ID KAD1_CAEEL Reviewed; 210 AA. AC Q20140; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 02-SEP-2026, entry version 145. DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171}; DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171}; DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171}; GN ORFNames=F38B2.4; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Bristol N2; RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y., RA Thierry-Mieg D., Thierry-Mieg J.; RT "The Caenorhabditis elegans transcriptome project, a complementary view of RT the genome."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_03171}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}. 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. {ECO:0000255|HAMAP-Rule:MF_03171}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03171}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z50045; CAA90364.1; -; Genomic_DNA. DR EMBL; AF304123; AAG50236.1; -; mRNA. DR PIR; T21947; T21947. DR RefSeq; NP_001257141.1; NM_001270212.4. DR AlphaFoldDB; Q20140; -. DR SMR; Q20140; -. DR BioGRID; 46227; 20. DR FunCoup; Q20140; 412. DR IntAct; Q20140; 1. DR STRING; 6239.F38B2.4a.1; -. DR PaxDb; 6239-F38B2.4a.1; -. DR PeptideAtlas; Q20140; -. DR EnsemblMetazoa; F38B2.4a.1; F38B2.4a.1; WBGene00009531. DR GeneID; 181317; -. DR KEGG; cel:CELE_F38B2.4; -. DR UCSC; F38B2.4; c. elegans. DR AGR; WB:WBGene00009531; -. DR CTD; 181317; -. DR WormBase; F38B2.4a; CE02218; WBGene00009531; -. DR eggNOG; KOG3079; Eukaryota. DR HOGENOM; CLU_032354_0_3_1; -. DR InParanoid; Q20140; -. DR OMA; GTQCDRM; -. DR OrthoDB; 442176at2759; -. DR PhylomeDB; Q20140; -. DR BRENDA; 2.7.4.3; 1045. DR Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates. DR PRO; PR:Q20140; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00009531; Expressed in larva and 3 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004017; F:AMP kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro. DR GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-ARBA. DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IEA:InterPro. DR GO; GO:0006225; P:UDP biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd01428; ADK; 1. DR FunFam; 3.40.50.300:FF:000315; Adenylate kinase 1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03171; Adenylate_kinase_AK1; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR028582; AK1. DR InterPro; IPR006267; AK1/5. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01360; aden_kin_iso1; 1. DR NCBIfam; NF011100; PRK14527.1; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..210 FT /note="Adenylate kinase isoenzyme 1" FT /id="PRO_0000158932" FT REGION 50..79 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT REGION 144..154 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 30..35 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 51 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 56 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 77..79 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 107..110 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 114 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 151 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 162 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" FT BINDING 190 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171" SQ SEQUENCE 210 AA; 22597 MW; 786CB879D83DDFFC CRC64; MAPTVERKNI NLAPLKAAGV PIFFIVGGPG SGKGTQCDKI VAKYGLTHLS SGDLLRDEVK SGSPRGAQLT AIMESGALVP LEVVLDLVKE AMLKAIEKGS KGFLIDGYPR EVAQGQQFES EIQEAKLVLF FDVAEETLVK RLLHRAQTSG RADDNADTIK KRLHTFVTST APVVDYYESK GKLVRINAEG SVDDIFAVVV ANLDKATSKL //