KGUA_HELPJ
ID KGUA_HELPJ Reviewed; 206 AA.
AC Q9ZMB7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=gmk; OrderedLocusNames=jhp_0304;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(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; AE001439; AAD05889.1; -; Genomic_DNA.
DR PIR; B71948; B71948.
DR RefSeq; WP_001058030.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZMB7; -.
DR SMR; Q9ZMB7; -.
DR STRING; 85963.jhp_0304; -.
DR EnsemblBacteria; AAD05889; AAD05889; jhp_0304.
DR GeneID; 66521570; -.
DR KEGG; hpj:jhp_0304; -.
DR PATRIC; fig|85963.30.peg.709; -.
DR eggNOG; COG0194; Bacteria.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000000804; 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..206
FT /note="Guanylate kinase"
FT /id="PRO_0000170548"
FT DOMAIN 5..183
FT /note="Guanylate kinase-like"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 23793 MW; 3A04A819DAA1D752 CRC64;
MNNDFNLLIL SGPSGAGKST LTKYLQEKIP KTHFSLSTTT RKPREGEVDG LHYNFVSEEE
FKQGIEKGQF LEWAIVHNHY YGTSKIPVEK ALKEGKIVIF DIDVQGHEIL KKHYPNACSV
FISTKNQEIL KERLLLRGTD SKETIEKRLI NAYKEMQCLE SFDYLIINED LEKSKEIILS
IAKTLVHRLK AFNFEKICKA WKNESL