AC MF_00235; DC Protein; auto c? or TR HAMAP; MF_00235; -; 1; level=0 XX Names: Adenylate_kinase_Adk XX ID KAD DE RecName: Full=Adenylate kinase; DE Short=AK; DE EC=2.7.4.3; DE AltName: Full=ATP-AMP transphosphorylase; DE AltName: Full=ATP:AMP phosphotransferase; DE AltName: Full=Adenylate monophosphate kinase; GN Name=adk; XX CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate CC group between ATP and AMP. Plays an important role in cellular energy CC homeostasis and in adenine nucleotide metabolism. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP CC from ADP: step 1/1. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. case CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. Some bacteria have evolved a zinc-coordinating structure CC that stabilizes the LID domain. else CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. end case CC -!- SIMILARITY: Belongs to the adenylate kinase family. XX DR Pfam; PF00406; ADK; 1; trigger=no DR Pfam; PF05191; ADK_lid; 0-1; trigger=no DR PRINTS; PR00094; ADENYLTKNASE; 1; trigger=no DR NCBIfam; TIGR01351; Adk; 1; trigger=no DR PROSITE; PS00113; ADENYLATE_KINASE; 1; trigger=no XX KW ATP-binding KW Cytoplasm KW Transferase KW Kinase KW Nucleotide-binding KW Nucleotide biosynthesis case KW Metal-binding KW Zinc end case XX GO GO:0004017; F:adenylate kinase activity GO GO:0005524; F:ATP binding case GO GO:0008270; F:zinc ion binding end case GO GO:0009165; P:nucleotide biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: KAD_ECOLI (P69441) FT BINDING 10..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [GA]-x-G-K-[GST]-[ST] FT BINDING 57..59 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: x-[LYF]-[VILM] FT BINDING 85..88 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: G-[FY]-P-R FT BINDING 132..133 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [STVI]-[YFH] FT REGION 30..59 FT /note="NMP" FT REGION 122..159 FT /note="LID" FT BINDING 31 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: [TS] FT BINDING 36 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: R FT BINDING 92 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: Q FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R FT BINDING 156 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: R FT BINDING 167 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: R FT BINDING 200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT From: KAD_BACSU (P16304) FT BINDING 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT Optional; Group: 1; Condition: C FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT Optional; Group: 1; Condition: C FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT Optional; Group: 1; Condition: C FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT Optional; Group: 1; Condition: [CD] XX Size: 181-253; Related: MF_03168!; MF_03169!; MF_03170!; MF_03171!; MF_03172!; Template: P69441; P9WKF5; P16304; P27142; P84139; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in NOSS1, SYNY3 Plasmid: None Comments: None XX # Revision 1.47 2023/06/01 //