ID   KGUA_MYCPN              Reviewed;         239 AA.
AC   P75526;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=MPN_246; ORFNames=MP586;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR   EMBL; U00089; AAB96234.1; -; Genomic_DNA.
DR   PIR; S73912; S73912.
DR   RefSeq; NP_109934.1; NC_000912.1.
DR   RefSeq; WP_010874603.1; NC_000912.1.
DR   AlphaFoldDB; P75526; -.
DR   SMR; P75526; -.
DR   IntAct; P75526; 2.
DR   STRING; 272634.MPN_246; -.
DR   EnsemblBacteria; AAB96234; AAB96234; MPN_246.
DR   GeneID; 66609108; -.
DR   KEGG; mpn:MPN_246; -.
DR   PATRIC; fig|272634.6.peg.265; -.
DR   HOGENOM; CLU_001715_1_1_14; -.
DR   OMA; EWAVVHG; -.
DR   BioCyc; MPNE272634:G1GJ3-389-MON; -.
DR   Proteomes; UP000000808; 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..239
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170568"
FT   DOMAIN          55..235
FT                   /note="Guanylate kinase-like"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  27002 MW;  59247177879BE2F6 CRC64;
     MQSRLAWSKG NWTGLVGSLI SLTSSSTSHA LVGNNSILIC GKIKIILNIE MVDTGRIFVI
     TGPSGVGKSS LVRCLIDHFK DKLRYSISAT TRKMRNSETE GVDYFFKDKA EFEKLIAADA
     FVEWAMYNDN YYGTLKSQAE QIIHNGGNLV LEIEYQGALQ VKQKYPNDVV LIFIKPPSME
     ELLVRLKKRN DEDAITIQNR LKQAEKECQQ IGHFKYVVTN NEFDKTLAEL QAILLAEFN