CDH_MYCBT
ID CDH_MYCBT Reviewed; 260 AA.
AC C1AQK4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
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}; OrderedLocusNames=JTY_2299;
OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=561275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL Vaccine 27:1710-1716(2009).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00319};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00319}.
CC -!- SIMILARITY: Belongs to the Cdh family. {ECO:0000255|HAMAP-
CC Rule:MF_00319}.
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DR EMBL; AP010918; BAH26583.1; -; Genomic_DNA.
DR RefSeq; WP_003411717.1; NZ_CP014566.1.
DR AlphaFoldDB; C1AQK4; -.
DR SMR; C1AQK4; -.
DR GeneID; 45426268; -.
DR KEGG; mbt:JTY_2299; -.
DR HOGENOM; CLU_077117_1_0_11; -.
DR OMA; SPFIMLA; -.
DR UniPathway; UPA00609; UER00664.
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; IPR036265; HIT-like_sf.
DR Pfam; PF02611; CDH; 1.
DR PIRSF; PIRSF001273; CDH; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..260
FT /note="CDP-diacylglycerol pyrophosphatase"
FT /id="PRO_1000133035"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00319"
SQ SEQUENCE 260 AA; 28608 MW; D2884BE3B6F1489D CRC64;
MPKSRRAVSL SVLIGAVIAA LAGALIAVTV PARPNRPEAD REALWKIVHD RCEFGYRRTG
AYAPCTFVDE QSGTALYKAD FDPYQFLLIP LARITGIEDP ALRESAGRNY LYDAWAARFL
VTARLNNSLP ESDVVLTINP KNARTQDQLH IHISCSSPTT SAALRNVDTS EYVGWKQLPI
DLGGRRFQGL AVDTKAFESR NLFRDIYLKV TADGKKMENA SIAVANVAQD QFLLLLAEGT
EDQPVAAETL QDHDCSITKS