AC MF_03169; DC Protein; auto c? TR HAMAP; MF_03169; -; 1; level=0 XX Names: Adenylate_kinase_AK3 XX ID KAD3 case DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial; DE EC=2.7.4.10; DE AltName: Full=Adenylate kinase 3; DE Short=AK 3; DE AltName: Full=Adenylate kinase 3 alpha-like 1; else case DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial; DE EC=2.7.4.10; DE AltName: Full=Adenylate kinase 3; DE Short=AK 3; else DE RecName: Full=GTP:AMP phosphotransferase, mitochondrial; DE EC=2.7.4.10; DE AltName: Full=Adenylate kinase 3; DE Short=AK 3; end case case GN Name=AK3; end case case GN Name=Adk3; end case case GN Name=ADK2; end case XX CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular CC nucleotides by catalyzing the interconversion of nucleoside phosphates. CC Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase CC activities. 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 -!- 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 binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent GTP CC 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 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:0046041; P:ITP metabolic process XX FT From: KAD3_BOVIN (P08760) FT BINDING 17..22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: G-x-G-K-G-T FT BINDING 64..66 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: x-L-[VMIL] FT BINDING 91..94 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: G-F-P-R FT BINDING 137..138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [VI]-Y FT REGION 37..66 FT /note="NMPbind" FT REGION 127..164 FT /note="LID" FT BINDING 38 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: [ST] FT BINDING 43 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: R FT BINDING 98 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: Q FT BINDING 128 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R FT BINDING 161 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: R FT BINDING 172 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT Condition: R FT BINDING 201 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [ST] case FT INIT_MET 1 FT /note="Removed" FT Condition: M end case XX Size: 206-273; Related: MF_00235; MF_03168; MF_03170!; MF_03171; MF_03172; Template: P08760; Q9UIJ7; P26364; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.13 2023/06/01 //