ID KGUA_PSEU2 Reviewed; 214 AA. AC Q4ZZY8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 93. 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=Psyr_0211; OS Pseudomonas syringae pv. syringae (strain B728a). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. OX NCBI_TaxID=205918; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B728a; RX PubMed=16043691; DOI=10.1073/pnas.0504930102; RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., RA Kyrpides N.C., Ivanova N., Lindow S.E.; RT "Comparison of the complete genome sequences of Pseudomonas syringae pv. RT syringae B728a and pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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; CP000075; AAY35284.1; -; Genomic_DNA. DR RefSeq; WP_003392601.1; NC_007005.1. DR RefSeq; YP_233322.1; NC_007005.1. DR AlphaFoldDB; Q4ZZY8; -. DR SMR; Q4ZZY8; -. DR STRING; 205918.Psyr_0211; -. DR KEGG; psb:Psyr_0211; -. DR PATRIC; fig|205918.7.peg.208; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_0_6; -. DR OrthoDB; 9808150at2; -. DR Proteomes; UP000000426; 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..214 FT /note="Guanylate kinase" FT /id="PRO_0000266374" FT DOMAIN 6..192 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 13..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 214 AA; 24194 MW; AF8EF27455965A7C CRC64; MTHITGTLYI ISAPSGAGKT SLVKALMDAQ QEPQHGAQAK IRVSVSHTTR AMRPGEVDGV NYNFVDRATF LSMIEHGDFL EQAEVFGNLY GTSQSHLQQT LDEGHDLILE IDWQGARQVR AQMPQARSIF ILPPTQQALR QRLTNRGQDS DEIIEARMRE AVSEMSHYSE YEYVVVNDDF AGALEDLKAI FRANRLTQQH QQEQYSELFQ ELLA //