KGUA_POLSJ
ID KGUA_POLSJ Reviewed; 206 AA.
AC Q12DV7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328};
DE EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328};
DE AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328};
GN Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328}; OrderedLocusNames=Bpro_1335;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000255|HAMAP-Rule:MF_00328}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00328};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00328}.
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DR EMBL; CP000316; ABE43285.1; -; Genomic_DNA.
DR RefSeq; WP_011482284.1; NC_007948.1.
DR AlphaFoldDB; Q12DV7; -.
DR SMR; Q12DV7; -.
DR STRING; 296591.Bpro_1335; -.
DR EnsemblBacteria; ABE43285; ABE43285; Bpro_1335.
DR KEGG; pol:Bpro_1335; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_4; -.
DR OMA; EWAVVHG; -.
DR OrthoDB; 1502854at2; -.
DR Proteomes; UP000001983; 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..206
FT /note="Guanylate kinase"
FT /id="PRO_0000266366"
FT DOMAIN 5..183
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ SEQUENCE 206 AA; 23570 MW; 8D2036DB6C03EAB2 CRC64;
MDYPGNLFVV AAPSGAGKSS LVKALMELDS AIQPAVSHTT RPPRGQEKHG REYFFLSPEE
FDSMVQRDAF LEWAHVHGHR YGTSRQAIEE RIAHGKDVIL EIDFQGAINI KRIFSNAVLI
FILPPSWEEL RSRLQRRGED SPEVIELRLK NAATEMAQAR EFDFVIINEL FERAVFDLKT
IVHAQRLKFS AQRRARAETF RALQIP