ID   KGUA_VIBCH              Reviewed;         207 AA.
AC   Q9KNM4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=VC_2708;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   FUNCTION (MICROBIAL INFECTION), AND CATALYTIC ACTIVITY (MICROBIAL
RP   INFECTION).
RX   PubMed=33926955; DOI=10.1126/science.abe6494;
RA   Sleiman D., Garcia P.S., Lagune M., Loc'h J., Haouz A., Taib N.,
RA   Roethlisberger P., Gribaldo S., Marliere P., Kaminski P.A.;
RT   "A third purine biosynthetic pathway encoded by aminoadenine-based viral
RT   DNA genomes.";
RL   Science 372:516-520(2021).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000250}.
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:0000269|PubMed:33926955}.
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;
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:0000269|PubMed:33926955};
CC   -!- PATHWAY: Purine metabolism. {ECO:0000269|PubMed:33926955}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF95848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF95848.1; ALT_INIT; Genomic_DNA.
DR   PIR; H82043; H82043.
DR   RefSeq; NP_232335.2; NC_002505.1.
DR   RefSeq; WP_000515790.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KNM4; -.
DR   SMR; Q9KNM4; -.
DR   STRING; 243277.VC_2708; -.
DR   PRIDE; Q9KNM4; -.
DR   DNASU; 2615536; -.
DR   EnsemblBacteria; AAF95848; AAF95848; VC_2708.
DR   GeneID; 57741301; -.
DR   KEGG; vch:VC_2708; -.
DR   PATRIC; fig|243277.26.peg.2583; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_0_6; -.
DR   OMA; EWAVVHG; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..207
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170636"
FT   DOMAIN          4..184
FT                   /note="Guanylate kinase-like"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  23333 MW;  0A007962E1B583F3 CRC64;
     MGKGTLYIVS APSGAGKSSL IAALLEQNPT YAMKVSVSHT TRGMRPGEQD GVHYHFVEKE
     HFIELIGKGE FLEYAEVFGN YYGTSRVWIE NTLNKGIDVF LDIDWQGARQ IRSQMPEAKS
     IFILPPSKEE LERRLNTRGQ DSDAVIAKRM GEAKSEISHY SEYDYVIIND DFDVALMDFK
     AIIRAERLKQ DKQAAKYSAM LSALLAE