UniProtKB - P0ABN1 (KDGL_ECOLI)
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>sp|P0ABN1|KDGL_ECOLI Diacylglycerol kinase OS=Escherichia coli (strain K12) OX=83333 GN=dgkA PE=1 SV=2 MANNTTGFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIACWLDVDAITRVLLI SSVMLVMIVEILNSAIEAVVDRIGSEYHELSGRAKDMGSAAVLIAIIVAVITWCILLWSH FGCommunity curation ()Add a publicationFeedback
Protein
Diacylglycerol kinase
Gene
dgkA
Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid (PubMed:218816, PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:2828054, PubMed:9305868). Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis (PubMed:217867, PubMed:6305970). In vitro, phosphorylates various substrates, including sn-1,2-dioleoylglycerol, sn-1,2-dioctanoylglycerol, sn-1,2-dipalmitoylglycerol, sn-1,2-dipalmitate and ceramide (PubMed:218816, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). Catalyzes direct phosphoryl transfer from Mg-ATP to diacylglycerol and does not form an enzyme-phosphate intermediate (PubMed:9305868).10 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.7"Diglyceride kinase mutants of Escherichia coli: inner membrane association of 1,2-diglyceride and its relation to synthesis of membrane-derived oligosaccharides."
Raetz C.R., Newman K.F.
J. Bacteriol. 137:860-868(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Diglyceride kinase from Escherichia coli. Modulation of enzyme activity by glycosphingolipids."
Bohnenberger E., Sandermann H. Jr.
Biochim. Biophys. Acta 685:44-50(1982) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.10"Lipid dependence of diacylglycerol kinase from Escherichia coli."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 132:645-650(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.11"Appearance of monoglyceride and triglyceride in the cell envelope of Escherichia coli mutants defective in diglyceride kinase."
Rotering H., Raetz C.R.
J. Biol. Chem. 258:8068-8073(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE. - Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:15062-15069(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer."
Badola P., Sanders C.R. II
J. Biol. Chem. 272:24176-24182(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVITY REGULATION.
Miscellaneous
This small kinase has long served as a model for investigating membrane protein enzymology, folding, assembly and stability.Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a 1,2-diacyl-sn-glycerolEC:2.7.1.107
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Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Diglyceride kinase from Escherichia coli. Modulation of enzyme activity by glycosphingolipids."
Bohnenberger E., Sandermann H. Jr.
Biochim. Biophys. Acta 685:44-50(1982) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.10"Lipid dependence of diacylglycerol kinase from Escherichia coli."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 132:645-650(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer."
Badola P., Sanders C.R. II
J. Biol. Chem. 272:24176-24182(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVITY REGULATION.
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Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Diglyceride kinase from Escherichia coli. Modulation of enzyme activity by glycosphingolipids."
Bohnenberger E., Sandermann H. Jr.
Biochim. Biophys. Acta 685:44-50(1982) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.10"Lipid dependence of diacylglycerol kinase from Escherichia coli."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 132:645-650(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer."
Badola P., Sanders C.R. II
J. Biol. Chem. 272:24176-24182(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVITY REGULATION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.9"Diglyceride kinase from Escherichia coli. Modulation of enzyme activity by glycosphingolipids."
Bohnenberger E., Sandermann H. Jr.
Biochim. Biophys. Acta 685:44-50(1982) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.10"Lipid dependence of diacylglycerol kinase from Escherichia coli."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 132:645-650(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer."
Badola P., Sanders C.R. II
J. Biol. Chem. 272:24176-24182(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVITY REGULATION.
Source: Rhea- Search for this reaction in UniProtKB.
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a 1,2-diacyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=a 1,2-diacyl-sn-glycero-3-phosphate- Search proteins in UniProtKB for this molecule.
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- 1,2-di-(9Z-octadecenoyl)-sn-glycerol
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Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:15062-15069(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:15062-15069(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
Source: Rhea- Search for this reaction in UniProtKB.
