Adenylate kinase
Details
- Name
- Adenylate kinase
- Kind
- protein
- Synonyms
- 2.7.4.3
- Adenylate monophosphate kinase
- AK
- ATP-AMP transphosphorylase
- ATP:AMP phosphotransferase
- dnaW
- plsA
- Gene Name
- adk
- UniProtKB Entry
- P69441Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsadenylate kinase activity / AMP binding / ATP binding / magnesium ion bindingProcessesADP biosynthetic process / AMP salvage / nucleotide phosphorylation / phospholipid biosynthetic process / purine ribonucleotide interconversion / RNA biosynthetic process / translationComponentscytosol
- General 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.
- Specific Function
- adenylate kinase activity
- Pfam Domain Function
- ADK_lid (PF05191)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P69441 UniProtKB Entry Name KAD_ECOLI GenBank Protein ID 40904 GenBank Gene ID X03038 PDB ID(s) 1AKE, 1ANK, 1E4V, 1E4Y, 2ECK, 3HPQ, 3HPR, 4AKE, 4X8H, 4X8L, 4X8M, 4X8O KEGG ID ecj:JW0463 NCBI Gene ID 945097 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Bis(Adenosine)-5'-Pentaphosphate experimental unknown target Details