AIPS_SACS2
ID AIPS_SACS2 Reviewed; 195 AA.
AC Q7LXU6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 Name=pgsA {ECO:0000312|EMBL:AAK40873.1};
GN OrderedLocusNames=SSO0556 {ECO:0000312|EMBL:AAK40873.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
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DR EMBL; AE006641; AAK40873.1; -; Genomic_DNA.
DR PIR; B90202; B90202.
DR RefSeq; WP_009991066.1; NC_002754.1.
DR AlphaFoldDB; Q7LXU6; -.
DR SMR; Q7LXU6; -.
DR STRING; 273057.SSO0556; -.
DR DNASU; 1454840; -.
DR EnsemblBacteria; AAK40873; AAK40873; SSO0556.
DR GeneID; 44129562; -.
DR KEGG; sso:SSO0556; -.
DR PATRIC; fig|273057.12.peg.566; -.
DR eggNOG; arCOG00670; Archaea.
DR HOGENOM; CLU_080384_1_0_2; -.
DR InParanoid; Q7LXU6; -.
DR OMA; DGNMARQ; -.
DR PhylomeDB; Q7LXU6; -.
DR BRENDA; 2.7.8.39; 6163.
DR BRENDA; 2.7.8.B13; 6163.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001974; 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..195
FT /note="Archaetidylinositol phosphate synthase"
FT /id="PRO_0000448365"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
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 195 AA; 22095 MW; D6A1323EC4E8A967 CRC64;
MVSMLTRIRR QIKRVIEPLA KTLAQLKVSA NFITMLGLIF AIVYYFEIMR SNTTLGIIFL
VFSALMDAID GEVARVSKTV SPLGSFLDST LDRIEDILYI SAFIFLGFSS YLVAIAVGLS
LTISYIRAKA ESLGLKMEGR GIIERGERII FVFVILLLYI IVSKQVSLYL FYLFMLLTAI
TVIQRFYAVY SLLRK
