AC   MF_03171;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_03171; -; 1; level=0
XX
Names: Adenylate_kinase_AK1
XX
ID   KAD1
case <OC:Vertebrata>
DE   RecName: Full=Adenylate kinase isoenzyme 1;
DE            Short=AK 1;
DE            EC=2.7.4.3;
DE            EC=2.7.4.6;
DE   AltName: Full=ATP-AMP transphosphorylase 1;
DE   AltName: Full=ATP:AMP phosphotransferase;
DE   AltName: Full=Adenylate monophosphate kinase;
DE   AltName: Full=Myokinase;
else
DE   RecName: Full=Adenylate kinase isoenzyme 1;
DE            Short=AK 1;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase 1;
DE   AltName: Full=ATP:AMP phosphotransferase;
DE   AltName: Full=Adenylate monophosphate kinase;
end case
case <OC:Vertebrata>
GN   Name=AK1;
end case
XX
case <OC:Vertebrata>
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       group between ATP and AMP. Also displays broad nucleoside diphosphate
CC       kinase activity. Plays an important role in cellular energy homeostasis
CC       and in adenine nucleotide metabolism.
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;
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.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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. AK1 subfamily.
XX
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1; trigger=no
DR   Pfam; PF00406; ADK; 1; trigger=no
DR   PRINTS; PR00094; ADENYLTKNASE; 1; trigger=no
DR   NCBIfam; TIGR01360; aden_kin_iso1; 1; trigger=no
XX
KW   ATP-binding
KW   Kinase
KW   Nucleotide-binding
KW   Transferase
KW   Cytoplasm
case <FTTag:acetyl>
KW   Acetylation
end case
XX
GO   GO:0005737; C:cytoplasm
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: KAD1_HUMAN (P00568)
FT   BINDING         18..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-S-G-K-G-T
FT   BINDING         65..67
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: x-L-V
FT   BINDING         94..97
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: G-Y-P-R
FT   REGION          38..67
FT                   /note="NMPbind"
FT   REGION          131..141
FT                   /note="LID"
FT   BINDING         39
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: [ST]
FT   BINDING         44
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         101
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: Q
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         138
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         149
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
case <OC:Mammalia>
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT   Tag: acetyl; Condition: M
end case
XX
Size: 193-211;
Related: MF_00235; MF_03168; MF_03169; MF_03170; MF_03172;
Template: P00568; P00571;
Scope:
 Eukaryota; Metazoa
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.13 2023/06/01
//