ID K0K175_SACES Unreviewed; 202 AA.
AC K0K175;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Phosphatidylinositol phosphate synthase {ECO:0000256|ARBA:ARBA00024082, ECO:0000256|HAMAP-Rule:MF_02241};
DE Short=PIP synthase {ECO:0000256|HAMAP-Rule:MF_02241};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_02241};
DE AltName: Full=CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00033137, ECO:0000256|HAMAP-Rule:MF_02241};
GN OrderedLocusNames=BN6_30310 {ECO:0000313|EMBL:CCH30338.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH30338.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH30338.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC -!- FUNCTION: Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-
CC inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a
CC lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming
CC phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of
CC phosphatidylinositol (PI) which is an essential lipid required for cell
CC wall formation. {ECO:0000256|HAMAP-Rule:MF_02241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate
CC + 1D-myo-inositol 3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H(+);
CC Xref=Rhea:RHEA:61216, ChEBI:CHEBI:15378, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:85356, ChEBI:CHEBI:144472;
CC Evidence={ECO:0000256|ARBA:ARBA00023935, ECO:0000256|HAMAP-
CC Rule:MF_02241};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + a CDP-1,2-diacyl-sn-glycerol = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:60504, ChEBI:CHEBI:15378, ChEBI:CHEBI:58088,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58401, ChEBI:CHEBI:60377;
CC Evidence={ECO:0000256|ARBA:ARBA00023976, ECO:0000256|HAMAP-
CC Rule:MF_02241};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02241};
CC Note=Contains a di-nuclear catalytic Mg(2+) center. {ECO:0000256|HAMAP-
CC Rule:MF_02241};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004805, ECO:0000256|HAMAP-
CC Rule:MF_02241}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_02241}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02241};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02241}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|HAMAP-
CC Rule:MF_02241, ECO:0000256|RuleBase:RU003750}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02241}.
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DR EMBL; HE804045; CCH30338.1; -; Genomic_DNA.
DR RefSeq; WP_015100450.1; NC_019673.1.
DR AlphaFoldDB; K0K175; -.
DR STRING; 1179773.BN6_30310; -.
DR KEGG; sesp:BN6_30310; -.
DR PATRIC; fig|1179773.3.peg.3025; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_080384_0_1_11; -.
DR OrthoDB; 116551at2; -.
DR BioCyc; SESP1179773:BN6_RS14730-MONOMER; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000006281; Chromosome.
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_02241; PIP_synthase; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR044268; PIP_synthase_PgsA1.
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_02241};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02241};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_02241};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02241};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02241};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02241};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02241};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_02241};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02241};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02241};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02241}.
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 29..32
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 70
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 74
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 80
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
SQ SEQUENCE 202 AA; 20812 MW; 8766A30A2F8E5B65 CRC64;
MLNIFARASV SRVTDPIGAW LLRRGLTPNT VTVLGTVCSV AASLWFIPRG QLFTGAAVVT
AFLLFDLIDG AMARAQGGGT AYGAVLDASC DRIADGALFA AIAWWCFGAD EHGLAAATLV
SLVGALVTSY VKARAEASGL SADGGVAERA DRFVVALIGV GLHGLGVPYV LPVALYLLAA
LVVITVAQRL LAVRRSAKEL AT
//
