ID KGUA_BLOFL Reviewed; 210 AA. AC Q7VRJ7; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 96. 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}; OrderedLocusNames=Bfl616; OS Blochmannia floridanus. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; ant endosymbionts; Blochmannia. OX NCBI_TaxID=203907; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12886019; DOI=10.1073/pnas.1533499100; RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., RA van Ham R.C.H.J., Gross R., Moya A.; RT "The genome sequence of Blochmannia floridanus: comparative analysis of RT reduced genomes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003). 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; BX248583; CAD83291.1; -; Genomic_DNA. DR AlphaFoldDB; Q7VRJ7; -. DR SMR; Q7VRJ7; -. DR STRING; 203907.Bfl616; -. DR KEGG; bfl:Bfl616; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_6; -. DR OrthoDB; 9808150at2; -. DR Proteomes; UP000002192; 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..210 FT /note="Guanylate kinase" FT /id="PRO_0000170516" FT DOMAIN 6..186 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 13..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 210 AA; 24549 MW; E06816F15BB4AA1E CRC64; MKKYSGLLGI ISAPSGAGKS TLINALQKND SILQIKLSIS YTTRKKRPGE VHGKDYYFIS IEEFQNMINQ NMFLEYAKVF NHYYGTEKNS IKLMLNSGVH VILNIDWQGM NQIRNKKLDF YTIFILPPSQ KELEKRLRFR GLDTDQVIFD RMKQAMNEIS HCKEYDYIII NDDFNIALIY LQSVILSKQL KIDYQEYHNS NLINNLLSCL //