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MetaCyc Enzyme: lipid kinase

Gene: yegS Accession Numbers: G7123 (MetaCyc), b2086, ECK2082

Species: Escherichia coli K-12 substr. MG1655

Summary:
YegS is a lipid kinase with phosphatidylglycerol kinase activity in vitro [Bakali07]. It shows sequence similarity to a family of eukaryotic non-protein kinases [Bakali06]. The physiological role of YegS is unknown, but a possible role in the response to acid stress has been proposed [Bakali07].

A crystal structure of YegS has been determined at 1.9 Å resolution; the protein shows structural similarity to a family of NAD kinases [Bakali06, Bakali07].

Locations: cytosol

Map Position: [2,166,736 -> 2,167,635]

Molecular Weight of Polypeptide: 32.039 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006911 , DIP:DIP-11889N , EchoBASE:EB4111 , EcoGene:EG14367 , EcoliWiki:b2086 , OU-Microarray:b2086 , PortEco:yegS , Pride:P76407 , Protein Model Portal:P76407 , RefSeq:NP_416590 , RegulonDB:G7123 , SMR:P76407 , String:511145.b2086 , UniProt:P76407

Relationship Links: InterPro:IN-FAMILY:IPR001206 , InterPro:IN-FAMILY:IPR005218 , InterPro:IN-FAMILY:IPR016064 , InterPro:IN-FAMILY:IPR022433 , InterPro:IN-FAMILY:IPR022862 , PDB:Structure:2BON , PDB:Structure:2JGR , Pfam:IN-FAMILY:PF00781 , Prosite:IN-FAMILY:PS50146 , Smart:IN-FAMILY:SM00046

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0046834 - lipid phosphorylation Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Bakali07]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0007205 - protein kinase C-activating G-protein coupled receptor signaling pathway Inferred by computational analysis [GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0008654 - phospholipid biosynthetic process Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0001727 - lipid kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Bakali07]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06]
GO:0003951 - NAD+ kinase activity Inferred by computational analysis [GOA01a]
GO:0004143 - diacylglycerol kinase activity Inferred by computational analysis [GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]
GO:0005829 - cytosol [Bakali07]

MultiFun Terms: metabolism

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Enzymatic reaction of: lipid kinase

Synonyms: phosphatidylglycerol kinase

an L-1-phosphatidyl-glycerol + ATP <=> an L-1-phosphatidylglycerol-phosphate + ADP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

Summary:
Enzymatic activity is absolutely dependent on the presence of a metal ion (Ca2+ or Mg2+); the activity profile with these two metal ions is complex [Bakali07].

Cofactors or Prosthetic Groups: Ca2+ [Bakali07]

Kinetic Parameters:

Substrate
Km (μM)
Citations
an L-1-phosphatidyl-glycerol
700.0
[Bakali07]

pH(opt): 7.5 [Bakali07]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 2 -> 133
[UniProt09]
UniProt: DAGKc;
Amino-Acid-Sites-That-Bind 40
[UniProt10b]
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 66 -> 72
[UniProt10b]
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 95
[UniProt10b]
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 215
[UniProt10]
UniProt: Magnesium; via carbonyl oxygen;
Metal-Binding-Site 218
[UniProt10]
UniProt: Magnesium;
Metal-Binding-Site 220
[UniProt10]
UniProt: Magnesium; via carbonyl oxygen;
Active-Site 271
[UniProt10b]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;

History:
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Bakali06: Bakali MA, Nordlund P, Hallberg BM (2006). "Expression, purification, crystallization and preliminary diffraction studies of the mammalian DAG kinase homologue YegS from Escherichia coli." Acta Crystallograph Sect F Struct Biol Cryst Commun 62(Pt 3);295-7. PMID: 16511327

Bakali07: Bakali MA, Dolores Herman M, Johnson KA, Kelly A, Wieslander A, Hallberg BM, Nordlund P (2007). "Crystal structure of YegS a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site." J Biol Chem 282(27):19644-52. PMID: 17351295

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Serres01: Serres MH, Gopal S, Nahum LA, Liang P, Gaasterland T, Riley M (2001). "A functional update of the Escherichia coli K-12 genome." Genome Biol 2(9);RESEARCH0035. PMID: 11574054

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10b: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Tue May 26, 2015, BIOCYC13B.