KGUA_YERPN
ID KGUA_YERPN Reviewed; 207 AA.
AC Q1CCZ3; D1Q2H0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=YPN_3810;
GN ORFNames=YP516_4330;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG20137.1; -; Genomic_DNA.
DR EMBL; ACNQ01000019; EEO74723.1; -; Genomic_DNA.
DR RefSeq; WP_002209000.1; NZ_ACNQ01000019.1.
DR AlphaFoldDB; Q1CCZ3; -.
DR SMR; Q1CCZ3; -.
DR EnsemblBacteria; ABG20137; ABG20137; YPN_3810.
DR GeneID; 66843567; -.
DR KEGG; ypn:YPN_3810; -.
DR HOGENOM; CLU_001715_1_0_6; -.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000008936; 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..207
FT /note="Guanylate kinase"
FT /id="PRO_0000266440"
FT DOMAIN 4..184
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ SEQUENCE 207 AA; 23504 MW; 01FDCD618EFED91E CRC64;
MVQGTLYIVS APSGAGKSSL IQALLKTQPL YDTQVSISHT TRAKRPGENH GEHYFFVSEK
EFCQMIDDDA FLEHAKVFEN YYGTSRLAIE QVLATGVDVF LDIDWQGAQQ IRAKMPTARS
IFILPPSKTE LDRRLRGRGQ DSEEVIAKRM EQAVAEMAHY AEYDYLIVND DFNLALSDLK
TIIRAERLRL GRQKQRHDAL ISKLLAD