CDSA_BRUME
ID CDSA_BRUME Reviewed; 270 AA.
AC Q8YHH2;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=BMEI0828;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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 inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL52009.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL52009.1; ALT_INIT; Genomic_DNA.
DR PIR; AF3355; AF3355.
DR RefSeq; WP_004683870.1; NZ_GG703780.1.
DR AlphaFoldDB; Q8YHH2; -.
DR SMR; Q8YHH2; -.
DR STRING; 224914.BMEI0828; -.
DR EnsemblBacteria; AAL52009; AAL52009; BMEI0828.
DR GeneID; 29593639; -.
DR KEGG; bme:BMEI0828; -.
DR PATRIC; fig|224914.52.peg.617; -.
DR eggNOG; COG0575; Bacteria.
DR OMA; PKFWPRV; -.
DR PhylomeDB; Q8YHH2; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000000419; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090729"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 270 AA; 28432 MW; 2A2923106D71A723 CRC64;
MSNLQTRIIT AIVLGTITLW LTWVGGVGFT LFSIAIGLAM FYEWTELSAT RQTAFSRLFG
WAWLIVTGIL LILDRGALLT IGFLVAGCAI LLVTQWKSGR GWPAAGLFYA GFSALSLSLL
RGDEPFGFTT IVFLFAVVWS TDIAAYFNGR ALGGPKLAPR FSPNKTWSGA IGGAAAAVTG
GLLVASLVAA PGGWGVPVLA LLLSIVSQIG DLAESWVKRQ FGAKDSGRLL PGHGGVLDRV
DGLVAAAALL YLFGAIFAEP DVPSAIFFSF