PIPS_CUTAK
ID PIPS_CUTAK Reviewed; 207 AA.
AC Q6A8U1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphatidylinositol phosphate synthase {ECO:0000303|PubMed:24269814};
DE Short=PIP synthase {ECO:0000303|PubMed:24269814};
DE EC=2.7.8.- {ECO:0000269|PubMed:24269814};
DE AltName: Full=CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase;
GN OrderedLocusNames=PPA1078 {ECO:0000312|EMBL:AAT82825.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=24269814; DOI=10.1016/j.bbrc.2013.11.054;
RA Morii H., Ogawa M., Fukuda K., Taniguchi H.;
RT "Ubiquitous distribution of phosphatidylinositol phosphate synthase and
RT archaetidylinositol phosphate synthase in Bacteria and Archaea, which
RT contain inositol phospholipid.";
RL Biochem. Biophys. Res. Commun. 443:86-90(2014).
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:0000269|PubMed:24269814}.
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:24269814};
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:24269814};
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:0000305|PubMed:24269814}.
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, ECO:0000305}.
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DR EMBL; AE017283; AAT82825.1; -; Genomic_DNA.
DR RefSeq; WP_002513638.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A8U1; -.
DR SMR; Q6A8U1; -.
DR STRING; 267747.PPA1078; -.
DR EnsemblBacteria; AAT82825; AAT82825; PPA1078.
DR GeneID; 66621058; -.
DR KEGG; pac:PPA1078; -.
DR eggNOG; COG0558; Bacteria.
DR HOGENOM; CLU_080384_0_1_11; -.
DR OMA; DGNMARQ; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000000603; 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; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..207
FT /note="Phosphatidylinositol phosphate synthase"
FT /id="PRO_0000448363"
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 28..31
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 69
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 73
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 79
FT /ligand="a CDP-1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:58332"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WPG7"
SQ SEQUENCE 207 AA; 22324 MW; C908EA3558572C4A CRC64;
MLEHFRAGWA KVMNPIADAL LRAHVTPDVV TWIGTIGAVL MALICFPQGW LWQGPWLVTL
FIFSDSLDGN MARKLGRHSQ WGSFLDSTLD RFGDAAIFTG VALYFAGPGN SVLWTAMACA
ALVFGMATSY VRAKAESLAL EAKVGIATRA DRLLVSLVAI EITGLARVGA FPHWCVVALP
IALCYLTLAG AITVVQRMVA VRRACES
