ID KAD_HALH5 Reviewed; 217 AA. AC P38372; Q9JPW7; Q9WWJ3; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 02-SEP-2026, entry version 155. DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; OrderedLocusNames=BH0155; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). OX NCBI_TaxID=272558; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=10192928; DOI=10.1271/bbb.63.452; RA Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.; RT "Sequence analysis of a 32-kb region including the major ribosomal protein RT gene clusters from alkaliphilic Bacillus sp. strain C-125."; RL Biosci. Biotechnol. Biochem. 63:452-455(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans RT and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=1512566; DOI=10.1099/00221287-138-7-1365; RA Kang S.K., Kudo T., Horikoshi K.; RT "Molecular cloning and characterization of an alkalophilic Bacillus sp. RT C125 gene homologous to Bacillus subtilis secY."; RL J. Gen. Microbiol. 138:1365-1370(1992). 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 disassembling the active CC center during each catalytic cycle provides an effective means to CC prevent ATP 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; AB017508; BAA75292.1; -; Genomic_DNA. DR EMBL; BA000004; BAB03874.1; -; Genomic_DNA. DR EMBL; D10360; BAA01192.1; -; Genomic_DNA. DR PIR; C44859; C44859. DR PIR; T44404; T44404. DR RefSeq; WP_010896338.1; NC_002570.2. DR AlphaFoldDB; P38372; -. DR SMR; P38372; -. DR STRING; 272558.gene:10725995; -. DR GeneID; 87595696; -. DR KEGG; bha:BH0155; -. DR eggNOG; COG0563; Bacteria. DR HOGENOM; CLU_032354_1_2_9; -. DR OrthoDB; 9805030at2; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004017; F:AMP kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniRule. DR CDD; cd01428; ADK; 1. DR FunFam; 3.40.50.300:FF:000106; Adenylate kinase mitochondrial; 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; IPR007862; Adenylate_kinase_lid-dom. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01351; adk; 1. DR NCBIfam; NF001379; PRK00279.1-1; 1. DR NCBIfam; NF001380; PRK00279.1-2; 1. DR NCBIfam; NF001381; PRK00279.1-3; 1. DR NCBIfam; NF011100; PRK14527.1; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR Pfam; PF00406; ADK; 1. DR Pfam; PF05191; ADK_lid; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..217 FT /note="Adenylate kinase" FT /id="PRO_0000158725" FT REGION 30..59 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT REGION 126..163 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 10..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 31 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 36 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 57..59 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 85..88 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 92 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 127 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 136..137 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 160 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 171 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT CONFLICT 4 FT /note="I -> N (in Ref. 3; BAA01192)" FT /evidence="ECO:0000305" SQ SEQUENCE 217 AA; 24170 MW; FD5DF854B3BA3592 CRC64; MNLILMGLPG AGKGTQAEKI IEKYGIPHIS TGDMFRAAMK NETELGLKAK SYMDAGELVP DEVTIGIVRD RLSQDDCQNG FLLDGFPRTV AQAEALEDIL ASLDKKLDYV INIDVPEQLL MDRLTGRRVS PTSGRTYHVI FNPPKVEGIC DVDGSELIQR DDDKPETVKK RLEVNQKQAQ PLIDFYSEKG YLQNINGDQD ISRVFEDINE LLKGLSS //