ID   KGUA_MYCGA              Reviewed;         195 AA.
AC   Q9KX62;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
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=MYCGA6400; ORFNames=MGA_0462;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RA   Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; L35043; AAF36761.1; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56990.1; -; Genomic_DNA.
DR   RefSeq; WP_011113900.1; NC_004829.2.
DR   AlphaFoldDB; Q9KX62; -.
DR   SMR; Q9KX62; -.
DR   KEGG; mga:MGA_0462; -.
DR   PATRIC; fig|233150.7.peg.717; -.
DR   HOGENOM; CLU_001715_1_1_14; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 1502854at2; -.
DR   Proteomes; UP000001418; 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..195
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170561"
FT   DOMAIN          12..191
FT                   /note="Guanylate kinase-like"
FT   BINDING         19..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        120
FT                   /note="R -> K (in Ref. 1; AAF36761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="L -> R (in Ref. 1; AAF36761)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="N -> S (in Ref. 1; AAF36761)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  22473 MW;  6AB0B0FBF9A66573 CRC64;
     MVVIYIMSNK QGLIILISGP SGVGKGTIVS RLLSDNNLKL NVSISATTRK KRASEVEGVH
     YFFKTKEEFE QMIANNQLLE YANYVNNYYG TPLSLVKEIL DKNENLILEI EYQGVIQVLR
     KGFRTLSIFV LPPSEDELVA RLKKRGTEND EVIKHRLEQA VKEYAHRELY DHTIINDDLE
     KTIEDIKQLI LKYNQ