KGUA_THEMA
ID KGUA_THEMA Reviewed; 207 AA.
AC Q9X215;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=gmk; OrderedLocusNames=TM_1689;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(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}.
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DR EMBL; AE000512; AAD36756.1; -; Genomic_DNA.
DR PIR; C72223; C72223.
DR RefSeq; NP_229489.1; NC_000853.1.
DR RefSeq; WP_004082205.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X215; -.
DR SMR; Q9X215; -.
DR STRING; 243274.THEMA_05795; -.
DR EnsemblBacteria; AAD36756; AAD36756; TM_1689.
DR KEGG; tma:TM1689; -.
DR eggNOG; COG0194; Bacteria.
DR InParanoid; Q9X215; -.
DR OMA; EWAVVHG; -.
DR OrthoDB; 1502854at2; -.
DR Proteomes; UP000008183; Chromosome.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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..207
FT /note="Guanylate kinase"
FT /id="PRO_0000170630"
FT DOMAIN 3..181
FT /note="Guanylate kinase-like"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 24037 MW; E38375CFF2E26963 CRC64;
MKGQLFVICG PSGAGKTSII KEVLKRLDNV VFSVSCTTRP KRPHEEDGKD YFFITEEEFL
KRVERGEFLE WARVHGHLYG TLRSFVESHI NEGKDVVLDI DVQGALSVKK KYSNTVFIYV
APPSYADLRE RILKRGTEKE ADVLVRLENA KWELMFMDEF DYIVVNENLE DAVEMVVSIV
RSERAKVTRN QDKIERFKME VKGWKKL
