ID KGUA_ECOUT Reviewed; 207 AA. AC Q1R4U3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. 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=UTI89_C4193; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTI89 / UPEC; RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., RA Gordon J.I.; RT "Identification of genes subject to positive selection in uropathogenic RT strains of Escherichia coli: a comparative genomics approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). 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 -!- SEQUENCE CAUTION: CC Sequence=ABE09621.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000243; ABE09621.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_001295237.1; NZ_CP064825.1. DR AlphaFoldDB; Q1R4U3; -. DR SMR; Q1R4U3; -. DR GeneID; 75202217; -. DR KEGG; eci:UTI89_C4193; -. DR HOGENOM; CLU_001715_1_2_6; -. DR Proteomes; UP000001952; 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..207 FT /note="Guanylate kinase" FT /id="PRO_0000266323" FT DOMAIN 4..184 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 207 AA; 23593 MW; 62A99DB4063651E4 CRC64; MAQGTLYIVS APSGAGKSSL IQALLKTQPL YDTQVSVSHT TRQPRPGEVH GEHYFFVNHD EFKEMISRDA FLEHAEVFGN YYGTSREAIE QVLATGVDVF LDIDWQGAQQ IRQKMPHARS IFILPPSKIE LDRRLRGRGQ DSEEVIAKRM AQAVAEMSHY AEYDYLIVND DFDTALTDLK TIIRAERLRM SRQKQRHDAL ISKLLAD //