CDS1_YEAST
ID CDS1_YEAST Reviewed; 457 AA.
AC P38221; D6VQ30;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosphatidate cytidylyltransferase;
DE EC=2.7.7.41;
DE AltName: Full=CDP-diacylglycerol synthase;
DE Short=CDP-DAG synthase;
DE Short=CDS;
DE AltName: Full=CDP-diglyceride pyrophosphorylase;
DE AltName: Full=CDP-diglyceride synthase;
DE Short=CDP-DG synthase;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN Name=CDS1; Synonyms=CDG1; OrderedLocusNames=YBR029C; ORFNames=YBR0313;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8557688; DOI=10.1074/jbc.271.2.789;
RA Shen H., Heacock P.N., Clancey C.J., Dowhan W.;
RT "The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces
RT cerevisiae is essential for cell growth.";
RL J. Biol. Chem. 271:789-795(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2822695; DOI=10.1016/s0021-9258(18)47833-7;
RA Kelley M.J., Carman G.M.;
RT "Purification and characterization of CDP-diacylglycerol synthase from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 262:14563-14570(1987).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=2163397; DOI=10.1128/jb.172.7.4115-4117.1990;
RA Kinney A.J., Carman G.M.;
RT "Enzymes of phosphoinositide synthesis in secretory vesicles destined for
RT the plasma membrane in Saccharomyces cerevisiae.";
RL J. Bacteriol. 172:4115-4117(1990).
RN [8]
RP MUTAGENESIS OF CYS-102.
RX PubMed=8910557; DOI=10.1074/jbc.271.46.29043;
RA Shen H., Dowhan W.;
RT "Reduction of CDP-diacylglycerol synthase activity results in the excretion
RT of inositol by Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:29043-29048(1996).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23623749; DOI=10.1016/j.cmet.2013.03.018;
RA Tamura Y., Harada Y., Nishikawa S., Yamano K., Kamiya M., Shiota T.,
RA Kuroda T., Kuge O., Sesaki H., Imai K., Tomii K., Endo T.;
RT "Tam41 is a CDP-diacylglycerol synthase required for cardiolipin
RT biosynthesis in mitochondria.";
RL Cell Metab. 17:709-718(2013).
CC -!- FUNCTION: Supplies CDP-diacylglycerol, which may play an important role
CC as both a precursor to phosphoinositide biosynthesis in the plasma
CC membrane and as a negative effector of phosphatidylinositol 4-kinase
CC activity, thereby exerting an effect on cell proliferation via a lipid-
CC dependent signal transduction cascade. {ECO:0000269|PubMed:2822695,
CC ECO:0000269|PubMed:8557688}.
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:0000269|PubMed:2822695};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2822695};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for CTP {ECO:0000269|PubMed:2822695};
CC KM=0.5 mM for phosphatidate {ECO:0000269|PubMed:2822695};
CC Vmax=4700 nmol/min/mg enzyme {ECO:0000269|PubMed:2822695};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:2822695};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Cytoplasmic vesicle, secretory vesicle.
CC Note=Exclusively present in the ER, and not in mitochondria. Also
CC associated with post-Golgi apparatus secretory vesicles destined for
CC the plasma membrane.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; X76078; CAA53685.1; -; Genomic_DNA.
DR EMBL; Z35898; CAA84971.1; -; Genomic_DNA.
DR EMBL; AY693074; AAT93093.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07150.1; -; Genomic_DNA.
DR PIR; S45885; S45885.
DR RefSeq; NP_009585.1; NM_001178377.1.
DR AlphaFoldDB; P38221; -.
DR SMR; P38221; -.
DR BioGRID; 32731; 248.
DR DIP; DIP-7898N; -.
DR IntAct; P38221; 3.
DR MINT; P38221; -.
DR STRING; 4932.YBR029C; -.
DR SwissLipids; SLP:000000050; -.
DR iPTMnet; P38221; -.
DR MaxQB; P38221; -.
DR PaxDb; P38221; -.
DR PRIDE; P38221; -.
DR EnsemblFungi; YBR029C_mRNA; YBR029C; YBR029C.
DR GeneID; 852317; -.
DR KEGG; sce:YBR029C; -.
DR SGD; S000000233; CDS1.
DR VEuPathDB; FungiDB:YBR029C; -.
DR eggNOG; KOG1440; Eukaryota.
DR GeneTree; ENSGT00940000170268; -.
DR HOGENOM; CLU_023471_1_1_1; -.
DR InParanoid; P38221; -.
DR OMA; FIMNNIF; -.
DR BioCyc; YEAST:YBR029C-MON; -.
DR BRENDA; 2.7.7.41; 984.
DR Reactome; R-SCE-1483148; Synthesis of PG.
DR Reactome; R-SCE-1483226; Synthesis of PI.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:P38221; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38221; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:SGD.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IMP:SGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:SGD.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IMP:SGD.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PTHR13773; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..457
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090722"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 102
FT /note="C->Y: Reduced enzyme level."
FT /evidence="ECO:0000269|PubMed:8910557"
SQ SEQUENCE 457 AA; 51823 MW; F9F3613856EDE172 CRC64;
MSDNPEMKPH GTSKEIVESV TDATSKAIDK LQEELHKDAS ESVTPVTKES TAATKESRKY
NFFIRTVWTF VMISGFFITL ASGHAWCIVL ILGCQIATFK ECIAVTSASG REKNLPLTKT
LNWYLLFTTI YYLDGKSLFK FFQATFYEYP VLNFIVTNHK FICYCLYLMG FVLFVCSLRK
GFLKFQFGSL CVTHMVLLLV VFQAHLIIKN VLNGLFWFLL PCGLVIVNDI FAYLCGITFG
KTKLIEISPK KTLEGFLGAW FFTALASIIL TRILSPYTYL TCPVEDLHTN FFSNLTCELN
PVFLPQVYRL PPIFFDKVQI NSITVKPIYF HALNLATFAS LFAPFGGFFA SGLKRTFKVK
DFGHSIPGHG GITDRVDCQF IMGSFANLYY ETFISEHRIT VDTVLSTILM NLNDKQIIEL
IDILIRFLSK KGIISAKNFE KLADIFNVTK KSLTNHS
