ID KGUA_RHORT Reviewed; 218 AA. AC Q2RXB1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, 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=Rru_A0429; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / OS NCIMB 8255 / S1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1; RX PubMed=21886856; DOI=10.4056/sigs.1804360; RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K., RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C., RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y., RA Roberts G.P., Reslewic S., Schwartz D.C.; RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1)."; RL Stand. Genomic Sci. 4:293-302(2011). 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; CP000230; ABC21234.1; -; Genomic_DNA. DR RefSeq; WP_011388188.1; NC_007643.1. DR RefSeq; YP_425521.1; NC_007643.1. DR AlphaFoldDB; Q2RXB1; -. DR SMR; Q2RXB1; -. DR STRING; 269796.Rru_A0429; -. DR EnsemblBacteria; ABC21234; ABC21234; Rru_A0429. DR KEGG; rru:Rru_A0429; -. DR PATRIC; fig|269796.9.peg.485; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_5; -. DR PhylomeDB; Q2RXB1; -. DR Proteomes; UP000001929; 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..218 FT /note="Guanylate kinase" FT /id="PRO_0000266387" FT DOMAIN 15..194 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 22..29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 218 AA; 24166 MW; E72F632C63CDC355 CRC64; MSAPSSAPAL IPRRGMMLVL SSPSGAGKTT ISRALLAEED GLEMSVSVTT RAPRPGERDG EHYHFIDVAR YMALTKDDGL LEHARVFENY YGTPRAPVEA ALARGCDVLF DIDWQGTQQV AEKARTDLVS IFILPPSVGE LERRLKGRAQ DSDAVVAARM AKAMDEISHY FEYDYIIVND DLDRSIADVR AILRAERLKR ARRIGLAEFV NRMRGAGE //