ID   KGUA_ONYPE              Reviewed;         212 AA.
AC   P60554;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=PAM_737;
OS   Onion yellows phytoplasma (strain OY-M).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=262768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY-M;
RX   PubMed=14661021; DOI=10.1038/ng1277;
RA   Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA   Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT   "Reductive evolution suggested from the complete genome sequence of a
RT   plant-pathogenic phytoplasma.";
RL   Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04822.1; -; Genomic_DNA.
DR   AlphaFoldDB; P60554; -.
DR   SMR; P60554; -.
DR   STRING; 262768.PAM_737; -.
DR   EnsemblBacteria; BAD04822; BAD04822; PAM_737.
DR   KEGG; poy:PAM_737; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_2_14; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 1502854at2; -.
DR   BioCyc; OYEL262768:G1G26-892-MON; -.
DR   Proteomes; UP000002523; 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..212
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170577"
FT   DOMAIN          7..187
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   212 AA;  24466 MW;  12E96B01513A52E0 CRC64;
     MKLNKKGLLI VLSGPSGVGK ATVRKALFEM TNHNFVYSVS ATTRKPRPGE QDGKDYHFLT
     KEEFEKGIEN NCFLEWAKFI DHYYGTPKKQ IQDFLKQGKE VFLEIEVEGA THLRKKRIPN
     TVFIFLVPPE KKALYDRLKK RGTEQEANIA KRIAKANNEF HLAHKYDYIV VNDEVANAAD
     RIIAIIRAEH AKTKRSIRNY LKILEDNGYA EQ