GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ECOLI:GLPK

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) glpK (ECO:0000255 with HAMAP-Rule:MF_00186)
Protein Name(s) Glycerol kinase (ECO:0000255 with HAMAP-Rule:MF_00186)

ATP:glycerol 3-phosphotransferase (ECO:0000255 with HAMAP-Rule:MF_00186) Glycerokinase (ECO:0000255 with HAMAP-Rule:MF_00186) GK (ECO:0000255 with HAMAP-Rule:MF_00186)

External Links
UniProt P0A6F3
EMBL M18393
M55990
L19201
U00096
AP009048
X15054
U41468
PIR A27339
RefSeq NP_418361.1
YP_491525.1
PDB 1BO5
1BOT
1BU6
1BWF
1GLA
1GLB
1GLC
1GLD
1GLE
1GLF
1GLJ
1GLL
3EZW
PDBsum 1BO5
1BOT
1BU6
1BWF
1GLA
1GLB
1GLC
1GLD
1GLE
1GLF
1GLJ
1GLL
3EZW
ProteinModelPortal P0A6F3
SMR P0A6F3
DIP DIP-36011N
IntAct P0A6F3
STRING 511145.b3926
SWISS-2DPAGE P0A6F3
PaxDb P0A6F3
PRIDE P0A6F3
EnsemblBacteria AAC76908
BAE77384
GeneID 12934168
948423
KEGG ecj:Y75_p3261
eco:b3926
PATRIC 32123365
EchoBASE EB0393
EcoGene EG10398
eggNOG COG0554
HOGENOM HOG000222134
InParanoid P0A6F3
KO K00864
OMA GWVEHEP
OrthoDB EOG6RZB46
PhylomeDB P0A6F3
BioCyc EcoCyc:GLYCEROL-KIN-MONOMER
ECOL316407:JW3897-MONOMER
MetaCyc:GLYCEROL-KIN-MONOMER
UniPathway UPA00618
EvolutionaryTrace P0A6F3
PRO PR:P0A6F3
Proteomes UP000000318
UP000000625
Genevestigator P0A6F3
GO GO:0005829
GO:0005524
GO:0004370
GO:0046872
GO:0008270
GO:0006974
GO:0019563
GO:0006071
GO:0006072
GO:0016310
HAMAP MF_00186
InterPro IPR018485
IPR018483
IPR018484
IPR005999
Pfam PF02782
PF00370
TIGRFAMs TIGR01311
PROSITE PS00933
PS00445

Annotations

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

enables

GO:0008270

zinc ion binding

PMID:8170944[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006071

glycerol metabolic process

PMID:5335908[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004370

glycerol kinase activity

PMID:5335908[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:9817843[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6F3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6F3

F

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:11967071[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:5335908[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019563

glycerol catabolic process

PMID:13930693[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

PMID:5335908[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006071

glycerol metabolic process

PMID:8631672[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:8432702[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004370

glycerol kinase activity

PMID:5335908[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004370

glycerol kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005999

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000577
InterPro:IPR018483
InterPro:IPR018484
InterPro:IPR018485

P

Seeded From UniProt

complete

involved_in

GO:0006072

glycerol-3-phosphate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005999

P

Seeded From UniProt

complete

enables

GO:0016773

phosphotransferase activity, alcohol group as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000577
InterPro:IPR018483
InterPro:IPR018484
InterPro:IPR018485

F

Seeded From UniProt

complete

enables

GO:0004370

glycerol kinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.1.30

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:UR000079255

F

Seeded From UniProt

complete

enables

GO:0004370

glycerol kinase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079255

F

Seeded From UniProt

complete

involved_in

GO:0006072

glycerol-3-phosphate metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079255

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:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

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

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

involved_in

GO:0006071

glycerol metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0319

P

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

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0019563

glycerol catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00618

P

Seeded From UniProt

complete

Notes

References

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

  1. Feese, M et al. (1994) Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 91 3544-8 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 Hayashi, SI & Lin, EC (1967) Purification and properties of glycerol kinase from Escherichia coli. J. Biol. Chem. 242 1030-5 PubMed GONUTS page
  3. 3.0 3.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  4. Feese, MD et al. (1998) Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure 6 1407-18 PubMed GONUTS page
  5. Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
  6. LIN, EC et al. (1962) Utilization of L-alpha-glycerophosphate by Escherichia coli without hydrolysis. Proc. Natl. Acad. Sci. U.S.A. 48 2145-50 PubMed GONUTS page
  7. Pettigrew, DW et al. (1996) A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. J. Bacteriol. 178 2846-52 PubMed GONUTS page
  8. Voegele, RT et al. (1993) Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator. J. Bacteriol. 175 1087-94 PubMed GONUTS page
  9. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  10. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page