DAGK_MYCTO
ID DAGK_MYCTO Reviewed; 309 AA.
AC P9WP28; L0TAM7; O53526;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Diacylglycerol kinase {ECO:0000303|PubMed:16689792};
DE Short=DAG kinase {ECO:0000305};
DE Short=DAGK {ECO:0000303|PubMed:16689792};
DE EC=2.7.1.107 {ECO:0000269|PubMed:16689792};
GN Name=dagK; OrderedLocusNames=MT2312;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=16689792; DOI=10.1111/j.1365-2958.2006.05174.x;
RA Owens R.M., Hsu F.F., VanderVen B.C., Purdy G.E., Hesteande E.,
RA Giannakas P., Sacchettini J.C., McKinney J.D., Hill P.J., Belisle J.T.,
RA Butcher B.A., Pethe K., Russell D.G.;
RT "M. tuberculosis Rv2252 encodes a diacylglycerol kinase involved in the
RT biosynthesis of phosphatidylinositol mannosides (PIMs).";
RL Mol. Microbiol. 60:1152-1163(2006).
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 (PubMed:16689792). Is also able to
CC phosphorylate other various amphipathic lipids of host and bacterial
CC origin in vitro, such as ceramide (PubMed:16689792).
CC {ECO:0000269|PubMed:16689792}.
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:0000269|PubMed:16689792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:16689792};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-hexadecanoylsphing-4-enine = ADP + H(+) + N-
CC (hexadecanoyl)-sphing-4-enine-1-phosphate; Xref=Rhea:RHEA:46340,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72959,
CC ChEBI:CHEBI:72963, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:16689792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46341;
CC Evidence={ECO:0000269|PubMed:16689792};
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:0000305|PubMed:16689792}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit a disruption of
CC the production of certain higher-order phosphatidylinositol mannosides
CC (PIMs) species. {ECO:0000269|PubMed:16689792}.
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AE000516; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE000516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H70861; H70861.
DR RefSeq; WP_003411603.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WP28; -.
DR SMR; P9WP28; -.
DR PRIDE; P9WP28; -.
DR GeneID; 45426232; -.
DR PATRIC; fig|83331.31.peg.2489; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
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; Secreted; Transferase.
FT CHAIN 1..309
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000427024"
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
