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Database: UniProt
Entry: R6W557_9FIRM
LinkDB: R6W557_9FIRM
Original site: R6W557_9FIRM 
ID   R6W557_9FIRM            Unreviewed;        87 AA.
AC   R6W557;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=BN636_00255 {ECO:0000313|EMBL:CDD04595.1};
OS   Ruminococcus sp. CAG:382.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262957 {ECO:0000313|EMBL:CDD04595.1, ECO:0000313|Proteomes:UP000018166};
RN   [1] {ECO:0000313|EMBL:CDD04595.1, ECO:0000313|Proteomes:UP000018166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:382 {ECO:0000313|Proteomes:UP000018166};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CDD04595.1}.
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DR   EMBL; CBGH010000294; CDD04595.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6W557; -.
DR   STRING; 1262957.BN636_00255; -.
DR   Proteomes; UP000018166; 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:CDD04595.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018166};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDD04595.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        67..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   87 AA;  9137 MW;  C84A99BB3AC25C69 CRC64;
     MILALIINGC GGGVHFNVLE AALTAIPLSF IGQIGDLSAS LAKRHFGVKD YGNIFPGHGG
     VLDRFDSIIP IAVMIYIITI IINTVSA
//
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