ID   KGUA_SYNS9              Reviewed;         187 AA.
AC   Q3AWM1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   24-JAN-2024, entry version 98.
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};
GN   OrderedLocusNames=Syncc9902_1730;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB26687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000097; ABB26687.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041425511.1; NC_007513.1.
DR   AlphaFoldDB; Q3AWM1; -.
DR   SMR; Q3AWM1; -.
DR   STRING; 316279.Syncc9902_1730; -.
DR   KEGG; sye:Syncc9902_1730; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_1_3; -.
DR   OrthoDB; 9808150at2; -.
DR   Proteomes; UP000002712; 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   CDD; cd00071; GMPK; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Transferase.
FT   CHAIN           1..187
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000266422"
FT   DOMAIN          5..183
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   187 AA;  20773 MW;  2A368A73FC0BA2C6 CRC64;
     MAHNGRLTVL TGPSGVGKGT LVKRLLDQHP EIWLSVSATT RQPRAGEEEG VSYFFHPRDT
     FDALVAAGGL LEWAEFASNC YGTPRDPVEE HLAAGRPVLL EIELEGARQV RTSFPDAFQV
     FLAPPSFAEL ERRIRGRGTD TEDAIQRRLA RAREELNAQN EFDAVVVNDD LDQALKQLET
     HMQLQAP
//