AC   MF_03170;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_03170; -; 1; level=0
XX
Names: Adenylate_kinase_AK4
XX
ID   KAD4
DE   RecName: Full=Adenylate kinase 4, mitochondrial;
DE            Short=AK 4;
DE            EC=2.7.4.10;
DE            EC=2.7.4.6;
DE   AltName: Full=Adenylate kinase 3-like;
DE   AltName: Full=GTP:AMP phosphotransferase AK4;
GN   Name=AK4; Synonyms=AK3L1;
XX
CC   -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC       nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC       Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor,
CC       but phosphorylates only AMP when using GTP as phosphate donor. Also
CC       displays broad nucleoside diphosphate kinase activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-
CC         diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         EC=2.7.4.10;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC         deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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 GTP/ATP binding. Assembling and dissambling the active
CC       center during each catalytic cycle provides an effective means to
CC       prevent GTP/ATP hydrolysis.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
XX
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1; trigger=no
DR   Pfam; PF00406; ADK; 1; trigger=no
DR   Pfam; PF05191; ADK_lid; 1; trigger=no
DR   PRINTS; PR00094; ADENYLTKNASE; 1; trigger=no
DR   NCBIfam; TIGR01351; adk; 1; trigger=no
XX
KW   ATP-binding
KW   GTP-binding
KW   Kinase
KW   Mitochondrion
KW   Nucleotide-binding
KW   Transferase
XX
GO   GO:0005759; C:mitochondrial matrix
GO   GO:0046899; F:nucleoside triphosphate adenylate kinase activity
GO   GO:0006172; P:ADP biosynthetic process
GO   GO:0046033; P:AMP metabolic process
GO   GO:0046039; P:GTP metabolic process
GO   GO:0046034; P:ATP metabolic process
XX
FT   From: KAD4_HUMAN (P27144)
FT   BINDING         15..20
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT   Condition: G-x-G-K-G-T
FT   BINDING         62..64
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: x-L-V
FT   BINDING         89..92
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: G-F-P-R
FT   BINDING         135..136
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT   Condition: V-Y
FT   REGION          35..64
FT                   /note="NMPbind"
FT   REGION          125..162
FT                   /note="LID"
FT   BINDING         36
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: S
FT   BINDING         41
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         96
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: Q
FT   BINDING         126
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT   Condition: R
FT   BINDING         170
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         199
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT   Condition: T
XX
Size: 223-231;
Related: MF_00235; MF_03168; MF_03169; MF_03171; MF_03172;
Template: P27144;
Scope:
 Eukaryota; Vertebrata
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.14 2023/06/01
//