ID KGUA_MYCGA Reviewed; 195 AA.
AC Q9KX62;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=gmk; OrderedLocusNames=MYCGA6400; ORFNames=MGA_0462;
OS Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasma gallisepticum).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RA Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; L35043; AAF36761.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56990.1; -; Genomic_DNA.
DR RefSeq; WP_011113900.1; NC_004829.2.
DR AlphaFoldDB; Q9KX62; -.
DR SMR; Q9KX62; -.
DR KEGG; mga:MGA_0462; -.
DR PATRIC; fig|233150.7.peg.717; -.
DR HOGENOM; CLU_001715_1_1_14; -.
DR OrthoDB; 9808150at2; -.
DR Proteomes; UP000001418; 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 CDD; cd00071; GMPK; 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; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..195
FT /note="Guanylate kinase"
FT /id="PRO_0000170561"
FT DOMAIN 12..191
FT /note="Guanylate kinase-like"
FT BINDING 19..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 120
FT /note="R -> K (in Ref. 1; AAF36761)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="L -> R (in Ref. 1; AAF36761)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="N -> S (in Ref. 1; AAF36761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 22473 MW; 6AB0B0FBF9A66573 CRC64;
MVVIYIMSNK QGLIILISGP SGVGKGTIVS RLLSDNNLKL NVSISATTRK KRASEVEGVH
YFFKTKEEFE QMIANNQLLE YANYVNNYYG TPLSLVKEIL DKNENLILEI EYQGVIQVLR
KGFRTLSIFV LPPSEDELVA RLKKRGTEND EVIKHRLEQA VKEYAHRELY DHTIINDDLE
KTIEDIKQLI LKYNQ
//
