GNTK_ECOLI
ID GNTK_ECOLI Reviewed; 175 AA.
AC P46859; P78116; Q2M7A0; Q59404;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Thermoresistant gluconokinase;
DE EC=2.7.1.12;
DE AltName: Full=Gluconate kinase 2;
GN Name=gntK; OrderedLocusNames=b3437, JW3400;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9135111; DOI=10.1006/jmbi.1996.0913;
RA Izu H., Adachi O., Yamada M.;
RT "Gene organization and transcriptional regulation of the gntRKU operon
RT involved in gluconate uptake and catabolism of Escherichia coli.";
RL J. Mol. Biol. 267:778-793(1997).
RN [2]
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 [3]
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).
RN [4]
RP PROTEIN SEQUENCE OF 2-20, AND CHARACTERIZATION.
RX PubMed=8655507; DOI=10.1128/jb.178.11.3260-3269.1996;
RA Tong S., Porco A., Isturiz T., Conway T.;
RT "Cloning and molecular genetic characterization of the Escherichia coli
RT gntR, gntK, and gntU genes of GntI, the main system for gluconate
RT metabolism.";
RL J. Bacteriol. 178:3260-3269(1996).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=11468405; DOI=10.1107/s090744490100871x;
RA Kraft L., Sprenger G.A., Lindqvist Y.;
RT "Crystallization and preliminary X-ray crystallographic studies of
RT recombinant thermoresistant gluconate kinase GntK from Escherichia coli.";
RL Acta Crystallogr. D 57:1159-1161(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC EC=2.7.1.12;
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC {ECO:0000305}.
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DR EMBL; D84362; BAA12325.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58235.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76462.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77856.1; -; Genomic_DNA.
DR RefSeq; NP_417894.2; NC_000913.3.
DR RefSeq; WP_000108330.1; NZ_STEB01000004.1.
DR PDB; 1KNQ; X-ray; 2.00 A; A/B=1-175.
DR PDB; 1KO1; X-ray; 2.09 A; A/B=1-175.
DR PDB; 1KO4; X-ray; 2.50 A; A/B=1-175.
DR PDB; 1KO5; X-ray; 2.28 A; A/B=1-175.
DR PDB; 1KO8; X-ray; 2.40 A; A/B=1-175.
DR PDB; 1KOF; X-ray; 2.80 A; A/B=1-175.
DR PDBsum; 1KNQ; -.
DR PDBsum; 1KO1; -.
DR PDBsum; 1KO4; -.
DR PDBsum; 1KO5; -.
DR PDBsum; 1KO8; -.
DR PDBsum; 1KOF; -.
DR AlphaFoldDB; P46859; -.
DR SMR; P46859; -.
DR DIP; DIP-9820N; -.
DR IntAct; P46859; 2.
DR STRING; 511145.b3437; -.
DR DrugBank; DB02076; 6-phospho-D-gluconic acid.
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR jPOST; P46859; -.
DR PaxDb; P46859; -.
DR PRIDE; P46859; -.
DR EnsemblBacteria; AAC76462; AAC76462; b3437.
DR EnsemblBacteria; BAE77856; BAE77856; BAE77856.
DR GeneID; 66672680; -.
DR GeneID; 947937; -.
DR KEGG; ecj:JW3400; -.
DR KEGG; eco:b3437; -.
DR PATRIC; fig|511145.12.peg.3533; -.
DR EchoBASE; EB2513; -.
DR eggNOG; COG3265; Bacteria.
DR HOGENOM; CLU_077168_1_0_6; -.
DR InParanoid; P46859; -.
DR OMA; IQHIWVV; -.
DR PhylomeDB; P46859; -.
DR BioCyc; EcoCyc:GLUCONOKINII-MON; -.
DR BioCyc; MetaCyc:GLUCONOKINII-MON; -.
DR UniPathway; UPA00792; -.
DR EvolutionaryTrace; P46859; -.
DR PRO; PR:P46859; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046316; F:gluconokinase activity; IDA:EcoCyc.
DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02021; GntK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR006001; Therm_gnt_kin.
DR PANTHER; PTHR43442; PTHR43442; 1.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01313; therm_gnt_kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8655507"
FT CHAIN 2..175
FT /note="Thermoresistant gluconokinase"
FT /id="PRO_0000087537"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1KNQ"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 59..79
FT /evidence="ECO:0007829|PDB:1KNQ"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:1KNQ"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1KNQ"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1KNQ"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:1KNQ"
SQ SEQUENCE 175 AA; 19543 MW; 5859A38413E8A586 CRC64;
MSTTNHDHHI YVLMGVSGSG KSAVASEVAH QLHAAFLDGD FLHPRRNIEK MASGEPLNDD
DRKPWLQALN DAAFAMQRTN KVSLIVCSAL KKHYRDLLRE GNPNLSFIYL KGDFDVIESR
LKARKGHFFK TQMLVTQFET LQEPGADETD VLVVDIDQPL EGVVASTIEV IKKGK
