ID   KGUA_DEIRA              Reviewed;         239 AA.
AC   Q9RS38;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=DR_2289;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF11836.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000513; AAF11836.1; ALT_INIT; Genomic_DNA.
DR   PIR; C75291; C75291.
DR   RefSeq; NP_296010.1; NC_001263.1.
DR   RefSeq; WP_027480091.1; NC_001263.1.
DR   AlphaFoldDB; Q9RS38; -.
DR   SMR; Q9RS38; -.
DR   STRING; 243230.DR_2289; -.
DR   EnsemblBacteria; AAF11836; AAF11836; DR_2289.
DR   KEGG; dra:DR_2289; -.
DR   PATRIC; fig|243230.17.peg.2518; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_1_0; -.
DR   InParanoid; Q9RS38; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 1502854at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..239
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170531"
FT   DOMAIN          19..197
FT                   /note="Guanylate kinase-like"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  26528 MW;  930AE5040D622722 CRC64;
     MMASAPQDRP AGTPPQGRGL LIVVTGASGV GKGTLRERWL AGQDVFYSTS WTTREPRPGE
     VNGRDYVFVS PAEFLAKAQQ NGFLEHAQFV GNHYGTPIEP IEAALERGQD VVLEIEVEGA
     MQVKDRMGEQ AILVFIMPPS LTELRRRLTG RATETPERIE KRLTRARDEI QAAHDFRYVI
     VNDNLDRAVS ELLAVQQAER AAQKAAEHWT PEEQQARALA DTVRSTALSR EALQQVVES