ID KGUA_MESHJ Reviewed; 197 AA. AC Q4AAI1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 92. 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=MHJ_0149; OS Mesomycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110) OS (Mycoplasma hyopneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae; OC Mesomycoplasma. OX NCBI_TaxID=262719; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J / ATCC 25934 / NCTC 10110; RX PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005; RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L., RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R., RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M., RA Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., RA Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., RA Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P., RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S., RA Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B., RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., RA Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., RA Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L., RA Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R., RA Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N., RA Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C., RA Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P., RA Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.; RT "Swine and poultry pathogens: the complete genome sequences of two strains RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae."; RL J. Bacteriol. 187:5568-5577(2005). 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; AE017243; AAZ44240.1; -; Genomic_DNA. DR AlphaFoldDB; Q4AAI1; -. DR SMR; Q4AAI1; -. DR KEGG; mhj:MHJ_0149; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_1_14; -. DR OrthoDB; 9808150at2; -. DR Proteomes; UP000000548; 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..197 FT /note="Guanylate kinase" FT /id="PRO_0000266352" FT DOMAIN 6..191 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 197 AA; 22780 MW; 4FA5F3EDAFD47141 CRC64; MKVKMSKLII LSGPSGVGKG TIESLLLKNK NLLIKLAISA TTREKRRDEI NGVNYFFLTV QEFKEKIEND EFIEWSCHFN NYYGTLKSQI KFIQSQNFIP LLEIDTTGAK NIIENYKNKG ELSQLLTIFI LPPSIESLKN RIQKRLTETN IQINQRLEKA KAEIKIKNLF KFQVVNDNLE ECVAQIEKII SKEIQKT //