A0A5B9AQS0 · A0A5B9AQS0_ECOLX
- ProteinDiacylglycerol kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids121 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis.
Catalytic activity
- a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H+
Cofactor
Note: Mn2+, Zn2+, Cd2+ and Co2+ support activity to lesser extents.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 10 | ATP (UniProtKB | ChEBI) | |||
Binding site | 10 | substrate | |||
Binding site | 17 | ATP (UniProtKB | ChEBI) | |||
Binding site | 23-26 | substrate | |||
Binding site | 29 | ATP (UniProtKB | ChEBI) | |||
Binding site | 29 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 31-35 | substrate | |||
Binding site | 48-51 | substrate | |||
Binding site | 56 | substrate | |||
Active site | 70 | Proton acceptor | |||
Binding site | 70 | substrate | |||
Binding site | 77 | ATP (UniProtKB | ChEBI) | |||
Binding site | 77 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 86-88 | ATP (UniProtKB | ChEBI) | |||
Binding site | 95-96 | ATP (UniProtKB | ChEBI) | |||
Binding site | 99 | substrate | |||
Binding site | 113-118 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent diacylglycerol kinase activity | |
Molecular Function | metal ion binding | |
Biological Process | phosphatidic acid biosynthetic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDiacylglycerol kinase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A5B9AQS0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 30-51 | Helical | |||
Transmembrane | 97-118 | Helical | |||
Keywords
- Cellular component
Structure
Sequence
- Sequence statusComplete
- Length121
- Mass (Da)13,124
- Last updated2019-11-13 v1
- MD5 ChecksumD439F519DF09E48DA94A3CC516BCA2FC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP042615 EMBL· GenBank· DDBJ | QED74908.1 EMBL· GenBank· DDBJ | Genomic DNA |