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P0A6V9 (GLK_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucokinase

EC=2.7.1.2
Alternative name(s):
Glucose kinase
Gene names
Name:glk
Ordered Locus Names:Z3654, ECs3268
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate. HAMAP-Rule MF_00524

Catalytic activity

ATP + D-glucose = ADP + D-glucose 6-phosphate. HAMAP-Rule MF_00524

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00524.

Sequence similarities

Belongs to the bacterial glucokinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glucokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Glucokinase HAMAP-Rule MF_00524
PRO_0000215125

Regions

Nucleotide binding8 – 136ATP Potential

Secondary structure

.......................................................... 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6V9 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 2D6CD956641A3823

FASTA32134,723
        10         20         30         40         50         60 
MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVIRVYLE EHKVEVKDGC 

        70         80         90        100        110        120 
IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND FTAVSMAIPM LKKEHLIQFG 

       130        140        150        160        170        180 
GAEPVEGKPI AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAPNSEEE AIILEILRAE 

       190        200        210        220        230        240 
IGHVSAERVL SGPGLVNLYR AIVKADNRLP ENLKPKDITE RALADSCTDC RRALSLFCVI 

       250        260        270        280        290        300 
MGRFGGNLAL NLGTFGGVFI AGGIVPRFLE FFKASGFRAA FEDKGRFKEY VHDIPVYLIV 

       310        320 
HDNPGLLGSG AHLRQTLGHI L 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57514.1.
BA000007 Genomic DNA. Translation: BAB36691.1.
PIRD91037.
F85881.
RefSeqNP_288958.1. NC_002655.2.
NP_311295.1. NC_002695.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q18X-ray2.36A/B2-321[»]
1SZ2X-ray2.20A/B2-321[»]
ProteinModelPortalP0A6V9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z3654.

Proteomic databases

PRIDEP0A6V9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57514; AAG57514; Z3654.
BAB36691; BAB36691; BAB36691.
GeneID915629.
961924.
KEGGece:Z3654.
ecs:ECs3268.
PATRIC18355936. VBIEscCol44059_3168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0837.
HOGENOMHOG000274469.
KOK00845.
OMADWVEMTN.
OrthoDBEOG64BQ47.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3222-MONOMER.
ECOO157:GLK-MONOMER.

Family and domain databases

HAMAPMF_00524. Glucokinase.
InterProIPR003836. Glucokinase.
[Graphical view]
PfamPF02685. Glucokinase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00749. glk. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6V9.

Entry information

Entry nameGLK_ECO57
AccessionPrimary (citable) accession number: P0A6V9
Secondary accession number(s): P46880, P78276
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references