ID   Q0RF84_FRAAA            Unreviewed;       181 AA.
AC   Q0RF84;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 121.
DE   RecName: Full=Guanylate kinase {ECO:0000256|ARBA:ARBA00016296, ECO:0000256|HAMAP-Rule:MF_00328};
DE            EC=2.7.4.8 {ECO:0000256|ARBA:ARBA00012961, ECO:0000256|HAMAP-Rule:MF_00328};
DE   AltName: Full=GMP kinase {ECO:0000256|ARBA:ARBA00030128, ECO:0000256|HAMAP-Rule:MF_00328};
GN   Name=gmk {ECO:0000256|HAMAP-Rule:MF_00328,
GN   ECO:0000313|EMBL:CAJ63864.1};
GN   OrderedLocusNames=FRAAL5231 {ECO:0000313|EMBL:CAJ63864.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63864.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ63864.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45986 / CECT 9034 / ACN14a
RC   {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000256|ARBA:ARBA00003531, ECO:0000256|HAMAP-Rule:MF_00328}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GMP + ATP = GDP + ADP; Xref=Rhea:RHEA:20780,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00048594, ECO:0000256|HAMAP-
CC         Rule:MF_00328};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00005790, ECO:0000256|HAMAP-Rule:MF_00328}.
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DR   EMBL; CT573213; CAJ63864.1; -; Genomic_DNA.
DR   RefSeq; WP_011606324.1; NC_008278.1.
DR   AlphaFoldDB; Q0RF84; -.
DR   STRING; 326424.FRAAL5231; -.
DR   KEGG; fal:FRAAL5231; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_1_11; -.
DR   OrthoDB; 9808150at2; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004385; F:GMP kinase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00071; GMPK; 1.
DR   FunFam; 3.30.63.10:FF:000002; Guanylate kinase 1; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00328}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00328};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00328}; Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00328}.
FT   DOMAIN          1..179
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00328,
FT                   ECO:0000256|PROSITE-ProRule:PRU00100"
SQ   SEQUENCE   181 AA;  19614 MW;  81A6332629E10ED3 CRC64;
     MGLTVLSGPS GVGKGTVVAA VRERHPEVWV SVSATTRAPR PGETDGVEYH FVDAEEFARM
     VKAGEFVEHA MFAGHAYGTP RGPLRERLAA GVPCLLEIEL LGARQVRSAM PDARFVFLAP
     PTFEELVRRL TGRGTESPEV IARRLDRARI ELAAETEFDH VVVNDDVRAA AARLVALMIG
     S
//