AC MF_02242; DC Protein; auto TR HAMAP; MF_02242; -; 1; level=0 XX Names: AIP_synthase XX ID AIPS DE RecName: Full=Archaetidylinositol phosphate synthase; DE Short=AIP synthase; DE EC=2.7.8.39; XX CC -!- FUNCTION: Catalyzes the formation of archaetidylinositol phosphate CC (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn- CC glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3- CC phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an CC ether-type inositol phospholipid ubiquitously distributed in archaea CC membranes and essential for glycolipid biosynthesis in archaea. CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn- CC glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3- CC phosphate; Xref=Rhea:RHEA:36823, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58401, ChEBI:CHEBI:60377, ChEBI:CHEBI:74004, CC ChEBI:CHEBI:74006; EC=2.7.8.39; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit.; CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I CC family. XX DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1; trigger=no DR Pfam; PF01066; CDP-OH_P_transf; 1; trigger=no DR General; Transmembrane; -; 4-5; trigger=yes XX KW Cell membrane KW Lipid biosynthesis KW Lipid metabolism KW Magnesium KW Manganese KW Membrane KW Metal-binding KW Phospholipid metabolism KW Transferase KW Transmembrane KW Transmembrane helix XX GO GO:0000287; F:magnesium ion binding GO GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups GO GO:0008654; P:phospholipid biosynthetic process GO GO:0005886; C:plasma membrane XX FT From: AIPS_METTH (O27726) FT ACT_SITE 93 FT /note="Proton acceptor" FT Condition: D FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D XX Size: 160-250; Related: None; Template: O27726; Q7LXU6; Q9YBS3; Scope: Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.5 2022/11/19 //