INGK_ECO57
ID INGK_ECO57 Reviewed; 434 AA.
AC P0AEW8; P22937;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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};
GN OrderedLocusNames=Z0596, ECs0530;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54826.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33953.1; -; Genomic_DNA.
DR PIR; B90695; B90695.
DR PIR; F85545; F85545.
DR RefSeq; NP_308557.1; NC_002695.1.
DR RefSeq; WP_000671574.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEW8; -.
DR SMR; P0AEW8; -.
DR STRING; 155864.EDL933_0553; -.
DR EnsemblBacteria; AAG54826; AAG54826; Z0596.
DR EnsemblBacteria; BAB33953; BAB33953; ECs_0530.
DR GeneID; 60903753; -.
DR GeneID; 914634; -.
DR KEGG; ece:Z0596; -.
DR KEGG; ecs:ECs_0530; -.
DR PATRIC; fig|386585.9.peg.637; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_060237_0_0_6; -.
DR OMA; LLGVMCN; -.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 Reference proteome; Transferase.
FT CHAIN 1..434
FT /note="Guanosine-inosine kinase"
FT /id="PRO_0000080071"
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
