ID KGUA_CARHZ Reviewed; 204 AA. AC Q3AC14; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-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=CHY_1488; OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / OS Z-2901). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Carboxydothermus. OX NCBI_TaxID=246194; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901; RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065; RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.; RT "Life in hot carbon monoxide: the complete genome sequence of RT Carboxydothermus hydrogenoformans Z-2901."; RL PLoS Genet. 1:563-574(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; CP000141; ABB15039.1; -; Genomic_DNA. DR RefSeq; WP_011344395.1; NC_007503.1. DR AlphaFoldDB; Q3AC14; -. DR SMR; Q3AC14; -. DR STRING; 246194.CHY_1488; -. DR KEGG; chy:CHY_1488; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_2_9; -. DR InParanoid; Q3AC14; -. DR OrthoDB; 9808150at2; -. DR Proteomes; UP000002706; 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..204 FT /note="Guanylate kinase" FT /id="PRO_0000266301" FT DOMAIN 4..182 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 11..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 204 AA; 23494 MW; BF350BF393EBD99B CRC64; MHKGMLVVVS GPSGAGKGTI CQEIRKRNPN LFYSISATTR EKRVGEIDGV HYYFIDRQQF EKMIANDEFL EWADVYGNYY GTPKKPVFEA LARGQDVILE IDIKGARQVK KTYPEGVFVF ILPPSISILE ERLRKRGTDK EEIIVKRMQM AWEEIANCDW YDYLILNDDL ETAVNDLEAV LTAEKLKPKR VNYRVLLEGG VLER //