ID KGUA_BACFN Reviewed; 204 AA. AC Q5L9N9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 95. 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=BF3500; OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 OS / NCTC 9343 / Onslow). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / RC Onslow; RX PubMed=15746427; DOI=10.1126/science.1107008; RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A., RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., RA Barrell B.G., Parkhill J.; RT "Extensive DNA inversions in the B. fragilis genome control variable gene RT expression."; RL Science 307:1463-1465(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; CR626927; CAH09188.1; -; Genomic_DNA. DR RefSeq; WP_005790592.1; NZ_UFTH01000001.1. DR AlphaFoldDB; Q5L9N9; -. DR SMR; Q5L9N9; -. DR PaxDb; 272559-BF9343_3407; -. DR KEGG; bfs:BF9343_3407; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_1_10; -. DR Proteomes; UP000006731; 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_0000266289" FT DOMAIN 16..196 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 23..30 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 204 AA; 22980 MW; 5D62E22010247C60 CRC64; MNPTERITTP HKTGEAKVII FSAPSGSGKS TIINYLLAQK LNLAFSISAT SRPPRGNEKH GVEYFFLSPD EFRQRIANNE FLEYEEVYTD RFYGTLKAQV EKQLAAGQNV VFDVDVVGGC NIKKYYGERA LSLFIQPPCI DELRRRLIGR GTDTPEVIES RIAKAEYELS FAPKFDKVII NDDLETAKAH ALKVIKEFLG IDTE //