Adenylate kinase

Details

Name
Adenylate kinase
Synonyms
  • 2.7.4.3
  • Adenylate monophosphate kinase
  • AK
  • ATP-AMP transphosphorylase
  • ATP:AMP phosphotransferase
  • dnaW
  • plsA
Gene Name
adk
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0002477|Adenylate kinase
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVT
DELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRI
VGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIG
YYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG
Number of residues
214
Molecular Weight
23585.845
Theoretical pI
5.45
GO Classification
Functions
adenylate kinase activity / AMP binding / ATP binding / magnesium ion binding
Processes
ADP biosynthetic process / AMP salvage / nucleotide phosphorylation / phospholipid biosynthetic process / purine ribonucleotide interconversion / RNA biosynthetic process / translation
Components
cytosol
General Function
Magnesium ion binding
Specific Function
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019085|Adenylate kinase (adk)
ATGCGTATCATTCTGCTTGGCGCTCCGGGCGCGGGGAAAGGGACTCAGGCTCAGTTCATC
ATGGAGAAATATGGTATTCCGCAAATCTCCACTGGCGATATGCTGCGTGCTGCGGTCAAA
TCTGGCTCCGAGCTGGGTAAACAAGCAAAAGACATTATGGATGCTGGCAAACTGGTCACC
GACGAACTGGTGATCGCGCTGGTTAAAGAGCGCATTGCTCAGGAAGACTGCCGTAATGGT
TTCCTGTTGGACGGCTTCCCGCGTACCATTCCGCAGGCAGACGCGATGAAAGAAGCGGGC
ATCAATGTTGATTACGTTCTGGAATTCGACGTACCGGACGAACTGATCGTTGACCGTATC
GTCGGTCGCCGCGTTCATGCGCCGTCTGGTCGTGTTTATCACGTTAAATTCAATCCGCCG
AAAGTAGAAGGCAAAGACGACGTTACCGGTGAAGAACTGACTACCCGTAAAGATGATCAG
GAAGAGACCGTACGTAAACGTCTGGTTGAATACCATCAGATGACAGCACCGCTGATCGGC
TACTACTCCAAAGAAGCAGAAGCGGGTAATACCAAATACGCGAAAGTTGACGGCACCAAG
CCGGTTGCTGAAGTTCGCGCTGATCTGGAAAAAATCCTCGGCTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP69441
UniProtKB Entry NameKAD_ECOLI
GenBank Protein ID40904
GenBank Gene IDX03038
General References
  1. Brune M, Schumann R, Wittinghofer F: Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli. Nucleic Acids Res. 1985 Oct 11;13(19):7139-51. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Bardwell JC, Craig EA: Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5177-81. [Article]
  5. Miyamoto K, Nakahigashi K, Nishimura K, Inokuchi H: Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12. J Mol Biol. 1991 Jun 5;219(3):393-8. [Article]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  7. Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608. [Article]
  8. Glaser M, Nulty W, Vagelos PR: Role of adenylate kinase in the regulation of macromolecular biosynthesis in a putative mutant of Escherichia coli defective in membrane phospholipid biosynthesis. J Bacteriol. 1975 Jul;123(1):128-36. [Article]
  9. Esmon BE, Kensil CR, Cheng CH, Glaser M: Genetic analysis of Escherichia coli mutants defective in adenylate kinase and sn-glycerol 3-phosphate acyltransferase. J Bacteriol. 1980 Jan;141(1):405-8. [Article]
  10. Reinstein J, Brune M, Wittinghofer A: Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli. Biochemistry. 1988 Jun 28;27(13):4712-20. [Article]
  11. Reinstein J, Schlichting I, Wittinghofer A: Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli. Biochemistry. 1990 Aug 14;29(32):7451-9. [Article]
  12. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  13. Munier-Lehmann H, Burlacu-Miron S, Craescu CT, Mantsch HH, Schultz CP: A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study. Proteins. 1999 Aug 1;36(2):238-48. [Article]
  14. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  15. Muller CW, Schulz GE: Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. J Mol Biol. 1992 Mar 5;224(1):159-77. [Article]
  16. Muller CW, Schulz GE: Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop. Proteins. 1993 Jan;15(1):42-9. [Article]
  17. Berry MB, Meador B, Bilderback T, Liang P, Glaser M, Phillips GN Jr: The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins. 1994 Jul;19(3):183-98. [Article]
  18. Muller CW, Schlauderer GJ, Reinstein J, Schulz GE: Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure. 1996 Feb 15;4(2):147-56. [Article]
  19. Berry MB, Bae E, Bilderback TR, Glaser M, Phillips GN Jr: Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase. Proteins. 2006 Feb 1;62(2):555-6. [Article]
  20. Schrank TP, Bolen DW, Hilser VJ: Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):16984-9. doi: 10.1073/pnas.0906510106. Epub 2009 Sep 21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01717Bis(Adenosine)-5'-PentaphosphateexperimentalunknownDetails