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Protein

Thermoresistant gluconokinase

Gene

gntK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + D-gluconate = ADP + 6-phospho-D-gluconate.

Pathwayi: D-gluconate degradation

This protein is involved in the pathway D-gluconate degradation, which is part of Carbohydrate acid metabolism.
View all proteins of this organism that are known to be involved in the pathway D-gluconate degradation and in Carbohydrate acid metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • gluconokinase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLUCONOKINII-MONOMER.
ECOL316407:JW3400-MONOMER.
MetaCyc:GLUCONOKINII-MONOMER.
UniPathwayiUPA00792.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermoresistant gluconokinase (EC:2.7.1.12)
Alternative name(s):
Gluconate kinase 2
Gene namesi
Name:gntK
Ordered Locus Names:b3437, JW3400
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12629. gntK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 175174Thermoresistant gluconokinasePRO_0000087537Add
BLAST

Proteomic databases

PaxDbiP46859.
PRIDEiP46859.

Interactioni

Protein-protein interaction databases

DIPiDIP-9820N.
IntActiP46859. 2 interactions.
STRINGi511145.b3437.

Structurei

Secondary structure

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Helixi21 – 3212Combined sources
Beta strandi35 – 384Combined sources
Helixi39 – 424Combined sources
Helixi45 – 528Combined sources
Helixi59 – 7921Combined sources
Beta strandi81 – 866Combined sources
Helixi92 – 998Combined sources
Beta strandi105 – 1117Combined sources
Helixi114 – 1229Combined sources
Helixi131 – 14010Combined sources
Beta strandi151 – 1555Combined sources
Helixi160 – 17213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNQX-ray2.00A/B1-175[»]
1KO1X-ray2.09A/B1-175[»]
1KO4X-ray2.50A/B1-175[»]
1KO5X-ray2.28A/B1-175[»]
1KO8X-ray2.40A/B1-175[»]
1KOFX-ray2.80A/B1-175[»]
ProteinModelPortaliP46859.
SMRiP46859. Positions 3-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46859.

Family & Domainsi

Sequence similaritiesi

Belongs to the gluconokinase GntK/GntV family.Curated

Phylogenomic databases

eggNOGiENOG4108Z67. Bacteria.
COG3265. LUCA.
HOGENOMiHOG000032567.
InParanoidiP46859.
KOiK00851.
OMAiMYCGGTT.
OrthoDBiEOG6XHC8K.
PhylomeDBiP46859.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR031322. Shikimate/glucono_kinase.
IPR006001. Therm_gnt_kin.
[Graphical view]
PfamiPF01202. SKI. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01313. therm_gnt_kin. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTNHDHHI YVLMGVSGSG KSAVASEVAH QLHAAFLDGD FLHPRRNIEK
60 70 80 90 100
MASGEPLNDD DRKPWLQALN DAAFAMQRTN KVSLIVCSAL KKHYRDLLRE
110 120 130 140 150
GNPNLSFIYL KGDFDVIESR LKARKGHFFK TQMLVTQFET LQEPGADETD
160 170
VLVVDIDQPL EGVVASTIEV IKKGK
Length:175
Mass (Da):19,543
Last modified:January 23, 2007 - v4
Checksum:i5859A38413E8A586
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84362 Genomic DNA. Translation: BAA12325.1.
U18997 Genomic DNA. Translation: AAA58235.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76462.2.
AP009048 Genomic DNA. Translation: BAE77856.1.
RefSeqiNP_417894.2. NC_000913.3.
WP_000108330.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76462; AAC76462; b3437.
BAE77856; BAE77856; BAE77856.
GeneIDi947937.
KEGGiecj:JW3400.
eco:b3437.
PATRICi32122312. VBIEscCol129921_3533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84362 Genomic DNA. Translation: BAA12325.1.
U18997 Genomic DNA. Translation: AAA58235.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76462.2.
AP009048 Genomic DNA. Translation: BAE77856.1.
RefSeqiNP_417894.2. NC_000913.3.
WP_000108330.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNQX-ray2.00A/B1-175[»]
1KO1X-ray2.09A/B1-175[»]
1KO4X-ray2.50A/B1-175[»]
1KO5X-ray2.28A/B1-175[»]
1KO8X-ray2.40A/B1-175[»]
1KOFX-ray2.80A/B1-175[»]
ProteinModelPortaliP46859.
SMRiP46859. Positions 3-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9820N.
IntActiP46859. 2 interactions.
STRINGi511145.b3437.

Proteomic databases

PaxDbiP46859.
PRIDEiP46859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76462; AAC76462; b3437.
BAE77856; BAE77856; BAE77856.
GeneIDi947937.
KEGGiecj:JW3400.
eco:b3437.
PATRICi32122312. VBIEscCol129921_3533.

Organism-specific databases

EchoBASEiEB2513.
EcoGeneiEG12629. gntK.

Phylogenomic databases

eggNOGiENOG4108Z67. Bacteria.
COG3265. LUCA.
HOGENOMiHOG000032567.
InParanoidiP46859.
KOiK00851.
OMAiMYCGGTT.
OrthoDBiEOG6XHC8K.
PhylomeDBiP46859.

Enzyme and pathway databases

UniPathwayiUPA00792.
BioCyciEcoCyc:GLUCONOKINII-MONOMER.
ECOL316407:JW3400-MONOMER.
MetaCyc:GLUCONOKINII-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP46859.
PROiP46859.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR031322. Shikimate/glucono_kinase.
IPR006001. Therm_gnt_kin.
[Graphical view]
PfamiPF01202. SKI. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01313. therm_gnt_kin. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene organization and transcriptional regulation of the gntRKU operon involved in gluconate uptake and catabolism of Escherichia coli."
    Izu H., Adachi O., Yamada M.
    J. Mol. Biol. 267:778-793(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Cloning and molecular genetic characterization of the Escherichia coli gntR, gntK, and gntU genes of GntI, the main system for gluconate metabolism."
    Tong S., Porco A., Isturiz T., Conway T.
    J. Bacteriol. 178:3260-3269(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20, CHARACTERIZATION.
  5. "Crystallization and preliminary X-ray crystallographic studies of recombinant thermoresistant gluconate kinase GntK from Escherichia coli."
    Kraft L., Sprenger G.A., Lindqvist Y.
    Acta Crystallogr. D 57:1159-1161(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.

Entry informationi

Entry nameiGNTK_ECOLI
AccessioniPrimary (citable) accession number: P46859
Secondary accession number(s): P78116, Q2M7A0, Q59404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.