ID A0A1J4VRJ8_9BACT Unreviewed; 269 AA.
AC A0A1J4VRJ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019373};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487};
DE AltName: Full=CDP-DAG synthase {ECO:0000256|ARBA:ARBA00032253};
DE AltName: Full=CDP-DG synthase {ECO:0000256|ARBA:ARBA00032743};
DE AltName: Full=CDP-diacylglycerol synthase {ECO:0000256|ARBA:ARBA00029893};
DE AltName: Full=CDP-diglyceride pyrophosphorylase {ECO:0000256|ARBA:ARBA00032396};
DE AltName: Full=CDP-diglyceride synthase {ECO:0000256|ARBA:ARBA00033406};
DE AltName: Full=CTP:phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00031825};
GN ORFNames=AUJ75_00880 {ECO:0000313|EMBL:OIO39796.1};
OS Candidatus Omnitrophica bacterium CG1_02_49_10.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805289 {ECO:0000313|EMBL:OIO39796.1, ECO:0000313|Proteomes:UP000182804};
RN [1] {ECO:0000313|EMBL:OIO39796.1, ECO:0000313|Proteomes:UP000182804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_49_10 {ECO:0000313|EMBL:OIO39796.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001698};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185}.
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:OIO39796.1}.
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DR EMBL; MNVT01000022; OIO39796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4VRJ8; -.
DR Proteomes; UP000182804; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 269 AA; 29785 MW; ADC1A6A8D5E06967 CRC64;
MRGLSYKRIA SAAVVIISLW SIIYIFPLWI FGIVCVLFVG VGTHEFFSML EKREVFIHKY
FGLLFAIYVP IAAFLTKGVN PASESAVIWA AIFIFFCLQF THKDNTLAVR DISVTFFVIM
YVSWMLSHVI KIRFMDNGAN LVAYLLLVCK SGDMGAYIIG NLFGHHPLIP RISPNKSVEG
CLGGMFFSIA VSVLGASLVP RIPLKDLIFL GFILGALAQF GDLTESLIKR NCRVKDSGDI
VPGLGGALDL ADSMIFSAPV FYLYLKVFL
//