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1,2-di-(9Z-octadecenoyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mg2+
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Manual assertion based on experiment ini
- Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Manual assertion based on experiment ini
- Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Requires a lipid activator for activity. Activation is observed with cardiolipin and a large number of phospholipids, sulfolipids, neutral lipids, fatty acids, alkylglycosides or detergents (PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). A lipid cofactor-induced conformational change may occur as part of the activation process (PubMed:3021764). Requires a second divalent cation in addition to Mg2+-ATP (PubMed:3009449). Inhibited by the tetraphosphate-linked ATP-DAG bisubstrate analog (PubMed:9305868).7 Publications
Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.9"Diglyceride kinase from Escherichia coli. Modulation of enzyme activity by glycosphingolipids."
Bohnenberger E., Sandermann H. Jr.
Biochim. Biophys. Acta 685:44-50(1982) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.10"Lipid dependence of diacylglycerol kinase from Escherichia coli."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 132:645-650(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:15062-15069(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer."
Badola P., Sanders C.R. II
J. Biol. Chem. 272:24176-24182(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVITY REGULATION.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=62 µM for sn-1,2-dipalmitate1 Publication
Manual assertion based on experiment ini
- Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=230 µM for ceramide1 Publication
Manual assertion based on experiment ini
- Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=1400 µM for ATP1 Publication
Manual assertion based on experiment ini
- Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=300 µM for ATP1 Publication
Manual assertion based on experiment ini
- Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=120 µM for ATP1 Publication
Manual assertion based on experiment ini
- Ref.18"Active sites of diacylglycerol kinase from Escherichia coli are shared between subunits."
Lau F.W., Chen X., Bowie J.U.
Biochemistry 38:5521-5527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-15; GLU-70; ASN-73; GLU-77; LYS-95 AND ASP-96.
- Vmax=10.4 µmol/min/mg enzyme1 Publication
Manual assertion based on experiment ini
- Ref.12"sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence."
Walsh J.P., Bell R.M.
J. Biol. Chem. 261:6239-6247(1986) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=48 µmol/min/mg enzyme with DAG as substrate1 Publication
Manual assertion based on experiment ini
- Ref.18"Active sites of diacylglycerol kinase from Escherichia coli are shared between subunits."
Lau F.W., Chen X., Bowie J.U.
Biochemistry 38:5521-5527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-15; GLU-70; ASN-73; GLU-77; LYS-95 AND ASP-96.
pH dependencei
Optimum pH is 6.3-8.3.1 Publication
Manual assertion based on experiment ini
- Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Temperature dependencei
Apoprotein in organic solution has an unusual stability towards heating to 100 degrees Celsius.1 Publication
Manual assertion based on experiment ini
- Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 10 | ATP2 Publications <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 10 | Substrate3 Publications Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 17 | ATP2 Publications Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 29 | Divalent metal cation6 Publications Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 29 | ATP2 Publications Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 56 | Substrate7 Publications Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 70 | Proton acceptor1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 70 | Substrate5 Publications Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 77 | Divalent metal cation6 Publications Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 77 | ATP2 Publications Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 99 | Substrate5 Publications Manual assertion inferred by curator fromi
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 86 – 88 | ATP2 Publications Manual assertion inferred by curator fromi
| 3 | |
| Nucleotide bindingi | 95 – 96 | ATP2 Publications Manual assertion inferred by curator fromi
| 2 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- diacylglycerol kinase activity Source: EcoCyc
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.8"Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme."
Bohnenberger E., Sandermann H. Jr.
Eur. J. Biochem. 94:401-407(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.14"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."
Russ E., Kaiser U., Sandermann H. Jr.
Eur. J. Biochem. 171:335-342(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.23"Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase."
Van Horn W.D., Kim H.J., Ellis C.D., Hadziselimovic A., Sulistijo E.S., Karra M.D., Tian C., Sonnichsen F.D., Sanders C.R.
Science 324:1726-1729(2009) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 2-122, SUBUNIT.
- metal ion binding Source: EcoCycInferred from direct assayi
- Ref.24"Crystal structure of the integral membrane diacylglycerol kinase."
