ID Q6W3A0_9CREN Unreviewed; 190 AA.
AC Q6W3A0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Archaetidylinositol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_02242};
DE Short=AIP synthase {ECO:0000256|HAMAP-Rule:MF_02242};
DE EC=2.7.8.39 {ECO:0000256|HAMAP-Rule:MF_02242};
GN Name=pgsA {ECO:0000313|EMBL:AAR24469.1};
OS uncultured crenarchaeote DeepAnt-EC39.
OC Archaea; Thermoproteota; environmental samples.
OX NCBI_TaxID=247023 {ECO:0000313|EMBL:AAR24469.1};
RN [1] {ECO:0000313|EMBL:AAR24469.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14686938; DOI=10.1046/j.1462-2920.2003.00533.x;
RA Lopez-Garcia P., Brochier C., Moreira D., Rodriguez-Valera F.;
RT "Comparative analysis of a genome fragment of an uncultivated mesopelagic
RT crenarchaeote reveals multiple horizontal gene transfers.";
RL Environ. Microbiol. 6:19-34(2004).
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 {ECO:0000256|HAMAP-Rule:MF_02242}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02242};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02242};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02242};
CC Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_02242};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_02242}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02242};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02242}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|HAMAP-Rule:MF_02242,
CC ECO:0000256|RuleBase:RU003750}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02242}.
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DR EMBL; AY316120; AAR24469.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6W3A0; -.
DR UniPathway; UPA00085; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1760; -; 1.
DR HAMAP; MF_02242; AIP_synthase; 1.
DR InterPro; IPR044270; AIP_synthase.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02242};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02242};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_02242};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02242};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_02242};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02242};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02242};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_02242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02242}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_02242};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02242}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT TRANSMEM 51..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT TRANSMEM 150..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02242"
SQ SEQUENCE 190 AA; 20484 MW; 6ED21775BA66DEB4 CRC64;
MLNNLRDSLQ PHLEKMGRGF ASTGISPNGW SCIGLVFAFV SAFIYGWNVE FSLIIGGIVL
LIAGFFDIVD GQVARASQKI TKSGGFLDSV FDKIAEVAIF LGILVGGFAE PYLVFLAITL
SLLVSYTRSR AESLGVKLQG IGIGERAERL LVIAIVGIIG FMEYAVIIVI IIAAITFIQR
IIVTVKALKE
//
