KDGL_SYNY3
ID KDGL_SYNY3 Reviewed; 175 AA.
AC Q55143;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Diacylglycerol kinase {ECO:0000250|UniProtKB:P0ABN1};
DE Short=DAGK {ECO:0000250|UniProtKB:P0ABN1};
DE EC=2.7.1.107 {ECO:0000250|UniProtKB:P0ABN1};
DE AltName: Full=Diglyceride kinase {ECO:0000250|UniProtKB:P0ABN1};
DE Short=DGK {ECO:0000250|UniProtKB:P0ABN1};
GN Name=dgkA; OrderedLocusNames=slr0054;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of sn-l,2-
CC diacylglycerol (DAG) to phosphatidic acid.
CC {ECO:0000250|UniProtKB:P0ABN1}.
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:P0ABN1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0ABN1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the bacterial diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA10279.1; -; Genomic_DNA.
DR PIR; S74361; S74361.
DR AlphaFoldDB; Q55143; -.
DR SMR; Q55143; -.
DR IntAct; Q55143; 1.
DR STRING; 1148.1001137; -.
DR PaxDb; Q55143; -.
DR EnsemblBacteria; BAA10279; BAA10279; BAA10279.
DR KEGG; syn:slr0054; -.
DR eggNOG; COG0818; Bacteria.
DR InParanoid; Q55143; -.
DR OMA; SFRYAAQ; -.
DR PhylomeDB; Q55143; -.
DR Proteomes; UP000001425; 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: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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14265; UDPK_IM_like; 1.
DR Gene3D; 1.10.287.3610; -; 1.
DR InterPro; IPR000829; DAGK.
DR InterPro; IPR036945; DAGK_sf.
DR InterPro; IPR033717; UDPK.
DR PANTHER; PTHR34299; PTHR34299; 1.
DR Pfam; PF01219; DAGK_prokar; 1.
DR PROSITE; PS01069; DAGK_PROKAR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..175
FT /note="Diacylglycerol kinase"
FT /id="PRO_0000195270"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0ABN1"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0ABN1"
SQ SEQUENCE 175 AA; 18248 MW; BF482FEF20C7FF8E CRC64;
MKSVYPMSSP SSAVFADQGL SGKANQTQPP PPLGLVVPAS KPGAKKPLRK NAWQVAPNLL
VSFRYAWAGV SYAFATQRNF RIHTFTGVAV ITAASLLHLE AIAVAVLALT SCLVMILELL
NTALESVVDL TVGQSYHELA KIAKDCAAGA VLLAAIAAVI VGGCLLLPPL LSLMV
