ID A0A2U9T766_9GAMM Unreviewed; 212 AA. AC A0A2U9T766; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 08-MAY-2019, entry version 6. DE RecName: Full=Guanylate kinase {ECO:0000256|HAMAP-Rule:MF_00328, ECO:0000256|SAAS:SAAS00356201}; DE EC=2.7.4.8 {ECO:0000256|HAMAP-Rule:MF_00328, ECO:0000256|SAAS:SAAS00356190}; DE AltName: Full=GMP kinase {ECO:0000256|HAMAP-Rule:MF_00328}; GN Name=gmk {ECO:0000256|HAMAP-Rule:MF_00328}; GN ORFNames=C9I47_2725 {ECO:0000313|EMBL:AWV08401.1}; OS Lysobacter maris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1605891 {ECO:0000313|EMBL:AWV08401.1, ECO:0000313|Proteomes:UP000249447}; RN [1] {ECO:0000313|EMBL:AWV08401.1, ECO:0000313|Proteomes:UP000249447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ9B {ECO:0000313|EMBL:AWV08401.1, RC ECO:0000313|Proteomes:UP000249447}; RA Zhang X.-Q.; RT "The complete genome of Lysobacter maris HZ9B, a marine bacterium RT antagonistic against terrestrial plant pathogens."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000256|HAMAP-Rule:MF_00328, ECO:0000256|SAAS:SAAS00036649}. 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:0000256|HAMAP- CC Rule:MF_00328, ECO:0000256|SAAS:SAAS01120090}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_00328, ECO:0000256|SAAS:SAAS00548802}. 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; CP029843; AWV08401.1; -; Genomic_DNA. DR KEGG; lmb:C9I47_2725; -. DR KO; K00942; -. DR Proteomes; UP000249447; 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 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 Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03263; guanyl_kin; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00328, KW ECO:0000256|SAAS:SAAS00238200}; KW Complete proteome {ECO:0000313|Proteomes:UP000249447}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00328, KW ECO:0000256|SAAS:SAAS00434181, ECO:0000313|EMBL:AWV08401.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00328, KW ECO:0000256|SAAS:SAAS00434271}; KW Reference proteome {ECO:0000313|Proteomes:UP000249447}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00328, KW ECO:0000256|SAAS:SAAS00434142}. FT DOMAIN 3 181 Guanylate kinase-like. FT {ECO:0000259|PROSITE:PS50052}. FT NP_BIND 10 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00328}. SQ SEQUENCE 212 AA; 23423 MW; F121CDAE1B9ED553 CRC64; MRGTLFIVAA PSGAGKSSIV NAVLARDPNI CLSISFTSRK PRPGERHAEH YHFVDEAEFE RMVEAGDFFE HARVHGDWKG TARQSVEPQL AAGRDVLLEI DWQGARQVRK QVPGAISVFI LPPSRAALEQ RMRNRGQDSE EVIAQRLAAA REEMSHYGEF DYVIVNEHFA MAVDEMCAVF TASRLRREMQ VARHGRLIGA LLAGPGGDGS GD //