A0A367EM82 · A0A367EM82_9ACTN
- ProteinPhosphatidylinositol phosphate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids250 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid required for cell wall formation.
Catalytic activity
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + 1D-myo-inositol 3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H+
- 1D-myo-inositol 3-phosphate + a CDP-1,2-diacyl-sn-glycerol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H+
Cofactor
Note: Contains a di-nuclear catalytic Mg2+ center.
Pathway
Lipid metabolism.
Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 29-32 | a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI) | ||||
Sequence: DVVT | ||||||
Binding site | 66 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 69 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 70 | a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 74 | a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 80 | a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 87 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 87 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 91 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 91 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphotransferase activity, for other substituted phosphate groups | |
Biological Process | phospholipid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol phosphate synthase
- EC number
- Short namesPIP synthase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A367EM82
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 52-68 | Helical | ||||
Sequence: FFWGTVVITLFVFSDML | ||||||
Transmembrane | 176-195 | Helical | ||||
Sequence: IAILLPIALWVVAVGSAITL |
Keywords
- Cellular component
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 209-250 | Disordered | ||||
Sequence: VDAAENHDAPSSPDASSASGTSSAPDASSASAAGDEEKRRTV | ||||||
Compositional bias | 218-237 | Polar residues | ||||
Sequence: PSSPDASSASGTSSAPDASS |
Sequence similarities
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length250
- Mass (Da)26,341
- Last updated2018-11-07 v1
- Checksum5E95CD888663544E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 218-237 | Polar residues | ||||
Sequence: PSSPDASSASGTSSAPDASS |