ID V6V8J8_CORUL Unreviewed; 229 AA.
AC V6V8J8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=D881_07700 {ECO:0000313|EMBL:ESU57670.1};
OS Corynebacterium ulcerans NCTC 12077.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1258583 {ECO:0000313|EMBL:ESU57670.1, ECO:0000313|Proteomes:UP000018265};
RN [1] {ECO:0000313|EMBL:ESU57670.1, ECO:0000313|Proteomes:UP000018265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12077 {ECO:0000313|EMBL:ESU57670.1,
RC ECO:0000313|Proteomes:UP000018265};
RA Pethick F.E., Lainson A.F., Yaga R., Flockhart A., Walker C.A., Smith D.G.,
RA Donachie W., Fontaine M.C.;
RT "Draft genome sequence of the Corynebacterium ulcerans type strain, NCTC
RT 12077.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESU57670.1}.
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DR EMBL; AYUJ01000007; ESU57670.1; -; Genomic_DNA.
DR RefSeq; WP_023635813.1; NZ_AYUJ01000007.1.
DR AlphaFoldDB; V6V8J8; -.
DR PATRIC; fig|1258583.3.peg.1577; -.
DR OrthoDB; 116551at2; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000018265; Unassembled WGS sequence.
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 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 33..65
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT TRANSMEM 155..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02241"
FT REGION 206..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 229 AA; 23880 MW; C91D9A248D12D1D5 CRC64;
MLSVHGRKPA AVIVEPVAQC FSKMGLSPNS VTVLGTVITV AIAVFLIPTG HLVAAALLSG
LFAAFDMVDG TMARMRGGGT KFGATLDASC DRITDGALFG AITWWLVYSY DAHKALVAAS
FVVLICSQVI SYVKARGEAS GFSMVGGLVE RPERLIIGLI GIGLTGFGVP FAIDVALWIL
AVGSIFTVAQ RLFIASRSEY AQDKIAPPAG AQEHPRGQAV DAGIAQEDV
//
