ID KAD6_METBF Reviewed; 182 AA. AC Q46FV0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 24-JAN-2024, entry version 90. DE RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00039}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039}; GN OrderedLocusNames=Mbar_A0258; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/jb.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that CC catalyzes the reversible transfer of the terminal phosphate group CC between nucleoside triphosphates and monophosphates. CC {ECO:0000255|HAMAP-Rule:MF_00039}. 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_00039}; CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00039}. 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; CP000099; AAZ69242.1; -; Genomic_DNA. DR AlphaFoldDB; Q46FV0; -. DR SMR; Q46FV0; -. DR STRING; 269797.Mbar_A0258; -. DR PaxDb; 269797-Mbar_A0258; -. DR KEGG; mba:Mbar_A0258; -. DR eggNOG; arCOG01038; Archaea. DR HOGENOM; CLU_079096_0_1_2; -. DR OMA; QCEIFGT; -. DR OrthoDB; 8730at2157; -. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12595:SF0; ADENYLATE KINASE ISOENZYME 6; 1. DR PANTHER; PTHR12595; POS9-ACTIVATING FACTOR FAP7-RELATED; 1. DR Pfam; PF13238; AAA_18; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1..182 FT /note="Putative adenylate kinase" FT /id="PRO_1000003091" FT REGION 30..53 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT REGION 104..114 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 10..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 105 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" SQ SEQUENCE 182 AA; 21069 MW; 6EE6678F65AE38CA CRC64; MLIGLTGTPG TGKTSVSKFL ERKRHWKVIH LNEMIKEEHL YTEVDEVRDA VIADMELVRQ RLEEIIGGKE NEVIILESHL AHYIADIVII LRVYPPELKM RLKARGYSEE KIRENIEAEA LDVILVEAFE WCKKVFEINT TGKSIEETEQ HIEKIIDHIL SGNEEELPEY KPGSIDWIDL VP //