A0A2D2M3S1 · A0A2D2M3S1_9PSED
- ProteinDiacylglycerol kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids120 (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 | 12 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 12 | substrate | ||||
Sequence: R | ||||||
Binding site | 19 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 31 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 31 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 50-53 | substrate | ||||
Sequence: WLQV | ||||||
Binding site | 58 | substrate | ||||
Sequence: R | ||||||
Active site | 72 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 72 | substrate | ||||
Sequence: E | ||||||
Binding site | 79 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 79 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 88-90 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ERH | ||||||
Binding site | 97-98 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KD | ||||||
Binding site | 101 | substrate | ||||
Sequence: S |
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 > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A2D2M3S1
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 | 33-53 | Helical | ||||
Sequence: AFRQLVLLNVVLIPLAFWLQV | ||||||
Transmembrane | 59-78 | Helical | ||||
Sequence: AILIAVCLLGLIVELLNSAV | ||||||
Transmembrane | 99-118 | Helical | ||||
Sequence: MGSAAQLVALSMVGLVWAVI |
Keywords
- Cellular component
Structure
Sequence
- Sequence statusComplete
- Length120
- Mass (Da)12,934
- Last updated2018-01-31 v1
- Checksum16D04063A7D4B467
Keywords
- Technical term