ID KGUA_STRT2 Reviewed; 209 AA. AC Q5M3I4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-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}; OrderedLocusNames=stu1431; OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=264199; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-250 / LMG 18311; RX PubMed=15543133; DOI=10.1038/nbt1034; RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.; RT "Complete sequence and comparative genome analysis of the dairy bacterium RT Streptococcus thermophilus."; RL Nat. Biotechnol. 22:1554-1558(2004). 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; CP000023; AAV61044.1; -; Genomic_DNA. DR RefSeq; WP_011226296.1; NC_006448.1. DR AlphaFoldDB; Q5M3I4; -. DR SMR; Q5M3I4; -. DR STRING; 264199.stu1431; -. DR GeneID; 66899192; -. DR KEGG; stl:stu1431; -. DR PATRIC; fig|264199.4.peg.1405; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_9; -. DR Proteomes; UP000001170; 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..209 FT /note="Guanylate kinase" FT /id="PRO_0000266418" FT DOMAIN 5..184 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 12..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 209 AA; 24053 MW; 99A65485CB8F2BA5 CRC64; MSERGLLIVF SGPSGVGKGT VRQEIFSKSD HKFEYSVSMT TRAQRPGEVD GKDYFFRSRE EFEELIRNGQ MLEYAEYVGN YYGTPLAYVN ETLDKGIDVF LEIEVQGALQ VKKKVPDAVF IFLTPPDLNE LEERLVGRGT DSEEVIAQRI ERAREEIALM SEYDYTIVND EVPLAAERVK RVIEAEHFRV ERVIGHYRNM ISDKRLSDK //