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Protein

Glucokinase

Gene

glk

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate.

Catalytic activityi

ATP + D-glucose = ADP + D-glucose 6-phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 136ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glucokinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3222-MONOMER.
ECOO157:GLK-MONOMER.
BRENDAi2.7.1.2. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucokinase (EC:2.7.1.2)
Alternative name(s):
Glucose kinase
Gene namesi
Name:glk
Ordered Locus Names:Z3654, ECs3268
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558 Componenti: Chromosome UP000002519 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321GlucokinasePRO_0000215125Add
BLAST

Proteomic databases

PRIDEiP0A6V9.

Interactioni

Protein-protein interaction databases

STRINGi155864.Z3654.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi14 – 218Combined sources
Turni22 – 243Combined sources
Beta strandi27 – 348Combined sources
Helixi35 – 373Combined sources
Helixi41 – 5111Combined sources
Beta strandi58 – 658Combined sources
Beta strandi69 – 724Combined sources
Beta strandi75 – 773Combined sources
Helixi83 – 908Combined sources
Beta strandi93 – 997Combined sources
Helixi100 – 1078Combined sources
Helixi108 – 1103Combined sources
Helixi113 – 1153Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi130 – 14718Combined sources
Beta strandi150 – 1556Combined sources
Helixi158 – 1603Combined sources
Helixi168 – 18013Combined sources
Beta strandi181 – 1833Combined sources
Helixi186 – 1883Combined sources
Helixi192 – 20514Combined sources
Helixi215 – 22410Combined sources
Helixi228 – 25225Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi263 – 2653Combined sources
Helixi266 – 2683Combined sources
Helixi269 – 2746Combined sources
Helixi277 – 2826Combined sources
Helixi285 – 2873Combined sources
Helixi288 – 2914Combined sources
Beta strandi296 – 2994Combined sources
Helixi304 – 31613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q18X-ray2.36A/B2-321[»]
1SZ2X-ray2.20A/B2-321[»]
ProteinModelPortaliP0A6V9.
SMRiP0A6V9. Positions 2-321.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6V9.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial glucokinase family.Curated

Phylogenomic databases

eggNOGiCOG0837.
HOGENOMiHOG000274469.
KOiK00845.
OMAiGHADFAP.
OrthoDBiEOG64BQ47.

Family and domain databases

HAMAPiMF_00524. Glucokinase.
InterProiIPR003836. Glucokinase.
[Graphical view]
PfamiPF02685. Glucokinase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00749. glk. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6V9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVIRVYLE
60 70 80 90 100
EHKVEVKDGC IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND
110 120 130 140 150
FTAVSMAIPM LKKEHLIQFG GAEPVEGKPI AVYGAGTGLG VAHLVHVDKR
160 170 180 190 200
WVSLPGEGGH VDFAPNSEEE AIILEILRAE IGHVSAERVL SGPGLVNLYR
210 220 230 240 250
AIVKADNRLP ENLKPKDITE RALADSCTDC RRALSLFCVI MGRFGGNLAL
260 270 280 290 300
NLGTFGGVFI AGGIVPRFLE FFKASGFRAA FEDKGRFKEY VHDIPVYLIV
310 320
HDNPGLLGSG AHLRQTLGHI L
Length:321
Mass (Da):34,723
Last modified:March 29, 2005 - v1
Checksum:i2D6CD956641A3823
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57514.1.
BA000007 Genomic DNA. Translation: BAB36691.1.
PIRiD91037.
F85881.
RefSeqiNP_288958.1. NC_002655.2.
NP_311295.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG57514; AAG57514; Z3654.
BAB36691; BAB36691; BAB36691.
GeneIDi915629.
961924.
KEGGiece:Z3654.
ecs:ECs3268.
PATRICi18355936. VBIEscCol44059_3168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57514.1.
BA000007 Genomic DNA. Translation: BAB36691.1.
PIRiD91037.
F85881.
RefSeqiNP_288958.1. NC_002655.2.
NP_311295.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q18X-ray2.36A/B2-321[»]
1SZ2X-ray2.20A/B2-321[»]
ProteinModelPortaliP0A6V9.
SMRiP0A6V9. Positions 2-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z3654.

Proteomic databases

PRIDEiP0A6V9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57514; AAG57514; Z3654.
BAB36691; BAB36691; BAB36691.
GeneIDi915629.
961924.
KEGGiece:Z3654.
ecs:ECs3268.
PATRICi18355936. VBIEscCol44059_3168.

Phylogenomic databases

eggNOGiCOG0837.
HOGENOMiHOG000274469.
KOiK00845.
OMAiGHADFAP.
OrthoDBiEOG64BQ47.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3222-MONOMER.
ECOO157:GLK-MONOMER.
BRENDAi2.7.1.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A6V9.

Family and domain databases

HAMAPiMF_00524. Glucokinase.
InterProiIPR003836. Glucokinase.
[Graphical view]
PfamiPF02685. Glucokinase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00749. glk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
  3. "Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose."
    Lunin V.V., Li Y., Schrag J.D., Iannuzzi P., Cygler M., Matte A.
    J. Bacteriol. 186:6915-6927(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiGLK_ECO57
AccessioniPrimary (citable) accession number: P0A6V9
Secondary accession number(s): P46880, P78276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 1, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.