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Database: UniProt
Entry: D6GRA6_FILAD
LinkDB: D6GRA6_FILAD
Original site: D6GRA6_FILAD 
ID   D6GRA6_FILAD            Unreviewed;       262 AA.
AC   D6GRA6;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019373, ECO:0000256|RuleBase:RU003938};
DE            EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN   Name=cdsA {ECO:0000313|EMBL:EFE28197.1};
GN   OrderedLocusNames=HMPREF0389_00111 {ECO:0000313|EMBL:EFE28197.1};
OS   Filifactor alocis (strain ATCC 35896 / CCUG 47790 / D40 B5) (Fusobacterium
OS   alocis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Filifactor.
OX   NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE28197.1, ECO:0000313|Proteomes:UP000007468};
RN   [1] {ECO:0000313|Proteomes:UP000007468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., Izard J.,
RA   Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL   Submitted (DEC-2010) 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         ECO:0000256|RuleBase:RU003938};
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, ECO:0000256|RuleBase:RU003938}.
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       ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; CP002390; EFE28197.1; -; Genomic_DNA.
DR   RefSeq; WP_014262181.1; NC_016630.1.
DR   AlphaFoldDB; D6GRA6; -.
DR   STRING; 546269.HMPREF0389_00111; -.
DR   KEGG; faa:HMPREF0389_00111; -.
DR   PATRIC; fig|546269.5.peg.550; -.
DR   eggNOG; COG4589; Bacteria.
DR   OrthoDB; 9799199at2; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000007468; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR000374; PC_trans.
DR   PANTHER; PTHR46382; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46382:SF1; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PROSITE; PS01315; CDS; 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:0000256|RuleBase:RU003938};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007468};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003938};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003938};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   262 AA;  29794 MW;  40EFD2B936C726DA CRC64;
     MLVRLLSALV LIPFLLFSVH CGGIYLFIFL CGASLIGLYE MTRVFQKKGY RVLEKELYFF
     TFLTYILLFS KEEIGKNYNM IPFLFLTGAV YMIQKRFSVE ELGLNILSYV YIPISLSYVF
     KVEQFTHSYV WFIFILAYAT DTFAYFSGKL FGKHKLIPKI SPNKTIEGAI GGIIGAVISC
     EIYLFYLGET KYVIPIIAVA IVGSILSQLG DLFASSIKRL FDVKDYGKLI PGHGGVLDRI
     DSVLFTAPFV YYAFVLIELF IK
//
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