Erg10 thiolase from Saccharomyces cerevisiae showed no acetyl-CoA/butyryl-CoA branched condensation activity, but variants at position F293 resulted the most active and selective biocatalysts for this reaction. | 29360348 |
| Type | IDs |
|---|---|
| Synonymous | LPB3, TSM0115 |
| Gene |
UniProtKB-ID:
THIL_YEAST
UniprotKB:
P41338
UniParc:
UPI0000136E4F
EMBL:
L20428,
BK006949,
U36624
EnsemblGenome:
YPL028W
KO:
sce:YPL028W
|
| Nucleutide sequences |
EMBL-CDS:
AAA62378.1,
AAB68159.1,
DAA11401.1
Gene_ORFName:
LPB3
EnsemblGenome_TRS:
YPL028W_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YPL028W
RefSeq:
NP_015297.1
|
| Others |
UniRef100:
UniRef100_P41338
UniRef90:
UniRef90_P41338
UniRef50:
UniRef50_P41338
|
| {{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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