AIPS_PYRHO
ID AIPS_PYRHO Reviewed; 188 AA.
AC O58215;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Archaetidylinositol phosphate synthase {ECO:0000250|UniProtKB:O27726};
DE Short=AIP synthase {ECO:0000250|UniProtKB:O27726};
DE EC=2.7.8.39 {ECO:0000250|UniProtKB:O27726};
GN OrderedLocusNames=PH0460;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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:0000250|UniProtKB:O27726}.
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:0000250|UniProtKB:O27726};
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:0000250|UniProtKB:O27726}.
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; BA000001; BAA29546.1; -; Genomic_DNA.
DR PIR; E71157; E71157.
DR RefSeq; WP_010884567.1; NC_000961.1.
DR AlphaFoldDB; O58215; -.
DR SMR; O58215; -.
DR STRING; 70601.3256863; -.
DR DNASU; 1444354; -.
DR EnsemblBacteria; BAA29546; BAA29546; BAA29546.
DR GeneID; 1444354; -.
DR KEGG; pho:PH0460; -.
DR eggNOG; arCOG00670; Archaea.
DR OMA; DGNMARQ; -.
DR OrthoDB; 115624at2157; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000752; 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 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW Membrane; Metal-binding; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..188
FT /note="Archaetidylinositol phosphate synthase"
FT /id="PRO_0000056822"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
SQ SEQUENCE 188 AA; 20418 MW; D7FE6234216D3214 CRC64;
MLSKIRPKVK QPLERIGKTL ASLGITPNQL TIIGFLITLL ASYEFYLQNQ ILAGIILAVG
AFLDALDGAL ARATGKVSKF GGFLDSTIDR LSDASILFGI ALGGLVRWDV TFLTLIGSYM
VSYSRCRAEL AGSGTLAIGI AERGERIIII FIASLFNAVK IGVYLVAILS WITFIQRVYE
AKKRLEMG