Li D., Lyons J.A., Pye V.E., Vogeley L., Aragao D., Kenyon C.P., Shah S.T., Doherty C., Aherne M., Caffrey M.
Nature 497:521-524(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-122 OF APOENZYME AND IN COMPLEX WITH ZINC AND 7.8 MONOACYLGLYCEROL, SUBUNIT, DOMAIN.
GO - Biological processi
- phosphatidic acid biosynthetic process Source: EcoCyc
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.6"Neutral lipid accumulation in the membranes of Escherichia coli mutants lacking diglyceride kinase."
Raetz C.R., Newman K.F.
J. Biol. Chem. 253:3882-3887(1978) [PubMed] [Europe PMC] [Abstract]Cited for: DISRUPTION PHENOTYPE.
- response to UV Source: EcoCycInferred from mutant phenotypei
- "Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database."
Sargentini N.J., Gularte N.P., Hudman D.A.
Mutat. Res. 793:1-14(2016) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Kinase, Transferase |
| Biological process | Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism |
| Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:DIACYLGLYKIN-MONOMER MetaCyc:DIACYLGLYKIN-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.1.107, 2026 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001806 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Diacylglycerol kinase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: DAGK1 Publication Manual assertion based on opinion ini
Alternative name(s): Diglyceride kinase1 Publication Manual assertion based on opinion ini
Short name: DGKCurated |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:dgkA1 Publication Manual assertion based on opinion ini
Synonyms:dgk1 Publication Manual assertion based on opinion ini
Ordered Locus Names:b4042, JW4002 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell inner membrane 4 Publications
Manual assertion based on experiment ini
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION. - Ref.7"Diglyceride kinase mutants of Escherichia coli: inner membrane association of 1,2-diglyceride and its relation to synthesis of membrane-derived oligosaccharides."
Raetz C.R., Newman K.F.
J. Bacteriol. 137:860-868(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.15"Membrane topology of Escherichia coli diacylglycerol kinase."
Smith R.L., O'Toole J.F., Maguire M.E., Sanders C.R. II
J. Bacteriol. 176:5459-5465(1994) [PubMed] [Europe PMC] [Abstract]Cited for: TOPOLOGY, SUBCELLULAR LOCATION. - Ref.21"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]Cited for: TOPOLOGY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.
Manual assertion based on experiment ini
- Ref.15"Membrane topology of Escherichia coli diacylglycerol kinase."
Smith R.L., O'Toole J.F., Maguire M.E., Sanders C.R. II
J. Bacteriol. 176:5459-5465(1994) [PubMed] [Europe PMC] [Abstract]Cited for: TOPOLOGY, SUBCELLULAR LOCATION.
- Cell inner membrane 4 Publications
Plasma Membrane
- plasma membrane Source: EcoCycInferred from direct assayi
- Ref.21"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]Cited for: TOPOLOGY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION. - "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS."
Zhang N., Chen R., Young N., Wishart D., Winter P., Weiner J.H., Li L.
Proteomics 7:484-493(2007) [PubMed] [Europe PMC] [Abstract] - "Partial purification and properties of diglyceride kinase from Escherichia coli."
Schneider E.G., Kennedy E.P.
Biochim Biophys Acta 441:201-212(1976) [PubMed] [Europe PMC] [Abstract] - Ref.7"Diglyceride kinase mutants of Escherichia coli: inner membrane association of 1,2-diglyceride and its relation to synthesis of membrane-derived oligosaccharides."
Raetz C.R., Newman K.F.
J. Bacteriol. 137:860-868(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
- plasma membrane Source: EcoCycInferred from direct assayi
Other locations
- integral component of membrane Source: UniProtKB-KW
- membrane Source: EcoCycInferred from direct assayi
- Ref.5"sn-1,2-Diacylglycerol kinase of Escherichia coli. Purification, reconstitution, and partial amino- and carboxyl-terminal analysis."
Loomis C.R., Walsh J.P., Bell R.M.
J. Biol. Chem. 260:4091-4097(1985) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-3 AND 121, IDENTIFICATION OF PROTEIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION.
