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Overview for MACiE Entry M0290

Version history

General Information

EC Number: 2.7.4.3 (A member of the Transferases, Transferring phosphorus-containing groups, Phosphotransferases with a phosphate group as acceptor)

Enzyme Name: adenylate kinase

Biological Species: Bacillus stearothermophilus (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

Representative PDB Code: 1zio - PHOSPHOTRANSFERASE (Resolution = 1.96 Å).

Catalytic CATH Codes:

  • 3.40.50.300 - P-loop containing nucleotide triphosphate hydrolases

Display structure information

Overall Reaction:

Image of ATP

Image of AMP

right arrow

Image of ADP

ATP
C00002
CHEBI:30616
AMP
C00020
CHEBI:456215
2 ADP
C00008
CHEBI:456216

Overall Comment: Adenylate kinase catalyses the reversible, Mg2+ dependent transfer of the terminal phosphate group of ATP to AMP, releasing two molecules of ADP.


View similar reactions


Stepwise Description of the Reaction

Step 1The terminal phosphate oxyanion of AMP attacks the gamma phosphate of ATP in an associative displacement reaction.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Arg 127 A Side Chain
Arg 129 A Side Chain
Arg 160 A Side Chain

Metal Cofactors for M0290

Type Het group Number Chain
magnesium MG 220 A Overview

References

  1. T. Dahnke et al. (1992), Biochemistry, 31, 6318-6328. Mechanism of adenylate kinase. Structural and functional roles of the conserved arginine-97 and arginine-132.
  2. M. B. Berry et al. (1998), Proteins, 32, 276-288. Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2$DTYPE ROOT:REFERENCES(2):MEDLINE_ID.
    Medline: 9715904
  3. M. Bellinzoni et al. (2006), Protein Sci., 15, 1489-1493. The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer.
    Medline: 16672241
  4. H. Krishnamurthy et al. (2005), Proteins, 58, 88-100. Associative mechanism for phosphoryl transfer: a molecular dynamics simulation of Escherichia coli adenylate kinase complexed with its substrates.
    Medline: 15521058

Homologue information for M0290 (1zio)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0212 nitrogenase
1.18.6.1
1n2c 3.40.50.300
0.00390.1174Compare
M0154 estrone sulfotransferase
2.8.2.4
1hy3 3.40.50.300
00Compare
M0178 H+-transporting two-sector ATPase
3.6.3.14
1e79 3.40.50.300
0.23070.6325Compare
M0074 dethiobiotin synthase
6.3.3.3
1bs1 3.40.50.300
0.05260.0208Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.40.50.300


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
nucleotide binding (molecular function)
adenylate kinase activity (molecular function)
ATP binding (molecular function)
cytoplasm (cellular component)
nucleobase-containing compound metabolic process (biological process)
nucleotide biosynthetic process (biological process)
kinase activity (molecular function)
phosphorylation (biological process)
transferase activity (molecular function)
phosphotransferase activity, phosphate group as acceptor (molecular function)
nucleotide kinase activity (molecular function)
nucleobase-containing compound kinase activity (molecular function)
metal ion binding (molecular function)
nucleotide phosphorylation (biological process)
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