ID   KGUA_ANADE              Reviewed;         226 AA.
AC   Q2IL45;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Adeh_2606;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000251; ABC82376.1; -; Genomic_DNA.
DR   RefSeq; WP_011421658.1; NC_007760.1.
DR   AlphaFoldDB; Q2IL45; -.
DR   SMR; Q2IL45; -.
DR   STRING; 290397.Adeh_2606; -.
DR   EnsemblBacteria; ABC82376; ABC82376; Adeh_2606.
DR   KEGG; ade:Adeh_2606; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_2_7; -.
DR   OMA; EWAVVHG; -.
DR   Proteomes; UP000001935; 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   Gene3D; 3.40.50.300; -; 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   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; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..226
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000266284"
FT   DOMAIN          13..193
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         20..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   226 AA;  24357 MW;  C057634EC13609CD CRC64;
     MSSDAAAQER LPGLLLVLSA PSGAGKTTLA HRLREASPDA VFSISATTRA PRGAEREGVD
     YHFVTAERFT ELVAQGAFAE WAEVHGQRYG TLRATVDEAL AAGKLALFDI DVQGGAQIKA
     AWPQQAATVL VLPPDEAELE RRLRGRDTDS DETIRRRLVA ARAEVARGLG SYDYVVVNDV
     LEGALAQLQA IVRHERLRHA GRWDPEAARV AEACRRSAAP LGGWAS