ID KAD_ANADF Reviewed; 214 AA. AC A7HBN9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 90. 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}; GN OrderedLocusNames=Anae109_1932; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5; RX PubMed=25614562; DOI=10.1128/genomea.01449-14; RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C., RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J., RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A., RA Loeffler F.E., Fields M.W.; RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic, RT metal-reducing bacterium isolated from a contaminated subsurface RT environment."; RL Genome Announc. 3:0-0(2015). 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. Some bacteria have evolved a zinc-coordinating structure CC that stabilizes the LID domain. {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; CP000769; ABS26135.1; -; Genomic_DNA. DR RefSeq; WP_012096714.1; NC_009675.1. DR AlphaFoldDB; A7HBN9; -. DR SMR; A7HBN9; -. DR STRING; 404589.Anae109_1932; -. DR KEGG; afw:Anae109_1932; -. DR eggNOG; COG0563; Bacteria. DR HOGENOM; CLU_032354_1_2_7; -. DR OrthoDB; 9805030at2; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000006382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. 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; IPR007862; Adenylate_kinase_lid-dom. 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 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; Metal-binding; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase; Zinc. FT CHAIN 1..214 FT /note="Adenylate kinase" FT /id="PRO_1000021708" 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 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" 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 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235" FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" 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" SQ SEQUENCE 214 AA; 23048 MW; B1A0367305582E41 CRC64; MILILLGPPG AGKGTQAKLL AAEYGVPHIS TGDMFRDHKA RGTELGKTVQ AIMDAGGLVT DDITNEMVKD RLSRPDVAKG FILDGYPRTS AQAEYLDGLL ASAGRAISRV LSYEVAEEAV VERISGRRSC PKCGAVYHVS ANPPRRMGYC DRDDAGLVQR DDDKPENVKK RMAEYAAKTE PLKRFYSARG LLATVEGIGT PEGILAVTKR VLAS //