ID KGUA_CHLTA Reviewed; 205 AA. AC Q3KMZ2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 91. 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=CTA_0032; OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=315277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13; RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005; RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.; RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and RT genitotropic strains."; RL Infect. Immun. 73:6407-6418(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; CP000051; AAX50280.1; -; Genomic_DNA. DR RefSeq; WP_009871377.1; NC_007429.1. DR AlphaFoldDB; Q3KMZ2; -. DR SMR; Q3KMZ2; -. DR KEGG; cta:CTA_0032; -. DR HOGENOM; CLU_001715_1_1_0; -. DR Proteomes; UP000002532; 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..205 FT /note="Guanylate kinase" FT /id="PRO_0000266302" FT DOMAIN 18..196 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 25..32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 205 AA; 23109 MW; 36F80274CC283DA5 CRC64; MSVKVISPFS QDGVQCFPKL FIISAPAGAG KTTLTHMLQR EFPDAFEKTV SSTTRSARPG EVHGVDYLFV SEDDFKQSLD REDFLEWVFL FGTYYGTSKA EISRVLQKGK HCIAVIDVQG ALALKKQMPA VTIFIQAPSQ EELERRLNAR DSEKDFQKKE RLEHSAVEIA AASEFDYVVV NDDLITAYQV LRSIFIAEEH RMSHG //