ID A0A1G5G296_9ACTN Unreviewed; 286 AA.
AC A0A1G5G296;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=SAMN02745898_10236 {ECO:0000313|EMBL:SCY45457.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCY45457.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCY45457.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCY45457.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FMVI01000002; SCY45457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5G296; -.
DR OrthoDB; 4749050at2; -.
DR Proteomes; UP000199326; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; 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 ECO:0000313|EMBL:SCY45457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199326};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCY45457.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 286 AA; 28873 MW; 317ED802B465A23B CRC64;
MSAALIAEEA AARAVPLVAG VLGAGGVAVA VLPSKVRMRA ELRRRWRTWA LVAPVFLGAY
LLGDGGTFVL AAGLGVIAVS EFVRMAGSAR GDHAVLVTAA VALPALAWLA PHLLDLRAAA
LLLIAAAVPS LLAGDDRSGF TRTARTAFGL LWIPVALTGL VTLGGTGVAV GLAVALGDVG
AWCGGTAMGR RGPLSRPLSP LSPNKTWAGV MGAAVATALL LLLIGAFALP LWGAVLGGCV
LGDLLESMVK RESGVKDAGS WLPGFGGLLD RIDSLLVALL LTMVTV
//
