HAMAP rule MF_00235
General rule information
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| Accession | MF_00235 |
| Dates | 1-JUN-2001 (Created)
14-MAY-2024 (Last updated, Version 48) |
| Name | Adenylate_kinase_Adk |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P69441 (KAD_ECOLI); P9WKF5 (KAD_MYCTU); P16304 (KAD_BACSU); P27142 (KAD_GEOSE); P84139 (KAD_SPOGL); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_00235 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=adk; |
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 | Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; 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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| ATP-binding | |
| Cytoplasm | |
| Transferase | |
| Kinase | |
| Nucleotide-binding | |
| Nucleotide biosynthesis | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| end case | |
Gene Ontology
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| 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:0044209; Biological process:AMP salvage | |
| GO:0005737; Cellular component:cytoplasm | |
Cross-references
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| Pfam | PF00406; ADK; 1; |
| Pfam | PF05191; ADK_lid; 0-1; |
| PRINTS | PR00094; ADENYLTKNASE; 1; |
| NCBIfam | 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 | 132 | 133 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[STVI]-[YFH] | ||||||||
| REGION | 30 | 59 | /note="NMP" | |||||||||
| REGION | 122 | 159 | /note="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) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 130 | 130 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural" |
C | 1 | |||||||
| BINDING | 133 | 133 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural" |
C | 1 | |||||||
| BINDING | 150 | 150 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="structural" |
C | 1 | |||||||
| BINDING | 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 MF_03169 MF_03170 MF_03171 MF_03172 |
| Fusion | Nter: None Cter: None |