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HAMAP rule MF_00235

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General rule information [?]

Accession MF_00235
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 47)
Name Adenylate_kinase_Adk
Scope
Bacteria
Archaea
Templates P69441 (KAD_ECOLI); P9WKF5 (KAD_MYCTU); P16304 (KAD_BACSU); P27142 (KAD_GEOSE); P84139 (KAD_SPOGL): [Recover all]
case <OC:Bacteria> or <OC:Archaea>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
KAD
Protein name
RecName: Full=Adenylate kinase;
Short=AK;
EC 2.7.4.3;
AltName: Full=ATP-AMP transphosphorylase;
AltName: Full=ATP:AMP phosphotransferase;
AltName: Full=Adenylate monophosphate kinase;
Gene name
adk

Comments [?]

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.
Catalytic activity RHEA:12973: AMP + ATP = 2 ADP
EC 2.7.4.3
Pathway Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subunit Monomer.
Subcellular location Cytoplasm.
case <FTGroup:1>
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 ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
else
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 ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
end case
Similarity Belongs to the adenylate kinase family.

Keywords [?]

ATP-binding
Cytoplasm
Transferase
Kinase
Nucleotide-binding
Nucleotide biosynthesis
case <FTGroup:1>
Metal-binding
Zinc
end case

Gene Ontology [?]

GO:0004017; Molecular function: adenylate kinase activity.
GO:0005524; Molecular function: ATP binding.
case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
GO:0009165; Biological process: nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF00406; ADK; 1;
PF05191; ADK_lid; 0-1;
PRINTS PR00094; ADENYLTKNASE; 1;
NCBIfam TIGR01351; Adk; 1;
PROSITE PS00113; ADENYLATE_KINASE; 1;

Features [?]

From: KAD_ECOLI (P69441)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     10     15       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     [GA]-x-G-K-[GST]-[ST]  
BINDING     57     59       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     x-[LYF]-[VILM]  
BINDING     85     88       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     G-[FY]-P-R  
BINDING (Optional)     132     133       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     [STVI]-[YFH]  
REGION     30     59       NMP        
REGION     122     159       LID        
BINDING     31     31       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     [TS]  
BINDING     36     36       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     R  
BINDING     92     92       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     Q  
BINDING     123     123       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     R  
BINDING     156     156       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     R  
BINDING     167     167       /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215     R  
BINDING     200     200       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616        
From: KAD_BACSU (P16304)
BINDING (Optional)     130     130       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural     C   1
BINDING (Optional)     133     133       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural     C   1
BINDING (Optional)     150     150       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural     C   1
BINDING (Optional)     153     153       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural     [CD]   1

Additional information [?]

Size range 181-253 amino acids
Related rules MF_03168 (KAD2 supersedes the current rule); MF_03169 (KAD3 supersedes the current rule); MF_03170 (KAD4 supersedes the current rule); MF_03171 (KAD1 supersedes the current rule); MF_03172 (KCY supersedes the current rule)
Fusion None


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