KGUA_LISMO
ID KGUA_LISMO Reviewed; 205 AA.
AC Q8Y672;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=lmo1827;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL591981; CAC99905.1; -; Genomic_DNA.
DR PIR; AC1303; AC1303.
DR RefSeq; NP_465352.1; NC_003210.1.
DR RefSeq; WP_003725659.1; NZ_CP023861.1.
DR PDB; 3TAU; X-ray; 2.05 A; A/B=1-205.
DR PDBsum; 3TAU; -.
DR AlphaFoldDB; Q8Y672; -.
DR SMR; Q8Y672; -.
DR STRING; 169963.lmo1827; -.
DR PaxDb; Q8Y672; -.
DR EnsemblBacteria; CAC99905; CAC99905; CAC99905.
DR GeneID; 985464; -.
DR KEGG; lmo:lmo1827; -.
DR PATRIC; fig|169963.11.peg.1872; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_9; -.
DR OMA; EWAVVHG; -.
DR PhylomeDB; Q8Y672; -.
DR BioCyc; LMON169963:LMO1827-MON; -.
DR Proteomes; UP000000817; 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..205
FT /note="Guanylate kinase"
FT /id="PRO_0000170558"
FT DOMAIN 5..184
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"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:3TAU"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3TAU"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:3TAU"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3TAU"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3TAU"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:3TAU"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3TAU"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3TAU"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:3TAU"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3TAU"
SQ SEQUENCE 205 AA; 23282 MW; 40579D7F0038C9E1 CRC64;
MTERGLLIVL SGPSGVGKGT VREAVFKDPE TSFDYSISMT TRLPREGEQD GVDYYFRSRE
VFEQAIKDGK MLEYAEYVGN YYGTPLEYVE EKLAAGVDIF LEIEVQGAMQ VRKAMPEGIF
IFLTPPDLSE LKNRIIGRGT ESMEVVEERM ETAKKEIEMM ASYDYAVVND VVANAVQKIK
GIVETEHLKT ERVIHRYKKM LEGLQ
