KGUA_PARMW
ID KGUA_PARMW Reviewed; 182 AA.
AC Q7U570;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SYNW1837;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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; BX569694; CAE08352.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7U570; -.
DR SMR; Q7U570; -.
DR STRING; 84588.SYNW1837; -.
DR EnsemblBacteria; CAE08352; CAE08352; SYNW1837.
DR KEGG; syw:SYNW1837; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_1_3; -.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000001422; 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; Transferase.
FT CHAIN 1..182
FT /note="Guanylate kinase"
FT /id="PRO_0000170628"
FT DOMAIN 2..180
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ SEQUENCE 182 AA; 20168 MW; 8B824F04F3CE4ED3 CRC64;
MGTLTVITGP SGVGKGTLVQ RLLARNPSIW VSVSATTRAP REGEREGESY FFHSRERFDA
LVQEGGLLEW AEFAGNCYGT PRAPVEQQLQ AGRPVLLEIE LEGARQVRRS FSKARQIFLA
PPSFEELERR IRGRGTDSED AIQQRLLRAR EELSAQGEFD AVVVNDDLDQ ALLKLEGLMG
LG