CDH_ECO24
ID CDH_ECO24 Reviewed; 251 AA.
AC A7ZUD2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=CDP-diacylglycerol pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00319};
DE EC=3.6.1.26 {ECO:0000255|HAMAP-Rule:MF_00319};
DE AltName: Full=CDP-diacylglycerol phosphatidylhydrolase {ECO:0000255|HAMAP-Rule:MF_00319};
DE AltName: Full=CDP-diglyceride hydrolase {ECO:0000255|HAMAP-Rule:MF_00319};
GN Name=cdh {ECO:0000255|HAMAP-Rule:MF_00319};
GN OrderedLocusNames=EcE24377A_4452;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-
CC 3-phosphate + CMP + 2 H(+); Xref=Rhea:RHEA:15221, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58332, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:60377; EC=3.6.1.26; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00319};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol degradation;
CC phosphatidate from CDP-diacylglycerol: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00319}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00319}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00319}.
CC -!- SIMILARITY: Belongs to the Cdh family. {ECO:0000255|HAMAP-
CC Rule:MF_00319}.
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DR EMBL; CP000800; ABV17277.1; -; Genomic_DNA.
DR RefSeq; WP_000708998.1; NC_009801.1.
DR AlphaFoldDB; A7ZUD2; -.
DR SMR; A7ZUD2; -.
DR EnsemblBacteria; ABV17277; ABV17277; EcE24377A_4452.
DR GeneID; 66672174; -.
DR KEGG; ecw:EcE24377A_4452; -.
DR HOGENOM; CLU_077117_0_1_6; -.
DR OMA; SPFIMLA; -.
DR UniPathway; UPA00609; UER00664.
DR Proteomes; UP000001122; Chromosome.
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:0008715; F:CDP-diacylglycerol diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046342; P:CDP-diacylglycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.428.30; -; 1.
DR HAMAP; MF_00319; Cdh; 1.
DR InterPro; IPR003763; CDP-diacylglyc_Pase.
DR InterPro; IPR015993; CDP-diacylglyc_Pase_proteobac.
DR InterPro; IPR036265; HIT-like_sf.
DR Pfam; PF02611; CDH; 1.
DR PIRSF; PIRSF001273; CDH; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR TIGRFAMs; TIGR00672; cdh; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..251
FT /note="CDP-diacylglycerol pyrophosphatase"
FT /id="PRO_1000059463"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00319"
SQ SEQUENCE 251 AA; 28383 MW; C987D3A4B12BE5F3 CRC64;
MKKAGLLFLV MIVIAVVAAG IGYWKLTGEE SDTLRKIVLE ECLPNQQQNQ NPSPCAEVKP
NAGYVVLKDL NGPLQYLLMP TYRINGTESP LLTDPSTPNF FWLAWQARDF MSKKYGQPVP
DRAVSLAINS RTGRTQNHFH IHISCIRPDV REQLDNNLAN ISSRWLPLPG GLRGHEYLAR
RVTESELVQR SPFMMLAEEV PEAREHMGSY GLAMVRQSDN SFVLLATQRN LLTLNRASAE
EIQDHQCEIL R
