ID CDSA_HAEIN Reviewed; 288 AA. AC P44937; O32623; O32627; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 130. DE RecName: Full=Phosphatidate cytidylyltransferase; DE EC=2.7.7.41 {ECO:0000250|UniProtKB:P0ABG1}; DE AltName: Full=CDP-diacylglycerol synthase; DE Short=CDP-DAG synthase; DE Short=CDP-DG synthase; DE Short=CDS; DE AltName: Full=CDP-diglyceride pyrophosphorylase; DE AltName: Full=CDP-diglyceride synthase; DE AltName: Full=CTP:phosphatidate cytidylyltransferase; GN Name=cdsA; Synonyms=cds; OrderedLocusNames=HI_0919; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=33, and Eagan / Serotype B; RA Loosmore S.M., Yang Y., Coleman D.C., Shortreed J.M., England D.M., RA Klein M.H.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Transferase that catalyzes the synthesis of a CDP- CC diacylglycerol (CDP-DAG), the activated form of a phosphatidate. CC {ECO:0000250|UniProtKB:P0ABG1}. 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:0000250|UniProtKB:P0ABG1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230; CC Evidence={ECO:0000250|UniProtKB:P0ABG1}; CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP- CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC {ECO:0000250|UniProtKB:P0ABG1}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0ABG1}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22577.1; -; Genomic_DNA. DR EMBL; U60831; AAB61967.1; -; Genomic_DNA. DR EMBL; U60832; AAB61972.1; -; Genomic_DNA. DR PIR; G64102; G64102. DR AlphaFoldDB; P44937; -. DR SMR; P44937; -. DR STRING; 71421.HI_0919; -. DR EnsemblBacteria; AAC22577; AAC22577; HI_0919. DR KEGG; hin:HI_0919; -. DR PATRIC; fig|71421.8.peg.960; -. DR eggNOG; COG0575; Bacteria. DR HOGENOM; CLU_037294_1_2_6; -. DR OrthoDB; 9799199at2; -. DR PhylomeDB; P44937; -. DR BioCyc; HINF71421:G1GJ1-958-MONOMER; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; ISS:UniProtKB. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central. 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 inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism; KW Membrane; Nucleotidyltransferase; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..288 FT /note="Phosphatidate cytidylyltransferase" FT /id="PRO_0000090736" FT TRANSMEM 10..30 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 52..72 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 89..109 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 192..212 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 223..243 FT /note="Helical" FT /evidence="ECO:0000255" FT VARIANT 16 FT /note="V -> F (in strain: Eagan)" FT VARIANT 59 FT /note="T -> A (in strain: 33)" FT VARIANT 81 FT /note="R -> H (in strain: Eagan)" SQ SEQUENCE 288 AA; 32247 MW; 67FFBF29997FAFA5 CRC64; MLKQRVLSAI VLIAAVLCAL FLFTPFYFAL ALGAVAILGI WEWTQFARLK QPLIRFFVTT FLGVFIFLWL YTEGNYLDAG RVFEQHLQLL LINAVSWWGL ALLLVISYPK SAKFWSKNPL LQLLFAFSTL IPFVAGVLRL RLEHYTHDPY HGLFLLLYVF ILVWAADSGA YFSGRAFGKR KLAPKVSPGK SWEGVIGGLI TALVLAFIFI HFSNNTLVGD RNITGFIILS VATVAISVLG DLTESMFKRE SGVKDSSQLI PGHGGVLDRI DSLTAAVPFF SYFYFFVL //