AIPS_AERPE
ID AIPS_AERPE Reviewed; 194 AA.
AC Q9YBS3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Archaetidylinositol phosphate synthase {ECO:0000303|PubMed:24269814};
DE Short=AIP synthase {ECO:0000303|PubMed:24269814};
DE EC=2.7.8.39 {ECO:0000269|PubMed:24269814};
GN OrderedLocusNames=APE_1526.1 {ECO:0000312|EMBL:BAA80525.2};
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=24269814; DOI=10.1016/j.bbrc.2013.11.054;
RA Morii H., Ogawa M., Fukuda K., Taniguchi H.;
RT "Ubiquitous distribution of phosphatidylinositol phosphate synthase and
RT archaetidylinositol phosphate synthase in Bacteria and Archaea, which
RT contain inositol phospholipid.";
RL Biochem. Biophys. Res. Commun. 443:86-90(2014).
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:0000269|PubMed:24269814}.
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 Evidence={ECO:0000269|PubMed:24269814};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O27726};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O27726};
CC Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:O27726};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000305|PubMed:24269814}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000255|HAMAP-Rule:MF_02242, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000002; BAA80525.2; -; Genomic_DNA.
DR PIR; G72633; G72633.
DR AlphaFoldDB; Q9YBS3; -.
DR SMR; Q9YBS3; -.
DR STRING; 272557.APE_1526.1; -.
DR EnsemblBacteria; BAA80525; BAA80525; APE_1526.1.
DR KEGG; ape:APE_1526.1; -.
DR PATRIC; fig|272557.25.peg.1029; -.
DR eggNOG; arCOG00670; Archaea.
DR OMA; DGNMARQ; -.
DR BRENDA; 2.7.8.39; 171.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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 Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW Membrane; Metal-binding; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..194
FT /note="Archaetidylinositol phosphate synthase"
FT /id="PRO_0000448366"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
SQ SEQUENCE 194 AA; 20735 MW; 9C3651A4F3627E71 CRC64;
MGVFNRLRSF YEARIAPTVA SFLSRISPDP NIYTLASPVA AAAALPAWLY ISPVASLLLI
ALSLLLDAVD GAVARFTGRV SPLGSFLDSS LDRISDSLYH ATLYIAGVHP LIVIAMLSGG
LIVPYLRAKG ESLGLEVRGR GLMERGERSI AILAILAISI YNLQTALALA SAAAVLVWIT
VIQRMVYIAG ELRR
