ID KGUA_EHRRW Reviewed; 209 AA. AC Q5HAK7; Q5FDG1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 102. 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=Erum6740, ERWE_CDS_07070; OS Ehrlichia ruminantium (strain Welgevonden). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=254945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden; RX PubMed=15637156; DOI=10.1073/pnas.0406633102; RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T., RA Allsopp B.A.; RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple RT tandem repeats of actively variable copy number."; RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden; RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium RT reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). 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; CR767821; CAH58406.1; -; Genomic_DNA. DR EMBL; CR925678; CAI27201.1; -; Genomic_DNA. DR RefSeq; WP_011155353.1; NC_006832.1. DR AlphaFoldDB; Q5HAK7; -. DR SMR; Q5HAK7; -. DR GeneID; 56785440; -. DR KEGG; eru:Erum6740; -. DR KEGG; erw:ERWE_CDS_07070; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_5; -. DR Proteomes; UP000001021; 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; Transferase. FT CHAIN 1..209 FT /note="Guanylate kinase" FT /id="PRO_0000266322" FT DOMAIN 9..188 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 16..23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 209 AA; 24376 MW; 31C2FBBFAD2B49B6 CRC64; MNNNLKSRGI MLVMSSPSGG GKTTISQLLV NELQGEIIRS VSVTTREPRN EEVEGKDYFF VTEDEFHHLC NTNQMLEYAK VFGNYYGIPR RFVMDNINNG ISILFSIDWQ GAFKLIDIMS EHVVSVFILP PSMEELKRRL YNRSGESDMI NQRLKEAAFE ISHCYRYNYI IVNHNIEESV QQIKSIFIAE KLKTHRKMFL EQVVKSYYI //