KGUA_COXBU
ID KGUA_COXBU Reviewed; 206 AA.
AC Q83EL7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=CBU_0301;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO89858.1; -; Genomic_DNA.
DR RefSeq; NP_819344.1; NC_002971.3.
DR RefSeq; WP_005771415.1; NZ_CDBG01000001.1.
DR PDB; 3TR0; X-ray; 1.85 A; A=1-202.
DR PDBsum; 3TR0; -.
DR AlphaFoldDB; Q83EL7; -.
DR SMR; Q83EL7; -.
DR STRING; 227377.CBU_0301; -.
DR DNASU; 1208183; -.
DR EnsemblBacteria; AAO89858; AAO89858; CBU_0301.
DR GeneID; 1208183; -.
DR KEGG; cbu:CBU_0301; -.
DR PATRIC; fig|227377.7.peg.296; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_6; -.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..206
FT /note="Guanylate kinase"
FT /id="PRO_0000170530"
FT DOMAIN 4..182
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"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3TR0"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3TR0"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3TR0"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3TR0"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3TR0"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:3TR0"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:3TR0"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:3TR0"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:3TR0"
SQ SEQUENCE 206 AA; 23809 MW; 815BFEA7481A0D9C CRC64;
MNKANLFIIS APSGAGKTSL VRALVKALAE IKISISHTTR PKRPGDQEGV DYFFIDETRF
QAMVKEGAFL EHATIYERHY GTEKDWVLRQ LKAGRDVLLE IDWQGARQIR ELFPPALSIF
ILPPSIEALR ERLIKRRQDD TAIIEQRLAL AREEMAHYKE FDYLVVNDNF DQAVQNLIHI
ISAERLQRDV QEKKLSRLLA ELVEKQ
