A0A367EM82 · A0A367EM82_9ACTN

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Contains a di-nuclear catalytic Mg2+ center.

Pathway

Lipid metabolism.
Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site29-32a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI)
Binding site66Mg2+ 1 (UniProtKB | ChEBI)
Binding site66Mg2+ 2 (UniProtKB | ChEBI)
Binding site69Mg2+ 1 (UniProtKB | ChEBI)
Binding site70a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI)
Binding site74a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI)
Binding site80a CDP-1,2-diacyl-sn-glycerol (UniProtKB | ChEBI)
Binding site87Mg2+ 1 (UniProtKB | ChEBI)
Binding site87Mg2+ 2 (UniProtKB | ChEBI)
Active site91Proton acceptor
Binding site91Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionmagnesium ion binding
Molecular Functionphosphotransferase activity, for other substituted phosphate groups
Biological Processphospholipid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphatidylinositol phosphate synthase
  • EC number
  • Short names
    PIP synthase
  • Alternative names
    • CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase

Gene names

    • ORF names
      DQ392_12775

Organism names

  • Taxonomic identifier
  • Strain
    • LHW50302
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A367EM82

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane52-68Helical
Transmembrane176-195Helical

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region209-250Disordered
Compositional bias218-237Polar residues

Sequence similarities

Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    250
  • Mass (Da)
    26,341
  • Last updated
    2018-11-07 v1
  • Checksum
    5E95CD888663544E
MLNKYARAFFTRVLTPFATLLLRLGVSPDVVTLIGTCGVTAGALVFYPMGEFFWGTVVITLFVFSDMLDGNMARQLGRSSRWGAFLDSTLDRVADAAVFGGIALWYAGRGDDLTLCAVTLFCLASGQVVSYTKARGESIGLPVDVNGLVERSERLVITLVLAGFSGFEKSFGVPHIAILLPIALWVVAVGSAITLGQRVVTVRREAAEVDAAENHDAPSSPDASSASGTSSAPDASSASAAGDEEKRRTV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias218-237Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QOIM01000032
EMBL· GenBank· DDBJ
RCG18792.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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