CDH_ECO57
ID CDH_ECO57 Reviewed; 251 AA.
AC Q8X7A5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=Z5463, ECs4843;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59111.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38266.1; -; Genomic_DNA.
DR PIR; C86081; C86081.
DR PIR; C91234; C91234.
DR RefSeq; NP_312870.1; NC_002695.1.
DR RefSeq; WP_000708998.1; NZ_SWKA01000005.1.
DR PDB; 2POF; X-ray; 1.40 A; A/B=27-251.
DR PDBsum; 2POF; -.
DR AlphaFoldDB; Q8X7A5; -.
DR SMR; Q8X7A5; -.
DR STRING; 155864.EDL933_5247; -.
DR EnsemblBacteria; AAG59111; AAG59111; Z5463.
DR EnsemblBacteria; BAB38266; BAB38266; ECs_4843.
DR GeneID; 66672174; -.
DR GeneID; 915054; -.
DR KEGG; ece:Z5463; -.
DR KEGG; ecs:ECs_4843; -.
DR PATRIC; fig|386585.9.peg.5065; -.
DR eggNOG; COG2134; Bacteria.
DR HOGENOM; CLU_077117_0_1_6; -.
DR OMA; SPFIMLA; -.
DR UniPathway; UPA00609; UER00664.
DR EvolutionaryTrace; Q8X7A5; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..251
FT /note="CDP-diacylglycerol pyrophosphatase"
FT /id="PRO_0000198575"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00319"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2POF"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2POF"
FT TURN 201..205
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:2POF"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:2POF"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:2POF"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2POF"
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
