ID   KGUA_BUCAI              Reviewed;         207 AA.
AC   P57509;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=BU434;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13132.1; -; Genomic_DNA.
DR   RefSeq; NP_240246.1; NC_002528.1.
DR   RefSeq; WP_009874387.1; NC_002528.1.
DR   AlphaFoldDB; P57509; -.
DR   SMR; P57509; -.
DR   STRING; 107806.10039098; -.
DR   EnsemblBacteria; BAB13132; BAB13132; BAB13132.
DR   KEGG; buc:BU434; -.
DR   PATRIC; fig|107806.10.peg.443; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_0_6; -.
DR   OMA; EWAVVHG; -.
DR   Proteomes; UP000001806; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..207
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170510"
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;  24092 MW;  0478657C73697655 CRC64;
     MSEGILFIIS APSGTGKSSL IQGLLKSKTL YNTRVSISHT TRIIRPGELH GKHYYFISKK
     EFEIMIKQEY FLEYAKVFSN YYGTSRKYIE KMLFSGIDVF LDIDWQGAKQ IKCKMPKSKS
     IFLLPPSKDT LYKRLRERGQ DSDSVIANRM EKAVDEMQHY SEYDYLIIND DFKQAVNDLI
     TIITAEHLCL FHQKNKHNLL ISNLLKC