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P0A6V9

- GLK_ECO57

UniProt

P0A6V9 - GLK_ECO57

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Protein

Glucokinase

Gene

glk

Organism
Escherichia coli O157:H7
Status
Reviewed - 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.

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: Chromosome, UP000002519: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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 – 118
Beta strandi14 – 218
Turni22 – 243
Beta strandi27 – 348
Helixi35 – 373
Helixi41 – 5111
Beta strandi58 – 658
Beta strandi69 – 724
Beta strandi75 – 773
Helixi83 – 908
Beta strandi93 – 997
Helixi100 – 1078
Helixi108 – 1103
Helixi113 – 1153
Beta strandi116 – 1183
Beta strandi130 – 14718
Beta strandi150 – 1556
Helixi158 – 1603
Helixi168 – 18013
Beta strandi181 – 1833
Helixi186 – 1883
Helixi192 – 20514
Helixi215 – 22410
Helixi228 – 25225
Beta strandi257 – 2615
Beta strandi263 – 2653
Helixi266 – 2683
Helixi269 – 2746
Helixi277 – 2826
Helixi285 – 2873
Helixi288 – 2914
Beta strandi296 – 2994
Helixi304 – 31613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiDWVEMTN.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG57514.1 .
BA000007 Genomic DNA. Translation: BAB36691.1 .
PIRi D91037.
F85881.
RefSeqi NP_288958.1. NC_002655.2.
NP_311295.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q18 X-ray 2.36 A/B 2-321 [» ]
1SZ2 X-ray 2.20 A/B 2-321 [» ]
ProteinModelPortali P0A6V9.
SMRi P0A6V9. Positions 2-321.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z3654.

Proteomic databases

PRIDEi P0A6V9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG57514 ; AAG57514 ; Z3654 .
BAB36691 ; BAB36691 ; BAB36691 .
GeneIDi 915629.
961924.
KEGGi ece:Z3654.
ecs:ECs3268.
PATRICi 18355936. VBIEscCol44059_3168.

Phylogenomic databases

eggNOGi COG0837.
HOGENOMi HOG000274469.
KOi K00845.
OMAi DWVEMTN.
OrthoDBi EOG64BQ47.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-3222-MONOMER.
ECOO157:GLK-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6V9.

Family and domain databases

HAMAPi MF_00524. Glucokinase.
InterProi IPR003836. Glucokinase.
[Graphical view ]
Pfami PF02685. Glucokinase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00749. glk. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 63 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