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 2 – 31 | Cytoplasmic1 Publication Manual assertion based on experiment ini
| 30 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 32 – 48 | Helical2 Publications Manual assertion inferred by curator fromi
| 17 | |
| Topological domaini | 49 – 51 | Periplasmic2 Publications Manual assertion inferred by curator fromi
| 3 | |
| Transmembranei | 52 – 69 | Helical2 Publications Manual assertion inferred by curator fromi
| 18 | |
| Topological domaini | 70 – 95 | Cytoplasmic1 Publication Manual assertion inferred by curator fromi
| 26 | |
| Transmembranei | 96 – 119 | Helical1 Publication Manual assertion inferred by curator fromi
| 24 | |
| Topological domaini | 120 – 122 | Periplasmic2 Publications Manual assertion based on experiment ini
| 3 |
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Mutant lacking this gene accumulates substantial amounts of diglyceride in the cytoplasmic membrane (PubMed:206553, PubMed:217867). Mutant also accumulates monoglyceride and triglyceride. Monoglyceride accumulates predominantly in the outer membrane, while triglyceride builds up together with diglyceride in the cytoplasmic membrane (PubMed:6305970).3 Publications
Manual assertion based on experiment ini
- Ref.6"Neutral lipid accumulation in the membranes of Escherichia coli mutants lacking diglyceride kinase."
Raetz C.R., Newman K.F.
J. Biol. Chem. 253:3882-3887(1978) [PubMed] [Europe PMC] [Abstract]Cited for: DISRUPTION PHENOTYPE. - Ref.7"Diglyceride kinase mutants of Escherichia coli: inner membrane association of 1,2-diglyceride and its relation to synthesis of membrane-derived oligosaccharides."
Raetz C.R., Newman K.F.
J. Bacteriol. 137:860-868(1979) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. - Ref.11"Appearance of monoglyceride and triglyceride in the cell envelope of Escherichia coli mutants defective in diglyceride kinase."
Rotering H., Raetz C.R.
J. Biol. Chem. 258:8068-8073(1983) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 15 | A → Q: 49% of wild-type specific activity. Inactivates wild-type subunits; when associated with S-73. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 19 | W → L: 60% of wild-type activity. 41% of wild-type activity; when associated with L-26. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 26 | W → L: 23% of wild-type activity. 41% of wild-type activity; when associated with L-19. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 31 | A → L: 93% decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 70 | E → A, D or Q: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 70 | E → C: 50% of wild-type specific activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 73 | N → A, Q or D: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 73 | N → S: 51% of wild-type specific activity. Inactivates wild-type subunits; when associated with Q-15. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 77 | E → L: 51% of wild-type specific activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 84 | G → P: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 95 | K → L: 54% of wild-type specific activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 96 | D → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 96 | D → E: 76% decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 96 | D → N: 27% of wild-type specific activity. Inactivates wild-type subunits. Almost no change in activity. 2 Publications Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000195260 | 2 – 122 | Diacylglycerol kinaseAdd BLAST | 121 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P0ABN1 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0ABN1 |
PRoteomics IDEntifications database More...PRIDEi | P0ABN1 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Expression is activated by the two-component system BasRS. Repressed by sigma-E factor.1 Publication
Manual assertion based on experiment ini
- Ref.22"Antagonistic regulation of dgkA and plsB genes of phospholipid synthesis by multiple stress responses in Escherichia coli."
Wahl A., My L., Dumoulin R., Sturgis J.N., Bouveret E.
Mol. Microbiol. 80:1260-1275(2011) [PubMed] [Europe PMC] [Abstract]Cited for: TRANSCRIPTIONAL REGULATION.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homotrimer.
5 PublicationsManual assertion based on experiment ini
- Ref.16"Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein."
Vinogradova O., Badola P., Czerski L., Soennichsen F.D., Sanders C.R. II
Biophys. J. 72:2688-2701(1997) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT. - Ref.23"Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase."
Van Horn W.D., Kim H.J., Ellis C.D., Hadziselimovic A., Sulistijo E.S., Karra M.D., Tian C., Sonnichsen F.D., Sanders C.R.
