PIPS_MYCMM
ID PIPS_MYCMM Reviewed; 234 AA.
AC B2HM76;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Phosphatidylinositol phosphate synthase {ECO:0000303|PubMed:20798167};
DE Short=PIP synthase {ECO:0000303|PubMed:20798167};
DE EC=2.7.8.- {ECO:0000269|PubMed:20798167};
DE AltName: Full=CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase;
GN Name=pgsA1 {ECO:0000312|EMBL:ACC40540.1};
GN OrderedLocusNames=MMAR_2090 {ECO:0000312|EMBL:ACC40540.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20798167; DOI=10.1093/jb/mvq093;
RA Morii H., Ogawa M., Fukuda K., Taniguchi H., Koga Y.;
RT "A revised biosynthetic pathway for phosphatidylinositol in Mycobacteria.";
RL J. Biochem. 148:593-602(2010).
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:0000269|PubMed:20798167}.
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:0000269|PubMed:20798167};
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:0000269|PubMed:20798167};
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:0000269|PubMed:20798167}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WPG7}.
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_02241}.
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DR EMBL; CP000854; ACC40540.1; -; Genomic_DNA.
DR RefSeq; WP_012393864.1; NC_010612.1.
DR AlphaFoldDB; B2HM76; -.
DR SMR; B2HM76; -.
DR STRING; 216594.MMAR_2090; -.
DR EnsemblBacteria; ACC40540; ACC40540; MMAR_2090.
DR KEGG; mmi:MMAR_2090; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_080384_0_1_11; -.
DR OMA; DGNMARQ; -.
DR OrthoDB; 1232102at2; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000001190; 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 1: Evidence at protein level;
KW Cell membrane; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="Phosphatidylinositol phosphate synthase"
FT /id="PRO_0000448360"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 211..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 234 AA; 24770 MW; 146B890B4A12D805 CRC64;
MSKAPFLSRA AFARVTNPLA RGLLRIGLTP DAVTIIGTTA SVAGALVLFP MGKLFPGACV
VWFFVLFDML DGAMARERGG GTRFGAVLDA ACDRISDGAV FGGLLWWVAF GMRDRLLVVA
TLICLVTSQV ISYIKARAEA SGLRGDGGII ERPERLIIVL AGAGVSDFPF IAWPPALPVA
MWLLAVTSVI TCGQRLYTVW TSPGATDLLV PSAPVRDDDA QGHPRSGDPG KTQR
