HAMAP rule MF_00235
General rule information
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Accession | MF_00235 |
Dates | 1-JUN-2001 (Created) 19-NOV-2022 (Last updated, Version 46) |
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
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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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
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case <FTGroup:1>
end case
Gene Ontology
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GO:0004017; Molecular function: adenylate kinase activity.
GO:0005524; Molecular function: ATP binding.
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.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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Pfam | PF00406; ADK; 1; |
PF05191; ADK_lid; 0-1; | |
PRINTS | PR00094; ADENYLTKNASE; 1; |
TIGRFAMs | TIGR01351; Adk; 1; |
PROSITE | PS00113; ADENYLATE_KINASE; 1; |
Features
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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
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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 |