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 12-SEP-2018, entry version 60. 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; Methanomicrobia; Methanosarcinales; OC 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., RA Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., RA 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 CC that catalyzes the reversible transfer of the terminal phosphate CC group between nucleoside triphosphates and monophosphates. CC {ECO:0000255|HAMAP-Rule:MF_00039}. CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP- CC 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 RefSeq; WP_011305297.1; NC_007355.1. DR ProteinModelPortal; Q46FV0; -. DR SMR; Q46FV0; -. DR STRING; 269797.Mbar_A0258; -. DR EnsemblBacteria; AAZ69242; AAZ69242; Mbar_A0258. DR GeneID; 3624967; -. DR KEGG; mba:Mbar_A0258; -. DR eggNOG; arCOG01038; Archaea. DR eggNOG; COG1936; LUCA. DR HOGENOM; HOG000224471; -. DR KO; K18532; -. DR OMA; DNVQCEI; -. DR OrthoDB; POG093Z0F8E; -. DR BioCyc; MBAR269797:GHUW-257-MONOMER; -. DR Proteomes; UP000008156; Chromosome. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12595:SF0; PTHR12595:SF0; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. FT CHAIN 1 182 Putative adenylate kinase. FT /FTId=PRO_1000003091. FT NP_BIND 10 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00039}. FT REGION 30 53 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00039}. FT REGION 104 114 LID. {ECO:0000255|HAMAP-Rule:MF_00039}. FT BINDING 101 101 ATP. {ECO:0000255|HAMAP-Rule:MF_00039}. FT BINDING 105 105 ATP. {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 //