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ECOLI:GLK

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) glk
Protein Name(s) Glucokinase

Glucose kinase

External Links
UniProt P0A6V8
EMBL U22490
U00096
AP009048
PIR A65013
RefSeq NP_416889.1
YP_490630.1
ProteinModelPortal P0A6V8
SMR P0A6V8
IntAct P0A6V8
STRING 511145.b2388
PaxDb P0A6V8
PRIDE P0A6V8
EnsemblBacteria AAC75447
BAA16258
GeneID 12931569
946858
KEGG ecj:Y75_p2355
eco:b2388
PATRIC 32120155
EchoBASE EB2791
EcoGene EG12957
eggNOG COG0837
HOGENOM HOG000274469
InParanoid P0A6V8
KO K00845
OMA GHADFAP
OrthoDB EOG64BQ47
PhylomeDB P0A6V8
BioCyc EcoCyc:GLUCOKIN-MONOMER
ECOL316407:JW2385-MONOMER
MetaCyc:GLUCOKIN-MONOMER
SABIO-RK P0A6V8
PRO PR:P0A6V8
Proteomes UP000000318
UP000000625
Genevestigator P0A6V8
GO GO:0005737
GO:0005524
GO:0004340
GO:0006096
HAMAP MF_00524
InterPro IPR003836
Pfam PF02685
TIGRFAMs TIGR00749

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004340

glucokinase activity

PMID:1097393[1]

ECO:0000316

UniProtKB:P69797


F

table two: gpt glk mpt = no glucose activity

complete

GO:0004340

glucokinase activity

PMID:9023215[2]

ECO:0000315

F

In Table 2, the overexpression of glk using a plasmid-encoded glk leads to an increased amount of glucokinase activity.

complete

involved_in

GO:0006096

glycolytic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12957
PANTHER:PTN000775530

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12957
PANTHER:PTN000775530

C

Seeded From UniProt

complete

enables

GO:0004340

glucokinase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12957
PANTHER:PTN000775530

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004340

glucokinase activity

PMID:17307338[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004340

glucokinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003836

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003836

F

Seeded From UniProt

complete

enables

GO:0005536

glucose binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003836

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003836

P

Seeded From UniProt

complete

involved_in

GO:0051156

glucose 6-phosphate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003836

P

Seeded From UniProt

complete

enables

GO:0004340

glucokinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.1.2

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094080

C

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094080

P

Seeded From UniProt

complete

enables

GO:0004340

glucokinase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094080

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094080

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Curtis, SJ & Epstein, W (1975) Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase. J. Bacteriol. 122 1189-99 PubMed GONUTS page
  2. Meyer, D et al. (1997) Molecular characterization of glucokinase from Escherichia coli K-12. J. Bacteriol. 179 1298-306 PubMed GONUTS page
  3. 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  5. Ogawa, T et al. (2007) Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli. Res. Microbiol. 158 159-63 PubMed GONUTS page