Science 324:1726-1729(2009) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 2-122, SUBUNIT. - Ref.24"Crystal structure of the integral membrane diacylglycerol kinase."
Li D., Lyons J.A., Pye V.E., Vogeley L., Aragao D., Kenyon C.P., Shah S.T., Doherty C., Aherne M., Caffrey M.
Nature 497:521-524(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-122 OF APOENZYME AND IN COMPLEX WITH ZINC AND 7.8 MONOACYLGLYCEROL, SUBUNIT, DOMAIN. - Ref.27"Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination."
Boland C., Li D., Shah S.T.A., Haberstock S., Dotsch V., Bernhard F., Caffrey M.
Cell. Mol. Life Sci. 71:4895-4910(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-122 IN COMPLEXES WITH ZINC AND 7.8 MONOACYLGLYCEROL, SUBUNIT. - Ref.29"Ternary structure reveals mechanism of a membrane diacylglycerol kinase."
Li D., Stansfeld P.J., Sansom M.S.P., Keogh A., Vogeley L., Howe N., Lyons J.A., Aragao D., Fromme P., Fromme R., Basu S., Grotjohann I., Kupitz C., Rendek K., Weierstall U., Zatsepin N.A., Cherezov V., Liu W. , Bandaru S., English N.J., Gati C., Barty A., Yefanov O., Chapman H.N., Diederichs K., Messerschmidt M., Boutet S., Williams G.J., Marvin Seibert M., Caffrey M.
Nat. Commun. 6:10140-10140(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 2-122 IN COMPLEXES WITH ZINC; MONOACYLGLYCEROLS AND ATP ANALOG, REACTION MECHANISM, SUBUNIT, DOMAIN, ACTIVE SITE, MUTAGENESIS OF ALA-31; GLU-70; ASN-73; GLY-84 AND ASP-96.
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.23"Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase."
Van Horn W.D., Kim H.J., Ellis C.D., Hadziselimovic A., Sulistijo E.S., Karra M.D., Tian C., Sonnichsen F.D., Sanders C.R.
Science 324:1726-1729(2009) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 2-122, SUBUNIT.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4261719, 281 interactors 852837, 2 interactors |
Database of interacting proteins More...DIPi | DIP-60228N |
STRING: functional protein association networks More...STRINGi | 511145.b4042 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 8 – 28 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| Helixi | 30 – 48 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 53 – 83 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 31 | |
| Helixi | 89 – 120 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 32 |
3D structure databases
Biological Magnetic Resonance Data Bank More...BMRBi | P0ABN1 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0ABN1 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0ABN1 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 14 – 19 | Substrate binding4 Publications Manual assertion inferred by curator fromi
| 6 | |
| Regioni | 23 – 26 | Substrate binding5 Publications Manual assertion inferred by curator fromi
| 4 | |
| Regioni | 31 – 35 | Substrate binding6 Publications Manual assertion inferred by curator fromi
| 5 | |
| Regioni | 48 – 51 | Substrate binding6 Publications Manual assertion inferred by curator fromi
| 4 | |
| Regioni | 113 – 118 | Substrate binding7 Publications Manual assertion inferred by curator fromi
| 6 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Contains three transmembrane helices and a N-terminal amphiphilic helix located on the cytoplasmic surface (PubMed:23676677, PubMed:26673816). Residues from different subunits participate in forming the active site (PubMed:10220339, PubMed:23676677). Contains three catalytic and substrate-binding sites centred about the membrane/cytosol interface (PubMed:26673816). The gamma-phosphate of the ATP is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane (PubMed:26673816).3 Publications
Manual assertion based on experiment ini
- Ref.18"Active sites of diacylglycerol kinase from Escherichia coli are shared between subunits."
Lau F.W., Chen X., Bowie J.U.
Biochemistry 38:5521-5527(1999) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-15; GLU-70; ASN-73; GLU-77; LYS-95 AND ASP-96. - Ref.24"Crystal structure of the integral membrane diacylglycerol kinase."
