ID KGUA_ANAPZ Reviewed; 210 AA. AC Q2GLF7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, 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}; GN OrderedLocusNames=APH_0170; OS Anaplasma phagocytophilum (strain HZ). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Anaplasma; phagocytophilum group. OX NCBI_TaxID=212042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(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 --------------------------------------------------------------------------- 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; CP000235; ABD43557.1; -; Genomic_DNA. DR RefSeq; WP_011450318.1; NC_007797.1. DR PDB; 3LNC; X-ray; 1.95 A; A/B=1-210. DR PDBsum; 3LNC; -. DR AlphaFoldDB; Q2GLF7; -. DR SMR; Q2GLF7; -. DR STRING; 212042.APH_0170; -. DR PaxDb; 212042-APH_0170; -. DR EnsemblBacteria; ABD43557; ABD43557; APH_0170. DR GeneID; 56368342; -. DR KEGG; aph:APH_0170; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_2_5; -. DR EvolutionaryTrace; Q2GLF7; -. DR Proteomes; UP000001943; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; KW Transferase. FT CHAIN 1..210 FT /note="Guanylate kinase" FT /id="PRO_0000266285" FT DOMAIN 6..186 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" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 22..27 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:3LNC" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 60..68 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 90..96 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 99..103 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 106..115 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 130..135 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 152..159 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 160..164 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 165..170 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 174..189 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:3LNC" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:3LNC" FT HELIX 198..205 FT /evidence="ECO:0007829|PDB:3LNC" SQ SEQUENCE 210 AA; 23928 MW; A49B447B562D4E93 CRC64; MLKSVGVILV LSSPSGCGKT TVANKLLEKQ KNNIVKSVSV TTRAARKGEK EGKDYYFVDR EEFLRLCSNG EIIEHAEVFG NFYGVPRKNL EDNVDKGVST LLVIDWQGAF KFMEMMREHV VSIFIMPPSM EELRRRLCGR RADDSEVVEA RLKGAAFEIS HCEAYDYVIV NEDIEETADR ISNILRAEQM KTCRQVGLRE LLESRFPIED //