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HAMAP rule MF_03171

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General rule information [?]

Accession MF_03171
Dates 11-MAR-2013 (Created)
1-JUN-2023 (Last updated, Version 13)
Name Adenylate_kinase_AK1
Scope(s) Eukaryota
Metazoa
Template(s) P00568 (KAD1_HUMAN); P00571 (KAD1_PIG); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_03171 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier KAD1
case <OC:Vertebrata>
Protein name RecName: Full=Adenylate kinase isoenzyme 1;
                 Short=AK 1;
                 EC=2.7.4.3;
                 EC=2.7.4.6;
AltName: Full=ATP-AMP transphosphorylase 1;
AltName: Full=ATP:AMP phosphotransferase;
AltName: Full=Adenylate monophosphate kinase;
AltName: Full=Myokinase;
else
Protein name RecName: Full=Adenylate kinase isoenzyme 1;
                 Short=AK 1;
                 EC=2.7.4.3;
AltName: Full=ATP-AMP transphosphorylase 1;
AltName: Full=ATP:AMP phosphotransferase;
AltName: Full=Adenylate monophosphate kinase;
end case
case <OC:Vertebrata>
Gene name Name=AK1;
end case

Comments [?]

case <OC:Vertebrata>
FUNCTIONCatalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
CATALYTIC ACTIVITY Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6;
CATALYTIC ACTIVITY Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
else
FUNCTIONCatalyzes 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.
end case
CATALYTIC ACTIVITY Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
SUBUNITMonomer.
SUBCELLULAR LOCATIONCytoplasm.
DOMAINConsists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
SIMILARITYBelongs to the adenylate kinase family. AK1 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0005737; Cellular component:cytoplasm
GO:0004017; Molecular function:adenylate kinase activity
GO:0006172; Biological process:ADP biosynthetic process
GO:0046033; Biological process:AMP metabolic process
GO:0046034; Biological process:ATP metabolic process

Cross-references [?]

PROSITE PS00113; ADENYLATE_KINASE; 1;
Pfam PF00406; ADK; 1;
PRINTS PR00094; ADENYLTKNASE; 1;
NCBIfam TIGR01360; aden_kin_iso1; 1;

Features [?]

From: KAD1_HUMAN (P00568)
Key From To Description Tag Condition FTGroup
BINDING 18 23 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
G-S-G-K-G-T
BINDING 65 67 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
x-L-V
BINDING 94 97 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
G-Y-P-R
REGION 38 67 /note="NMPbind"
REGION 131 141 /note="LID"
BINDING 39 39 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
[ST]
BINDING 44 44 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
R
BINDING 101 101 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
Q
BINDING 132 132 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R
BINDING 138 138 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
R
BINDING 149 149 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
R
BINDING 177 177 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
case <OC:Mammalia>
MOD_RES 1 1 /note="N-acetylmethionine" acetyl M
end case

Additional information [?]

Size range 193-211 amino acids
Related rules MF_00235
MF_03168
MF_03169
MF_03170
MF_03172
Fusion Nter: None Cter: None



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