Li D., Lyons J.A., Pye V.E., Vogeley L., Aragao D., Kenyon C.P., Shah S.T., Doherty C., Aherne M., Caffrey M.
Nature 497:521-524(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-122 OF APOENZYME AND IN COMPLEX WITH ZINC AND 7.8 MONOACYLGLYCEROL, SUBUNIT, DOMAIN. - Ref.29"Ternary structure reveals mechanism of a membrane diacylglycerol kinase."
Li D., Stansfeld P.J., Sansom M.S.P., Keogh A., Vogeley L., Howe N., Lyons J.A., Aragao D., Fromme P., Fromme R., Basu S., Grotjohann I., Kupitz C., Rendek K., Weierstall U., Zatsepin N.A., Cherezov V., Liu W. , Bandaru S., English N.J., Gati C., Barty A., Yefanov O., Chapman H.N., Diederichs K., Messerschmidt M., Boutet S., Williams G.J., Marvin Seibert M., Caffrey M.
Nat. Commun. 6:10140-10140(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 2-122 IN COMPLEXES WITH ZINC; MONOACYLGLYCEROLS AND ATP ANALOG, REACTION MECHANISM, SUBUNIT, DOMAIN, ACTIVE SITE, MUTAGENESIS OF ALA-31; GLU-70; ASN-73; GLY-84 AND ASP-96.
The presence of Trp residues has a clear effect on thermal stability. Of the mutants containing a single Trp residue, only that containing Trp-113 was found to give active protein.1 Publication
Manual assertion based on experiment ini
- Ref.20"The role of tryptophan residues in an integral membrane protein: diacylglycerol kinase."
Clark E.H., East J.M., Lee A.G.
Biochemistry 42:11065-11073(2003) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN, MUTAGENESIS OF TRP-19 AND TRP-26.
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the bacterial diacylglycerol kinase family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0818, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_112343_3_1_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0ABN1 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0ABN1 |
Family and domain databases
Conserved Domains Database More...CDDi | cd14264, DAGK_IM, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.3830.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000829, DAGK IPR033718, DAGK_prok IPR036945, DAGK_sf |
The PANTHER Classification System More...PANTHERi | PTHR34299, PTHR34299, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01219, DAGK_prokar, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01069, DAGK_PROKAR, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P0ABN1-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MANNTTGFTR IIKAAGYSWK GLRAAWINEA AFRQEGVAVL LAVVIACWLD
60 70 80 90 100
VDAITRVLLI SSVMLVMIVE ILNSAIEAVV DRIGSEYHEL SGRAKDMGSA
110 120
AVLIAIIVAV ITWCILLWSH FG
Length:122
Mass (Da):13,245
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iD5B4F86925FA6A17
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | K00127 Genomic DNA Translation: AAA24394.1 U00006 Genomic DNA Translation: AAC43136.1 U00096 Genomic DNA Translation: AAC77012.1 AP009048 Genomic DNA Translation: BAE78044.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A00667, KIECDG |
NCBI Reference Sequences More...RefSeqi | NP_418466.1, NC_000913.3 WP_000002907.1, NZ_STEB01000022.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC77012; AAC77012; b4042 BAE78044; BAE78044; BAE78044 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 58462962 948543 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW4002 eco:b4042 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2666 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P0ABN1 | Diacylglycerol kinase | 122 | UniRef100_P0ABN3 | |||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| +153 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P0ABN1 | Diacylglycerol kinase | 122 | UniRef90_P0ABN3 | |||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| +322 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P0ABN1 | Diacylglycerol kinase | 122 | UniRef50_P0ABN3 | |||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| Diacylglycerol kinase | 122 | |||||
