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HAMAP rule MF_03170

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General rule information [?]

Accession MF_03170
Dates 11-MAR-2013 (Created)
1-JUN-2023 (Last updated, Version 14)
Name Adenylate_kinase_AK4
Scope(s) Eukaryota
Vertebrata
Template(s) P27144 (KAD4_HUMAN); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_03170 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier KAD4
Protein name RecName: Full=Adenylate kinase 4, mitochondrial;
                 Short=AK 4;
                 EC=2.7.4.10;
                 EC=2.7.4.6;
AltName: Full=Adenylate kinase 3-like;
AltName: Full=GTP:AMP phosphotransferase AK4;
Gene name Name=AK4; Synonyms=AK3L1;

Comments [?]

FUNCTIONInvolved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity.
CATALYTIC ACTIVITY Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'- diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10;
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;
SUBUNITMonomer.
SUBCELLULAR LOCATIONMitochondrion matrix.
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 GTP/ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP/ATP hydrolysis.
SIMILARITYBelongs to the adenylate kinase family. AK3 subfamily.

Keywords [?]

ATP-binding
GTP-binding
Kinase
Mitochondrion
Nucleotide-binding
Transferase

Gene Ontology [?]

GO:0005759; Cellular component:mitochondrial matrix
GO:0046899; Molecular function:nucleoside triphosphate adenylate kinase activity
GO:0006172; Biological process:ADP biosynthetic process
GO:0046033; Biological process:AMP metabolic process
GO:0046039; Biological process:GTP metabolic process
GO:0046034; Biological process:ATP metabolic process

Cross-references [?]

PROSITE PS00113; ADENYLATE_KINASE; 1;
Pfam PF00406; ADK; 1;
Pfam PF05191; ADK_lid; 1;
PRINTS PR00094; ADENYLTKNASE; 1;
NCBIfam TIGR01351; adk; 1;

Features [?]

From: KAD4_HUMAN (P27144)
Key From To Description Tag Condition FTGroup
BINDING 15 20 /ligand="a ribonucleoside 5'-triphosphate"
/ligand_id="ChEBI:CHEBI:61557"		 G-x-G-K-G-T
BINDING 62 64 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"		 x-L-V
BINDING 89 92 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"		 G-F-P-R
BINDING 135 136 /ligand="a ribonucleoside 5'-triphosphate"
/ligand_id="ChEBI:CHEBI:61557"		 V-Y
REGION 35 64 /note="NMPbind"
REGION 125 162 /note="LID"
BINDING 36 36 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"		 S
BINDING 41 41 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"		 R
BINDING 96 96 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"		 Q
BINDING 126 126 /ligand="a ribonucleoside 5'-triphosphate"
/ligand_id="ChEBI:CHEBI:61557"		 R
BINDING 170 170 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"		 R
BINDING 199 199 /ligand="a ribonucleoside 5'-triphosphate"
/ligand_id="ChEBI:CHEBI:61557"		 T

Additional information [?]

Size range 223-231 amino acids
Related rules MF_00235
MF_03168
MF_03169
MF_03171
MF_03172
Fusion Nter: None Cter: None



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