CDSA_THEMA
ID CDSA_THEMA Reviewed; 270 AA.
AC Q9X1B7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Phosphatidate cytidylyltransferase;
DE EC=2.7.7.41;
DE AltName: Full=CDP-DAG synthase;
DE AltName: Full=CDP-DG synthase;
DE AltName: Full=CDP-diacylglycerol 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; OrderedLocusNames=TM_1397;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36468.1; -; Genomic_DNA.
DR PIR; F72259; F72259.
DR RefSeq; NP_229198.1; NC_000853.1.
DR RefSeq; WP_004081613.1; NZ_CP011107.1.
DR PDB; 4Q2E; X-ray; 3.40 A; A/B=1-270.
DR PDB; 4Q2G; X-ray; 3.40 A; A/B=1-270.
DR PDBsum; 4Q2E; -.
DR PDBsum; 4Q2G; -.
DR AlphaFoldDB; Q9X1B7; -.
DR SMR; Q9X1B7; -.
DR STRING; 243274.THEMA_07330; -.
DR EnsemblBacteria; AAD36468; AAD36468; TM_1397.
DR KEGG; tma:TM1397; -.
DR eggNOG; COG0575; Bacteria.
DR InParanoid; Q9X1B7; -.
DR OMA; VFDSFAY; -.
DR OrthoDB; 1533756at2; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR000374; PC_trans.
DR PROSITE; PS01315; CDS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Nucleotidyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..270
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090758"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:4Q2G"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 25..45
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 51..69
FT /evidence="ECO:0007829|PDB:4Q2E"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4Q2E"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 121..154
FT /evidence="ECO:0007829|PDB:4Q2E"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 169..191
FT /evidence="ECO:0007829|PDB:4Q2E"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4Q2G"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4Q2G"
FT HELIX 204..229
FT /evidence="ECO:0007829|PDB:4Q2E"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4Q2E"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4Q2E"
FT HELIX 244..265
FT /evidence="ECO:0007829|PDB:4Q2E"
SQ SEQUENCE 270 AA; 30099 MW; BDAAF664120D7D3E CRC64;
MDDLKTRVIT ASVVAPFVVL CFVSYESLIG LVSAILILAG YELITLEMKE RDARFFYVIL
LALYPVLYGL VFEEPTQPLS ILFITGVVFS LITDKDPSQV FKTVAAFSIA LIYVTFFLSF
FLPIYRDFGA ANALLVLTST WVFDSFAYFT GLKFGRTRIS PRYSPRKSLE GVIGGFLGVV
IYTFLYRLVV NDLLSVNVIS FRTFLPFAAT VAIMDTFGDI FESALKRHYG VKDSGKTLPG
HGGMLDRIDG LLFVAPVSYI VFKILEGVVR