| +390 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K00127 Genomic DNA Translation: AAA24394.1 U00006 Genomic DNA Translation: AAC43136.1 U00096 Genomic DNA Translation: AAC77012.1 AP009048 Genomic DNA Translation: BAE78044.1 |
| PIRi | A00667, KIECDG |
| RefSeqi | NP_418466.1, NC_000913.3 WP_000002907.1, NZ_STEB01000022.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2KDC | NMR | - | A/B/C | 2-122 | [»] | |
| 3ZE3 | X-ray | 2.05 | A/B/C/D/E/F | 2-122 | [»] | |
| 3ZE4 | X-ray | 3.70 | A/B/C | 2-122 | [»] | |
| 3ZE5 | X-ray | 3.10 | A/B/C | 2-122 | [»] | |
| 4BPD | X-ray | 3.30 | A/B/C/D/E/F | 2-122 | [»] | |
| 4BRB | X-ray | 2.55 | A/B/C/D/E/F | 2-122 | [»] | |
| 4BRR | X-ray | 2.44 | A/B/C/D/E/F | 2-122 | [»] | |
| 4CJZ | X-ray | 3.25 | A/B/C | 2-122 | [»] | |
| 4CK0 | X-ray | 2.92 | A/B/C | 2-122 | [»] | |
| 4D2E | X-ray | 2.28 | A/B/C/D/E/F | 2-122 | [»] | |
| 4UP6 | X-ray | 3.80 | A/B/C | 2-122 | [»] | |
| 4UXW | X-ray | 3.15 | A/B/C | 2-122 | [»] | |
| 4UXX | X-ray | 2.70 | A/B/C | 2-122 | [»] | |
| 4UXZ | X-ray | 2.18 | A/B/C/D/E/F | 2-122 | [»] | |
| 4UYO | X-ray | 2.18 | A/B/C/D/E/F | 2-122 | [»] | |
| 5D56 | X-ray | 2.80 | A/B/C/D/E/F | 2-122 | [»] | |
| 5D57 | X-ray | 2.80 | A/B/C/D/E/F | 2-122 | [»] | |
| 5D6I | X-ray | 3.09 | A/B/C | 2-122 | [»] | |
| 5DWK | X-ray | 2.60 | A/B/C/D/E/F | 2-122 | [»] | |
| BMRBi | P0ABN1 | |||||
| SMRi | P0ABN1 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4261719, 281 interactors 852837, 2 interactors |
| DIPi | DIP-60228N |
| STRINGi | 511145.b4042 |
Chemistry databases
| SwissLipidsi | SLP:000001806 |
Proteomic databases
| jPOSTi | P0ABN1 |
| PaxDbi | P0ABN1 |
| PRIDEi | P0ABN1 |
Genome annotation databases
| EnsemblBacteriai | AAC77012; AAC77012; b4042 BAE78044; BAE78044; BAE78044 |
| GeneIDi | 58462962 948543 |
| KEGGi | ecj:JW4002 eco:b4042 |
| PATRICi | fig|1411691.4.peg.2666 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0220 |
Phylogenomic databases
| eggNOGi | COG0818, Bacteria |
| HOGENOMi | CLU_112343_3_1_6 |
| InParanoidi | P0ABN1 |
| PhylomeDBi | P0ABN1 |
Enzyme and pathway databases
| BioCyci | EcoCyc:DIACYLGLYKIN-MONOMER MetaCyc:DIACYLGLYKIN-MONOMER |
| BRENDAi | 2.7.1.107, 2026 |
Miscellaneous databases
| EvolutionaryTracei | P0ABN1 |
Protein Ontology More...PROi | PR:P0ABN1 |
Family and domain databases
| CDDi | cd14264, DAGK_IM, 1 hit |
| Gene3Di | 1.10.3830.10, 1 hit |
| InterProi | View protein in InterPro IPR000829, DAGK IPR033718, DAGK_prok IPR036945, DAGK_sf |
| PANTHERi | PTHR34299, PTHR34299, 1 hit |
| Pfami | View protein in Pfam PF01219, DAGK_prokar, 1 hit |
| PROSITEi | View protein in PROSITE PS01069, DAGK_PROKAR, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | KDGL_ECOLI | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P0ABN1Primary (citable) accession number: P0ABN1 Secondary accession number(s): P00556, Q2M6R2 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | April 7, 2021 | |
| This is version 120 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
