ID   INGK_ECOL6              Reviewed;         434 AA.
AC   P0AEW7; P22937;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Guanosine-inosine kinase {ECO:0000255|HAMAP-Rule:MF_02246};
DE            EC=2.7.1.73 {ECO:0000255|HAMAP-Rule:MF_02246};
GN   Name=gsk {ECO:0000255|HAMAP-Rule:MF_02246}; OrderedLocusNames=c0597;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP
CC       and IMP, respectively. {ECO:0000255|HAMAP-Rule:MF_02246}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + guanosine = ADP + GMP + H(+); Xref=Rhea:RHEA:27710,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16750, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02246};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + inosine = ADP + H(+) + IMP; Xref=Rhea:RHEA:21140,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17596, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02246};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02246};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from inosine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_02246}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02246}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000305}.
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DR   EMBL; AE014075; AAN79075.1; -; Genomic_DNA.
DR   RefSeq; WP_000671574.1; NC_004431.1.
DR   AlphaFoldDB; P0AEW7; -.
DR   SMR; P0AEW7; -.
DR   STRING; 199310.c0597; -.
DR   PRIDE; P0AEW7; -.
DR   DNASU; 1036004; -.
DR   EnsemblBacteria; AAN79075; AAN79075; c0597.
DR   GeneID; 60903753; -.
DR   KEGG; ecc:c0597; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_060237_0_0_6; -.
DR   OMA; LLGVMCN; -.
DR   BioCyc; ECOL199310:C0597-MON; -.
DR   UniPathway; UPA00591; UER00647.
DR   UniPathway; UPA00909; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106366; F:guanosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008906; F:inosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_02246; Gua_Ino_kinase; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR046405; IngK.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Purine salvage;
KW   Transferase.
FT   CHAIN           1..434
FT                   /note="Guanosine-inosine kinase"
FT                   /id="PRO_0000080072"
FT   BINDING         40..45
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02246"
FT   BINDING         93..97
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02246"
FT   BINDING         198
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02246"
FT   BINDING         284..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02246"
FT   BINDING         357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02246"
FT   BINDING         402
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02246"
SQ   SEQUENCE   434 AA;  48449 MW;  04693F70D1540236 CRC64;
     MKFPGKRKSK HYFPVNARDP LLQQFQPENE TSAAWVVGID QTLVDIEAKV DDEFIERYGL
     SAGHSLVIED DVAEALYQEL KQKNLITHQF AGGTIGNTMH NYSVLADDRS VLLGVMCSNI
     EIGSYAYRYL CNTSSRTDLN YLQGVDGPIG RCFTLIGESG ERTFAISPGH MNQLRAESIP
     EDVIAGASAL VLTSYLVRCK PGEPMPEATM KAIEYAKKYN VPVVLTLGTK FVIAENPQWW
     QQFLKDHVSI LAMNEDEAEA LTGESDPLLA SDKALDWVDL VLCTAGPIGL YMAGFTEDEA
     KRKTQHPLLP GAIAEFNQYE FSRAMRHKDC QNPLRVYSHI APYMGGPEKI MNTNGAGDGA
     LAALLHDITA NSYHRSNVPN SSKHKFTWLT YSSLAQVCKY ANRVSYQVLN QHSPRLTRGL
     PEREDSLEES YWDR