ID   KGUA_SYNE7              Reviewed;         183 AA.
AC   Q8KPQ7; Q31NZ8;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   27-MAR-2024, entry version 107.
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=Synpcc7942_1191; ORFNames=sef0037;
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S.,
RA   Gonzalez A., Salinas I., Golden S.S., Youderian P.;
RT   "Synechococcus elongatus PCC7942 cosmid 7G3.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
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=AAM82712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY120853; AAM82712.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000100; ABB57221.1; -; Genomic_DNA.
DR   RefSeq; WP_011377908.1; NZ_JACJTX010000003.1.
DR   AlphaFoldDB; Q8KPQ7; -.
DR   SMR; Q8KPQ7; -.
DR   STRING; 1140.Synpcc7942_1191; -.
DR   PaxDb; 1140-Synpcc7942_1191; -.
DR   GeneID; 76399931; -.
DR   KEGG; syf:Synpcc7942_1191; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_2_3; -.
DR   OrthoDB; 9808150at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1191-MONOMER; -.
DR   Proteomes; UP000889800; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..183
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170627"
FT   DOMAIN          4..182
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   183 AA;  20305 MW;  B3CDB916A041409B CRC64;
     MSIGRVVVLT GPSGVGKGTL LKAILSQHPE AFLSISATTR SPRPGEVDGQ HYYFLSREEF
     QTKIAEQEFL EWAEFAGNLY GTPRSPVIEQ VNLGRTVILE IELEGARQVR KTLPSARQVM
     LLPPSVEELE RRIRERATED EAAIARRLLQ AQTEIGAAKE FDRCVINDQL DTAITALEAA
     IFS
//