DAGK_MYCTU
ID DAGK_MYCTU Reviewed; 309 AA.
AC P9WP29; L0TAM7; O53526;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Diacylglycerol kinase {ECO:0000250|UniProtKB:P9WP28};
DE Short=DAG kinase {ECO:0000250|UniProtKB:P9WP28};
DE Short=DAGK {ECO:0000250|UniProtKB:P9WP28};
DE EC=2.7.1.107 {ECO:0000250|UniProtKB:P9WP28};
GN Name=dagK; OrderedLocusNames=Rv2252;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of diacylglycerol (DAG) into
CC phosphatidic acid. Is involved in the biosynthesis of
CC phosphatidylinositol mannosides (PIMs), probably via a role in the
CC biosynthesis of phosphatidylinositol (PI), a PIM precursor, which is
CC derived from phosphatidic acid. {ECO:0000250|UniProtKB:P9WP28}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000250|UniProtKB:P9WP28};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000250|UniProtKB:P9WP28};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q6GFF9};
CC Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC structural role and is required for catalytic activity.
CC {ECO:0000250|UniProtKB:Q6GFF9};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:P9WP28}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45033.1; -; Genomic_DNA.
DR PIR; H70861; H70861.
DR RefSeq; NP_216768.1; NC_000962.3.
DR RefSeq; WP_003411603.1; NZ_NVQJ01000008.1.
DR AlphaFoldDB; P9WP29; -.
DR SMR; P9WP29; -.
DR STRING; 83332.Rv2252; -.
DR SwissLipids; SLP:000001234; -.
DR PaxDb; P9WP29; -.
DR DNASU; 888429; -.
DR GeneID; 45426232; -.
DR GeneID; 888429; -.
DR KEGG; mtu:Rv2252; -.
DR TubercuList; Rv2252; -.
DR eggNOG; COG1597; Bacteria.
DR OMA; GFDSRVN; -.
DR PhylomeDB; P9WP29; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell wall; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Secreted; Transferase.
FT CHAIN 1..309
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000386484"
FT DOMAIN 9..140
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6GFF9"
FT BINDING 19..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 76..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q6GFF9"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q6GFF9"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q6GFF9"
SQ SEQUENCE 309 AA; 32805 MW; 34F5E363D62BB284 CRC64;
MSAGQLRRHE IGKVTALTNP LSGHGAAVKA AHGAIARLKH RGVDVVEIVG GDAHDARHLL
AAAVAKGTDA VMVTGGDGVV SNALQVLAGT DIPLGIIPAG TGNDHAREFG LPTKNPKAAA
DIVVDGWTET IDLGRIQDDN GIEKWFGTVA ATGFDSLVND RANRMRWPHG RMRYYIAMLA
ELSRLRPLPF RLVLDGTEEI VADLTLADFG NTRSYGGGLL ICPNADHSDG LLDITMAQSD
SRTKLLRLFP TIFKGAHVEL DEVSTTRAKT VHVECPGINV YADGDFACPL PAEISAVPAA
LQVLRPRHG
