KGUA_ECOLI
ID KGUA_ECOLI Reviewed; 207 AA.
AC P60546; P24234; Q2M7W1;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8 {ECO:0000269|PubMed:8390989};
DE AltName: Full=GMP kinase;
GN Name=gmk; Synonyms=spoR; OrderedLocusNames=b3648, JW3623;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=8390989; DOI=10.1016/s0021-9258(19)85243-2;
RA Gentry D., Bengra C., Ikehara K., Cashel M.;
RT "Guanylate kinase of Escherichia coli K-12.";
RL J. Biol. Chem. 268:14316-14321(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000269|PubMed:8390989}.
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 Evidence={ECO:0000269|PubMed:8390989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20781;
CC Evidence={ECO:0000305|PubMed:8390989};
CC -!- SUBUNIT: Homotetramer (under low ionic conditions) or homodimer (under
CC high ionic conditions). {ECO:0000269|PubMed:8390989}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; M84400; AAB88711.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62001.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76672.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77645.1; -; Genomic_DNA.
DR PIR; S43041; KIECGU.
DR RefSeq; NP_418105.1; NC_000913.3.
DR RefSeq; WP_001295237.1; NZ_STEB01000024.1.
DR PDB; 1S96; X-ray; 2.00 A; A/B=1-207.
DR PDB; 2AN9; X-ray; 2.35 A; A/B=1-207.
DR PDB; 2ANB; X-ray; 2.90 A; A=1-207.
DR PDB; 2ANC; X-ray; 3.20 A; A/B/C/D/E/F=1-207.
DR PDB; 2F3R; X-ray; 2.50 A; A/B=1-207.
DR PDB; 2F3T; X-ray; 3.16 A; A/B/C/D/E/F=1-207.
DR PDBsum; 1S96; -.
DR PDBsum; 2AN9; -.
DR PDBsum; 2ANB; -.
DR PDBsum; 2ANC; -.
DR PDBsum; 2F3R; -.
DR PDBsum; 2F3T; -.
DR AlphaFoldDB; P60546; -.
DR SMR; P60546; -.
DR BioGRID; 4262568; 25.
DR IntAct; P60546; 5.
DR STRING; 511145.b3648; -.
DR ChEMBL; CHEMBL3309016; -.
DR jPOST; P60546; -.
DR PaxDb; P60546; -.
DR PRIDE; P60546; -.
DR EnsemblBacteria; AAC76672; AAC76672; b3648.
DR EnsemblBacteria; BAE77645; BAE77645; BAE77645.
DR GeneID; 66672457; -.
DR GeneID; 948163; -.
DR KEGG; ecj:JW3623; -.
DR KEGG; eco:b3648; -.
DR PATRIC; fig|511145.12.peg.3768; -.
DR EchoBASE; EB0958; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_0_6; -.
DR InParanoid; P60546; -.
DR OMA; EWAVVHG; -.
DR PhylomeDB; P60546; -.
DR BioCyc; EcoCyc:GUANYL-KIN-MON; -.
DR BioCyc; MetaCyc:GUANYL-KIN-MON; -.
DR BRENDA; 2.7.4.8; 2026.
DR EvolutionaryTrace; P60546; -.
DR PRO; PR:P60546; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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..207
FT /note="Guanylate kinase"
FT /id="PRO_0000170534"
FT DOMAIN 4..184
FT /note="Guanylate kinase-like"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2F3T"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1S96"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2AN9"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2AN9"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1S96"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2ANB"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:1S96"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:1S96"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1S96"
SQ SEQUENCE 207 AA; 23593 MW; 62A99DB4063651E4 CRC64;
MAQGTLYIVS APSGAGKSSL IQALLKTQPL YDTQVSVSHT TRQPRPGEVH GEHYFFVNHD
EFKEMISRDA FLEHAEVFGN YYGTSREAIE QVLATGVDVF LDIDWQGAQQ IRQKMPHARS
IFILPPSKIE LDRRLRGRGQ DSEEVIAKRM AQAVAEMSHY AEYDYLIVND DFDTALTDLK
TIIRAERLRM SRQKQRHDAL ISKLLAD
