Lipid kinase yegS (P76407)

Identification
Name:Lipid kinase yegS
Synonyms:Not Available
Gene Name:yegS
Enzyme Class:Not Available
Biological Properties
General Function:Involved in diacylglycerol kinase activity
Specific Function:In vitro phosphorylates phosphatidylglycerol but not diacylglycerol; the in vivo substrate is unknown
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Reactions:
1.0an L-1-phosphatidyl-glycerol+1.0Thumb → 1.0an L-1-phosphatidylglycerol-phosphate+1.0Thumb+1.0Thumb
1.0an L-1-phosphatidyl-glycerol + 1.0Adenosine triphosphate → 1.0an L-1-phosphatidylglycerol-phosphate + 1.0ADP + 1.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
diacylglycerol kinase activity
ion binding
kinase activity
lipid kinase activity
metal ion binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
cell surface receptor linked signaling pathway
G-protein coupled receptor protein signaling pathway
signaling
signaling pathway
Gene Properties
Blattner:b2086
Gene OrientationClockwise
Centisome Percentage:46.70
Left Sequence End2166736
Right Sequence End2167635
Gene Sequence:
>900 bp
ATGAAGCGTGAAGAAATCGCTGATCTGATGGCGTTTGTCGTCGTTGCAGAGGAGCGTAGC
TTCACTCGTGCAGCAGCCCGCCTGAGCATGGCGCAGTCAGCTTTAAGCCAGATAGTGCGT
CGTATAGAAGAACGATTGGGATTGCGGCTTCTGACGCGAACCACGCGCAGCGTTGTTCCA
ACTGAAGCGGGCGAGCATCTTTTGTCTGTTCTTGGCCCTATGTTGCATGACATAGATTCA
GCCATGGCATCCCTGAGCGATCTGCAGAACCGCCCATCCGGGACAATACGTATTACTACT
GTAGAACATGCAGCAAAAACGATATTGTTACCAGCAATGCGCACATTCCTGAAATCGCAT
CCTGAAATTGATATTCAGCTCACCATTGATTATGGTTTGACCGATGTCGTTTCTGAACGT
TTTGATGCAGGCGTCCGTCTGGGTGGGGAGATGGATAAAGATATGATCGCCATTCGAATC
GGGCCAGATATACCAATGGCTATTGTTGGCTCACCGGATTATTTTTCTCGCCGAAGTGTT
CCAACGTCAGTGTCACAATTAATAGATCATCAGGCAATTAATTTGTATCTTCCCACATCG
GGTACAGCAAATCGCTGGAGATTAATACGCGGTGGACGTGAAGTTCGTGTTCGCATGGAA
GGTCAGCTTTTACTGAATACGATAGACCTGATCATTGATGCTGCAATTGATGGGCATGGA
TTGGCGTATCTACCTTATGATCAGGTTGAGCGGGCTATTAAAGAAAAAAAACTGATACGT
GTTTTGGATAAATTCACACCAGATTTACCCGGTTATCACCTGTACTATCCACACCGTCGA
CATGCTGGCTCGGCATTCTCATTATTTATAGATAGGCTGAAGTATAAAGGTGCTGTTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:299
Protein Molecular Weight:32038
Protein Theoretical pI:4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Lipid kinase yegS
MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKFGVAT
VIAGGGDGTINEVSTALIQCEGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGD
AIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGSVSYIIHGLMRMDTLQPDRC
EIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLK
SDEDNPNIIEGASSWFDIQAPHDITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR
References
External Links:
ResourceLink
Uniprot ID:P76407
Uniprot Name:YEGS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742185
Ecogene ID:EG14367
Ecocyc:EG14367
ColiBase:b2086
Kegg Gene:b2086
EchoBASE ID:EB4111
CCDB:YEGS_ECOLI
BacMap:16130026
General Reference:
  • Bakali, H. M., Herman, M. D., Johnson, K. A., Kelly, A. A., Wieslander, A., Hallberg, B. M., Nordlund, P. (2007). "Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site." J Biol Chem 282:19644-19652. Pubmed: 17351295
  • Bakali, M. A., Nordlund, P., Hallberg, B. M. (2006). "Expression, purification, crystallization and preliminary diffraction studies of the mammalian DAG kinase homologue YegS from Escherichia coli." Acta Crystallogr Sect F Struct Biol Cryst Commun 62:295-297. Pubmed: 16511327
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040