ID   KGUA_SYNS3              Reviewed;         190 AA.
AC   Q0I868;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=sync_2153;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00328}.
CC   -!- FUNCTION: (Microbial infection) Catalyzes the phosphorylation of dZMP
CC       to dZDP, when the bacterium is infected by a phage that produces the
CC       substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'-
CC       triphosphate), which is then used by the phage as a DNA polymerase
CC       substrate. {ECO:0000250|UniProtKB:Q9KNM4}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dZMP = ADP + dZDP; Xref=Rhea:RHEA:67640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:172927, ChEBI:CHEBI:172929,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9KNM4};
CC   -!- PATHWAY: Purine metabolism. {ECO:0000250|UniProtKB:Q9KNM4}.
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; CP000435; ABI47312.1; -; Genomic_DNA.
DR   RefSeq; WP_011620066.1; NC_008319.1.
DR   AlphaFoldDB; Q0I868; -.
DR   SMR; Q0I868; -.
DR   STRING; 64471.sync_2153; -.
DR   EnsemblBacteria; ABI47312; ABI47312; sync_2153.
DR   KEGG; syg:sync_2153; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_1_3; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 1502854at2; -.
DR   Proteomes; UP000001961; 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..190
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000266420"
FT   DOMAIN          8..186
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   190 AA;  21070 MW;  64E3D2EF2F6768CD CRC64;
     MAPDGSIARP TVLTGPSGVG KGTLVARLRE RHPEIWLSVS ATTRAPRSGE IDGIHYFFHS
     KERFNKLVQS GGLLEWAEFA GNCYGTPREP VSERVANGIP VLLEIELEGA RQVRKSLPEA
     IQIFLAPPSV EELEKRIRGR GTEAEEAIQR RLKRAQEELE AQTEFDAVIV NDDLETALAE
     LEKQMNLTIS