AC   MF_03168;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_03168; -; 1; level=0
XX
Names: Adenylate_kinase_AK2
XX
ID   KAD2
case <OC:Vertebrata>
DE   RecName: Full=Adenylate kinase 2, mitochondrial;
DE            Short=AK 2;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase 2;
DE   AltName: Full=ATP:AMP phosphotransferase;
DE   AltName: Full=Adenylate monophosphate kinase;
else
DE   RecName: Full=Adenylate kinase;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase;
DE   AltName: Full=ATP:AMP phosphotransferase;
DE   AltName: Full=Adenylate kinase cytosolic and mitochondrial;
DE   AltName: Full=Adenylate monophosphate kinase;
end case
case <OC:Saccharomyces>
DE   + Flags: Precursor;
end case
case <OC:Vertebrata>
GN   Name=AK2;
end case
case <OC:Caenorhabditis>
GN   Name=let-754;
end case
case <OC:Insecta>
GN   Name=Ak2;
end case
case <OC:Fungi>
GN   Name=ADK1;
end case
XX
case <OC:Vertebrata>
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. Adenylate kinase
CC       activity is critical for regulation of the phosphate utilization and
CC       the AMP de novo biosynthesis pathways. Plays a key role in
CC       hematopoiesis.
else
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. Adenylate kinase
CC       activity is critical for regulation of the phosphate utilization and
CC       the AMP de novo biosynthesis pathways.
end case
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   -!- SUBUNIT: Monomer.
case <OC:Vertebrata>
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Mitochondrion intermembrane
CC       space. Note=Predominantly mitochondrial.
end 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.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 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   Kinase
KW   Mitochondrion
KW   Nucleotide-binding
KW   Transferase
case not <OC:Vertebrata>
KW   Cytoplasm
end case
case <FTTag:acetyl>
KW   Acetylation
end case
case <FTTag:disulfid>
KW   Disulfide bond
end case
XX
GO   GO:0005758; C:mitochondrial intermembrane space
case not <OC:Vertebrata>
GO   GO:0005737; C:cytoplasm
end case
GO   GO:0004017; F:adenylate kinase activity
GO   GO:0006172; P:ADP biosynthetic process
GO   GO:0046033; P:AMP metabolic process
GO   GO:0046034; P:ATP metabolic process
XX
FT   From: KAD2_YEAST (P07170)
FT   BINDING         16..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[AS]-G-K-G-T
FT   BINDING         63..65
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: x-L-V
FT   BINDING         92..95
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: G-F-P-R
FT   BINDING         143..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [ST]-Y
FT   REGION          36..65
FT                   /note="NMPbind"
FT   REGION          133..170
FT                   /note="LID"
FT   BINDING         37
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: T
FT   BINDING         42
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         99
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: Q
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         167
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         178
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
case <OC:Saccharomyces>
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT   CHAIN           3..Cter
FT                   /note="Adenylate kinase"
FT   MOD_RES         3
FT                   /note="N-acetylserine"
FT   Tag: acetyl; Condition: S
end case
FT   From: KAD2_HUMAN (P54819)
case <OC:Mammalia>
FT   INIT_MET        1
FT                   /note="Removed"
FT   Condition: M
end case
case <OC:Vertebrata>
FT   DISULFID        42..92
FT   Tag: disulfid; Condition: C-x*-C
end case
XX
Size: 220-278;
Related: MF_00235; MF_03169; MF_03170; MF_03171; MF_03172;
Template: P54819; Q9U915; P07170;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in CANAL
Plasmid: None
Comments: None
XX
# Revision 1.16 2023/06/01
//