AC   MF_00235;
DC   Protein; auto
c?   <OC:Bacteria> or <OC:Archaea>
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 <FTGroup:1>
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 disassembling the active
CC       center during each catalytic cycle provides an effective means to
CC       prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating
CC       structure 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 disassembling the active
CC       center during each catalytic cycle provides an effective means to
CC       prevent ATP 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 <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
GO   GO:0004017; F:AMP kinase activity
GO   GO:0005524; F:ATP binding
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0044209; P:AMP salvage
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
# Version: 37
# Last updated date: 2025-08-19
# Created date: 2005-02-28
//