ID KGUA_OLEA2 Reviewed; 206 AA. AC Q30XT1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328}; DE EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328}; DE AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328}; GN Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328}; GN OrderedLocusNames=Dde_2719; OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) OS (Desulfovibrio alaskensis). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Oleidesulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20; RX PubMed=21685289; DOI=10.1128/jb.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:456216; EC=2.7.4.8; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00328}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00328}. 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; CP000112; ABB39515.1; -; Genomic_DNA. DR RefSeq; WP_011368541.1; NC_007519.1. DR AlphaFoldDB; Q30XT1; -. DR SMR; Q30XT1; -. DR STRING; 207559.Dde_2719; -. DR KEGG; dde:Dde_2719; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_7; -. DR Proteomes; UP000002710; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00071; GMPK; 1. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00328; Guanylate_kinase; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR017665; Guanylate_kinase. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR03263; guanyl_kin; 1. DR PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1. DR PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..206 FT /note="Guanylate kinase" FT /id="PRO_0000266318" FT DOMAIN 7..185 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 14..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 206 AA; 23732 MW; 6DA521CABD8CF894 CRC64; MVRPRSGIVL VLCAPSGTGK TTLTRRLLEE FPRFAFSVSY TTRQPRAGEE HGREYNFVDE ETFIRLRDEG FFAEWAEVHG NFYGTPLEDT RQLLARGRDV LFDIDVQGAA QLRGSLKQGC YVFILPPSGA ELERRLRARG TDPEDTIRRR LANARRELQQ AHWFNAWIVN DNLEQAYDEL RAAYLAATLS PTCRPELVDE LLQDWR //