ID KAD1_SYNY3 Reviewed; 187 AA. AC P73302; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 07-OCT-2020, sequence version 3. DT 24-JAN-2024, entry version 146. DE RecName: Full=Adenylate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00235}; DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_00235}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP:AMP phosphotransferase 1 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=Adenylate monophosphate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00235}; GN Name=adk1 {ECO:0000255|HAMAP-Rule:MF_00235}; GN OrderedLocusNames=sll1815; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP PROTEIN SEQUENCE OF 2-21. RX PubMed=9298645; DOI=10.1002/elps.1150180806; RA Sazuka T., Ohara O.; RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain RT PCC6803: linking 130 protein spots with their respective genes."; RL Electrophoresis 18:1252-1258(1997). 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_00235}. 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_00235}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP CC from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}. 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. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00235}. 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; BA000022; BAA17330.1; -; Genomic_DNA. DR PIR; S77483; S77483. DR AlphaFoldDB; P73302; -. DR SMR; P73302; -. DR STRING; 1148.gene:10498193; -. DR PaxDb; 1148-1652408; -. DR EnsemblBacteria; BAA17330; BAA17330; BAA17330. DR KEGG; syn:sll1815; -. DR eggNOG; COG0563; Bacteria. DR InParanoid; P73302; -. DR PhylomeDB; P73302; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IBA:GO_Central. DR GO; GO:0009123; P:nucleoside monophosphate metabolic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01351; adk; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR PANTHER; PTHR23359:SF206; UMP-CMP 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 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298645" FT CHAIN 2..187 FT /note="Adenylate kinase 1" FT /id="PRO_0000158871" FT REGION 34..63 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT REGION 130..136 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 14..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 35 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 40 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 61..63 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 89..92 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 96 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 133 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 144 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" SQ SEQUENCE 187 AA; 20454 MW; 37863DB1DA94A14B CRC64; MAMAKGLIFL GAPGSGKGTQ AVGLAETLGI PHISTGDMLR QAIADGTELG NQAKGYMDKG ELVPDQLILG LIEERLGHKD AKAGWILDGF PRNVNQAIFL DELLVNIGHR THWVINLKVP DEVIVERLLA RGRADDNETT IRNRLLVYTE QTAPLMAYYQ EQGKLYSLDG NQPVEAIATN LEKLVKP //