Identification
Name:Adenylate kinase
Synonyms:
  • AK
  • ATP-AMP transphosphorylase
Gene Name:adk
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth
Cellular Location:Cytoplasm
SMPDB Pathways:
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+Thumb2 Thumb
Thumb+ThumbThumb+Thumb
Thumb+Thumb2 Thumb
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
ThumbThumb+Adenosine diphosphate+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+Thumb2 Thumb
Thumb+ThumbThumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb2 Thumb
Metabolites:
ECMDB IDNameView
ECMDB00050AdenosineMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01532dATPMetaboCard
ECMDB01245dCDPMetaboCard
ECMDB00998dCTPMetaboCard
ECMDB00905Deoxyadenosine monophosphateMetaboCard
ECMDB01191Deoxyuridine triphosphateMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01440dGTPMetaboCard
ECMDB01274dTDPMetaboCard
ECMDB01000dUDPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03335IDPMetaboCard
ECMDB00189Inosine triphosphateMetaboCard
ECMDB01342Thymidine 5'-triphosphateMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00285Uridine triphosphateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
adenylate kinase activity
ATP binding
binding
catalytic activity
kinase activity
nucleobase, nucleoside, nucleotide kinase activity
nucleoside binding
nucleotide kinase activity
phosphotransferase activity, phosphate group as acceptor
purine nucleoside binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Gene Properties
Blattner:b0474
Gene OrientationClockwise
Centisome Percentage:10.70
Left Sequence End496399
Right Sequence End497043
Gene Sequence:
>645 bp
ATGCGTATCATTCTGCTTGGCGCTCCGGGCGCGGGGAAAGGGACTCAGGCTCAGTTCATC
ATGGAGAAATATGGTATTCCGCAAATCTCCACTGGCGATATGCTGCGTGCTGCGGTCAAA
TCTGGCTCCGAGCTGGGTAAACAAGCAAAAGACATTATGGATGCTGGCAAACTGGTCACC
GACGAACTGGTGATCGCGCTGGTTAAAGAGCGCATTGCTCAGGAAGACTGCCGTAATGGT
TTCCTGTTGGACGGCTTCCCGCGTACCATTCCGCAGGCAGACGCGATGAAAGAAGCGGGC
ATCAATGTTGATTACGTTCTGGAATTCGACGTACCGGACGAACTGATCGTTGACCGTATC
GTCGGTCGCCGCGTTCATGCGCCGTCTGGTCGTGTTTATCACGTTAAATTCAATCCGCCG
AAAGTAGAAGGCAAAGACGACGTTACCGGTGAAGAACTGACTACCCGTAAAGATGATCAG
GAAGAGACCGTACGTAAACGTCTGGTTGAATACCATCAGATGACAGCACCGCTGATCGGC
TACTACTCCAAAGAAGCAGAAGCGGGTAATACCAAATACGCGAAAGTTGACGGCACCAAG
CCGGTTGCTGAAGTTCGCGCTGATCTGGAAAAAATCCTCGGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:214
Protein Molecular Weight:23586
Protein Theoretical pI:5
PDB File:2ECK
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Adenylate kinase
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVT
DELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRI
VGRRVHAPSGRVYHVKFNPPKVEGKDDVTGEELTTRKDDQEETVRKRLVEYHQMTAPLIG
YYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG
References
External Links:
ResourceLink
Uniprot ID:P69441
Uniprot Name:KAD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674613
PDB ID:2ECK
Ecogene ID:EG10032
Ecocyc:EG10032
ColiBase:b0474
Kegg Gene:b0474
EchoBASE ID:EB0031
CCDB:KAD_ECOLI
BacMap:16128458
General Reference:
  • Bardwell, J. C., Craig, E. A. (1987). "Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli." Proc Natl Acad Sci U S A 84:5177-5181. Pubmed: 3299380
  • Berry, M. B., Meador, B., Bilderback, T., Liang, P., Glaser, M., Phillips, G. N. Jr (1994). "The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP." Proteins 19:183-198. Pubmed: 7937733
  • 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
  • Brune, M., Schumann, R., Wittinghofer, F. (1985). "Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli." Nucleic Acids Res 13:7139-7151. Pubmed: 2997739
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Miyamoto, K., Nakahigashi, K., Nishimura, K., Inokuchi, H. (1991). "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12." J Mol Biol 219:393-398. Pubmed: 2051480
  • Muller, C. W., Schlauderer, G. J., Reinstein, J., Schulz, G. E. (1996). "Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding." Structure 4:147-156. Pubmed: 8805521
  • Muller, C. W., Schulz, G. E. (1992). "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 224:159-177. Pubmed: 1548697
  • Muller, C. W., Schulz, G. E. (1993). "Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop." Proteins 15:42-49. Pubmed: 8451239
  • Munier-Lehmann, H., Burlacu-Miron, S., Craescu, C. T., Mantsch, H. H., Schultz, C. P. (1999). "A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study." Proteins 36:238-248. Pubmed: 10398370
  • Reinstein, J., Brune, M., Wittinghofer, A. (1988). "Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli." Biochemistry 27:4712-4720. Pubmed: 2844237
  • Reinstein, J., Schlichting, I., Wittinghofer, A. (1990). "Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli." Biochemistry 29:7451-7459. Pubmed: 2223776
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842