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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
Eukaryota; Vertebrata
Template P27144 (KAD4_HUMAN)
case <OC:Eukaryota>
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
AK4, AK3L1

Comments [?]

Function Involved 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 RHEA:13749: a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP
EC 2.7.4.10
RHEA:44640: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
EC 2.7.4.6
RHEA:18113: a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP
EC 2.7.4.6
Subunit Monomer.
Subcellular location Mitochondrion matrix.
Domain Consists 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.
Similarity Belongs to the adenylate kinase family. AK3 subfamily.

Keywords [?]


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;
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       NMPbind        
REGION     125     162       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 (KAD); MF_03168 (KAD2); MF_03169 (KAD3); MF_03171 (KAD1); MF_03172 (KCY)
Fusion None