ID KAD_SYNFM Reviewed; 213 AA. AC A0LIL1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 101. 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=Sfum_1576; OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB). OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales; OC Syntrophobacteraceae; Syntrophobacter. OX NCBI_TaxID=335543; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10017 / MPOB; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.; RT "Complete sequence of Syntrophobacter fumaroxidans MPOB."; RL Submitted (OCT-2006) 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_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; CP000478; ABK17263.1; -; Genomic_DNA. DR RefSeq; WP_011698433.1; NC_008554.1. DR AlphaFoldDB; A0LIL1; -. DR SMR; A0LIL1; -. DR STRING; 335543.Sfum_1576; -. DR KEGG; sfu:Sfum_1576; -. DR eggNOG; COG0563; Bacteria. DR HOGENOM; CLU_032354_1_2_7; -. DR InParanoid; A0LIL1; -. DR OrthoDB; 9805030at2; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000001784; 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..213 FT /note="Adenylate kinase" FT /id="PRO_1000021776" 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 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 213 AA; 23226 MW; 455B36B689579F3E CRC64; MNIILLGPPG AGKGTQASRL IGKYAIPQIS TGDMLRAALK EGTPLGLEAK KYMDQGALVP DSVVIGLVKE RIQKPDCSKG YMLDGFPRNV SQAEALDMML GELKQRIDGV VCIEVPNKEL LGRLTGRRTC RSCGAGFHVM FDPPKTDGKC DKCGGELYQR DDDNEATVSS RLKVYEDQTK PLIDYYEKQG KLRRIDGVGS MDAIFGRITA ILG //