ID KGUA_LISMF Reviewed; 205 AA. AC Q71YI9; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 97. 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=LMOf2365_1855; OS Listeria monocytogenes serotype 4b (strain F2365). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=265669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F2365; RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H., RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., RA Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne RT pathogen Listeria monocytogenes reveal new insights into the core genome RT components of this species."; RL Nucleic Acids Res. 32:2386-2395(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; AE017262; AAT04625.1; -; Genomic_DNA. DR RefSeq; WP_003725659.1; NC_002973.6. DR AlphaFoldDB; Q71YI9; -. DR SMR; Q71YI9; -. DR KEGG; lmf:LMOf2365_1855; -. DR HOGENOM; CLU_001715_1_2_9; -. 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..205 FT /note="Guanylate kinase" FT /id="PRO_0000170557" 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 205 AA; 23282 MW; 40579D7F0038C9E1 CRC64; MTERGLLIVL SGPSGVGKGT VREAVFKDPE TSFDYSISMT TRLPREGEQD GVDYYFRSRE VFEQAIKDGK MLEYAEYVGN YYGTPLEYVE EKLAAGVDIF LEIEVQGAMQ VRKAMPEGIF IFLTPPDLSE LKNRIIGRGT ESMEVVEERM ETAKKEIEMM ASYDYAVVND VVANAVQKIK GIVETEHLKT ERVIHRYKKM LEGLQ //