PIPS_MYCTO
ID PIPS_MYCTO Reviewed; 217 AA.
AC P9WPG6; L0TBS2; Q79FC5; Q7D6W6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Phosphatidylinositol phosphate synthase {ECO:0000250|UniProtKB:P9WPG7};
DE Short=PIP synthase {ECO:0000250|UniProtKB:P9WPG7};
DE EC=2.7.8.- {ECO:0000250|UniProtKB:P9WPG7};
DE AltName: Full=CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase;
GN Name=pgsA1; OrderedLocusNames=MT2687;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 for mycobacteria
CC required for formation of their cell wall.
CC {ECO:0000250|UniProtKB:P9WPG7}.
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:0000250|UniProtKB:P9WPG7};
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:0000250|UniProtKB:P9WPG7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WPG7};
CC Note=Contains a di-nuclear catalytic Mg(2+) center.
CC {ECO:0000250|UniProtKB:P9WPG7};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC biosynthesis. {ECO:0000250|UniProtKB:P9WPG7}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WPG7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WPG7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P9WPG7}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000255|HAMAP-Rule:MF_02241, ECO:0000305}.
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DR EMBL; AE000516; AAK47003.1; -; Genomic_DNA.
DR PIR; C70571; C70571.
DR RefSeq; WP_003413482.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPG6; -.
DR SMR; P9WPG6; -.
DR EnsemblBacteria; AAK47003; AAK47003; MT2687.
DR KEGG; mtc:MT2687; -.
DR PATRIC; fig|83331.31.peg.2897; -.
DR HOGENOM; CLU_080384_0_1_11; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000001020; 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_02241; PIP_synthase; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
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; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="Phosphatidylinositol phosphate synthase"
FT /id="PRO_0000426955"
FT TRANSMEM 30..48
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT TRANSMEM 54..77
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT TRANSMEM 83..110
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT TRANSMEM 115..140
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT TRANSMEM 152..166
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT TRANSMEM 176..200
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 31..34
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 72
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 76
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 82
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
SQ SEQUENCE 217 AA; 23252 MW; 49BCA9781E35AF2C CRC64;
MSKLPFLSRA AFARITTPIA RGLLRVGLTP DVVTILGTTA SVAGALTLFP MGKLFAGACV
VWFFVLFDML DGAMARERGG GTRFGAVLDA TCDRISDGAV FCGLLWWIAF HMRDRPLVIA
TLICLVTSQV ISYIKARAEA SGLRGDGGFI ERPERLIIVL TGAGVSDFPF VPWPPALSVG
MWLLAVASVI TCVQRLHTVW TSPGAIDRMA IPGKGDR
