ID KGUA_PASMU Reviewed; 208 AA. AC P57888; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=PM0922; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000250}. 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; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. {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; AE004439; AAK03006.1; -; Genomic_DNA. DR RefSeq; WP_005722822.1; NC_002663.1. DR AlphaFoldDB; P57888; -. DR SMR; P57888; -. DR STRING; 272843.PM0922; -. DR EnsemblBacteria; AAK03006; AAK03006; PM0922. DR GeneID; 77206225; -. DR KEGG; pmu:PM0922; -. DR PATRIC; fig|272843.6.peg.932; -. DR HOGENOM; CLU_001715_1_0_6; -. DR OrthoDB; 9808150at2; -. DR Proteomes; UP000000809; 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; 2. 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..208 FT /note="Guanylate kinase" FT /id="PRO_0000170579" FT DOMAIN 4..185 FT /note="Guanylate kinase-like" FT BINDING 11..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" SQ SEQUENCE 208 AA; 23377 MW; A811EA7F89A39CC1 CRC64; MAQGNLYILS APSGAGKSSL ISALLNQQQD NKMMVSVSHT TRQPRPGEQE GVHYYFVSVE AFESLIEQDL FLEYAKVFGG NYYGTSLPAI EENLAKGIDV FLDIDWQGAQ QIRQKVPNVK SIFILPPSLA ELERRLIGRG QDSTEVIAAR MSKAIDEISH YNEYDYVIVN DVFEQALADF QAILRAERLT LTHQQKQNQA LIEQLLAK //