| Type | Description |
|---|---|
| Definition | cyclopropane fatty acyl phospholipid synthase |
| Date | Results | Publications |
|---|---|---|
| 2011-02-26 11:10:00 | both chemical steps of this enzymatic cyclopropanation, the methyl addition onto the double bond and the deprotonation step, are rate determining, a common situation in efficient enzymes. | 20538038 |
| 2010-01-21 00:00:00 | Experiments are described that distinguish between two mechanistic scenarios for the cyclopropanation of unactivated olefins by cyclopropane fatty acid synthase. | 15491158 |
| 2010-01-21 00:00:00 | report mutagenetic and chemical rescue experiments that confirm an important role for bicarbonate in E. coli CFAS catalysis; propose that residue E239, one of the bicarbonate ligands, could form a catalytic dyad with this ion | 16216082 |
| 2007-11-05 21:38:00 | N-terminus verified by Edman degradation on mature peptide | 1445840 |
| Type | IDs |
|---|---|
| Synonymous | ECK1657, cdfA |
| Gene |
UniProtKB-ID:
CFA_ECOLI
UniprotKB:
P0A9H7
UniParc:
UPI0000167DB0
EMBL:
X69109,
AP009048,
M98330,
U00096
EnsemblGenome:
BAA15428,
b1661
KO:
eco:b1661,
ecj:JW1653
|
| Nucleutide sequences |
EMBL-CDS:
AAC74733.1,
AAA23562.1,
BAA15428.1
EnsemblGenome_TRS:
AAC74733,
BAA15428
|
| Protein sequencees |
EnsemblGenome_PRO:
BAA15428,
AAC74733
RefSeq:
NP_416178.1
|
| Others |
UniRef100:
UniRef100_P0A9H8
UniRef90:
UniRef90_P0A9H8
UniRef50:
UniRef50_P0A9H8
|
| {{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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