ID KGUA_SHEFN Reviewed; 207 AA. AC Q088T7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 88. 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=Sfri_0365; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 400; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000447; ABI70228.1; -; Genomic_DNA. DR RefSeq; WP_011635855.1; NC_008345.1. DR AlphaFoldDB; Q088T7; -. DR SMR; Q088T7; -. DR STRING; 318167.Sfri_0365; -. DR KEGG; sfr:Sfri_0365; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_6; -. DR OrthoDB; 9808150at2; -. DR Proteomes; UP000000684; 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..207 FT /note="Guanylate kinase" FT /id="PRO_0000266397" FT DOMAIN 5..184 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT REGION 30..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..49 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 12..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 207 AA; 23019 MW; 8F2744164E2658AA CRC64; MSTRGNLFIV SAPSGAGKSS LISTLLKDKP SDKQVSVSHT TRKPRPGEVD GQHYHFITVE QFKALIAQNA FIEWAEVFGN FYGTSKLVIE QTLDKGIDVF LDIDWQGAEQ VKKLMETAIG VFILPPSKAE LERRLTGRGQ DSQQVIDSRM AQAVSEMSHY AQYEFIIVND DFDNALADLS AIIRSQRLTC ASQQHAQNDM IVDLLAD //