ID KGUA_FUSNN Reviewed; 185 AA. AC Q8RHI9; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 12-AUG-2020, 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}; OrderedLocusNames=FN2033; OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / OS JCM 8532 / LMG 13131). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium. OX NCBI_TaxID=190304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131; RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O., RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M., RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C., RA Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum RT strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). 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; AE009951; AAL94118.1; -; Genomic_DNA. DR RefSeq; NP_602819.1; NC_003454.1. DR SMR; Q8RHI9; -. DR STRING; 190304.FN2033; -. DR EnsemblBacteria; AAL94118; AAL94118; FN2033. DR GeneID; 992197; -. DR KEGG; fnu:FN2033; -. DR PATRIC; fig|190304.8.peg.496; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_1_0; -. DR InParanoid; Q8RHI9; -. DR KO; K00942; -. DR OMA; AGNYYGT; -. DR BioCyc; FNUC190304:G1FZS-520-MONOMER; -. DR Proteomes; UP000002521; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central. 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 Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03263; guanyl_kin; 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..185 FT /note="Guanylate kinase" FT /id="PRO_0000170540" FT DOMAIN 4..181 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT NP_BIND 11..18 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 185 AA; 21025 MW; 988EF86443662B96 CRC64; MSLGALYVVS GPSGAGKSTV CKLVRERLGI NLSISATSRK PRNGEQEGVD YFFITAEEFE RKIKNDDFLE YANVHGNYYG TLKSEVEERL KRGEKVLLEI DVQGGVQVKN KFPEANLIFF KTANKEELEK RLRGRNTDSE EVIQARLKNS LKELEYESKY DRVIINNEIE QACNDLISII ENGVK //