UniProtKB - P0A6F3 (GLPK_ECOLI)
Protein
Glycerol kinase
Gene
glpK
Organism
Escherichia coli (strain K12)
Status
Functioni
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP.UniRule annotation3 Publications
Catalytic activityi
- EC:2.7.1.30UniRule annotation1 Publication
Activity regulationi
Activity of this regulatory enzyme is affected by several metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) causes alterations in the quaternary structure of the enzyme. FBP inhibition requires that the enzyme exist only in a tetrameric state. Salt such as KCl reduces the affinity of the tetrameric form of the enzyme for FBP. Unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system, also inhibits non-competitively and allostericaly the activity. Unlike FBP, both the dimer and the tetramer appear to be fully sensitive to enzyme EIIA-Glc inhibition. Zn(+2) greatly enhances the inhibitory potency of EIIA-Glc. Both allosteric regulatory agents is strongly pH dependent, with maximal inhibition occurring at pH 6.5.8 Publications
Kineticsi
- KM=1.3 µM for glycerol4 Publications
- KM=400 µM for D-glyceraldehyde4 Publications
- KM=500 µM for dihydroxyacetone4 Publications
- KM=3 mM for L-glyceraldehyde4 Publications
- KM=4 mM for ATP4 Publications
pH dependencei
Optimum pH is 9.8.4 Publications
: glycerol degradation via glycerol kinase pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes sn-glycerol 3-phosphate from glycerol.UniRule annotationProteins known to be involved in this subpathway in this organism are:
- Glycerol kinase (glpK), Glycerol kinase (glpK)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sn-glycerol 3-phosphate from glycerol, the pathway glycerol degradation via glycerol kinase pathway and in Polyol metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 14 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 18 | ATP | 1 | |
Binding sitei | 136 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 268 | ATP | 1 | |
Binding sitei | 311 | ATP; via carbonyl oxygen | 1 | |
Binding sitei | 315 | ATP; via amide nitrogen | 1 | |
Binding sitei | 330 | ATP | 1 | |
Metal bindingi | 479 | Zinc; shared with EIIA-Glc | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 14 – 16 | ATP | 3 | |
Nucleotide bindingi | 412 – 416 | ATP | 5 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- glycerol kinase activity Source: UniProtKB
- identical protein binding Source: IntAct
- metal ion binding Source: EcoCyc
- zinc ion binding Source: UniProtKB
GO - Biological processi
- cellular response to DNA damage stimulus Source: EcoliWiki
- glycerol-3-phosphate metabolic process Source: UniProtKB-UniRule
- glycerol catabolic process Source: EcoCyc
- glycerol metabolic process Source: UniProtKB
- phosphorylation Source: EcoCyc
Keywordsi
Molecular function | Allosteric enzyme, Kinase, Transferase |
Biological process | Glycerol metabolism |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:GLYCEROL-KIN-MONOMER MetaCyc:GLYCEROL-KIN-MONOMER |
BRENDAi | 2.7.1.30, 2026 |
UniPathwayi | UPA00618;UER00672 |
Chemistry databases
SwissLipidsi | SLP:000001805 |
Names & Taxonomyi
Protein namesi | Recommended name: Glycerol kinaseUniRule annotation (EC:2.7.1.30UniRule annotation)Alternative name(s): ATP:glycerol 3-phosphotransferaseUniRule annotation GlycerokinaseUniRule annotation Short name: GKUniRule annotation |
Gene namesi | Name:glpKUniRule annotation Ordered Locus Names:b3926, JW3897 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 59 | S → W: Abolishes inhibition of GK by FBP via disruption of the dimer-tetramer assembly reaction. Inhibition by EIIA-Glc is unchanged compared to wild type. The activity of this mutant is significantly higher than wild-type, and the Michaelis constants are increased slightly compared to wild-type. 1 Publication | 1 | |
Mutagenesisi | 66 | A → T: Although it completely abolishes FBP regulation and disruptes dimer-tetramer equilibrium, the crystal structure is essentially identical to the symmetric tetramer found in the FBP-bound form of the enzyme. 1 Publication | 1 | |
Mutagenesisi | 231 | G → D: Displays an increased enzymatic activity and a decreased allosteric regulation by FBP compared to wild-type. It displays a dimer form and is resistant to tetramer formation in the presence of FBP, whereas wild-type dimers are converted into inactive tetramers in the presence of FBP. 1 Publication | 1 | |
Mutagenesisi | 237 | R → A: Drastically reduces inhibition of GK by FBP and lowers, but did not eliminate, the ability of FBP to promote tetramer association. 1 Publication | 1 | |
Mutagenesisi | 305 | G → S in glpK22; abolishes glucose control of glycerol utilization. | 1 | |
Mutagenesisi | 475 | I → D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. It increases the affinity for FBP about fivefold. 1 Publication | 1 | |
Mutagenesisi | 480 | R → D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. Regulation by FBP is not affected by this substitution. No inhibition by EIIA-Glc is observed, which is consistent with a decrease in affinity for EIIA-Glc of about 250-fold. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04551, beta-D-fructofuranose 1,6-bisphosphate DB02937, Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000059451 | 2 – 502 | Glycerol kinaseAdd BLAST | 501 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 233 | N6-malonyllysine1 Publication | 1 |
Proteomic databases
jPOSTi | P0A6F3 |
PaxDbi | P0A6F3 |
PRIDEi | P0A6F3 |
2D gel databases
SWISS-2DPAGEi | P0A6F3 |
Expressioni
Inductioni
By L-alpha-glycerol 3-phosphate.1 Publication
Interactioni
Subunit structurei
Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc (crr). Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
UniRule annotation9 PublicationsBinary interactionsi
P0A6F3
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-548038,EBI-548038 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4263162, 380 interactors |
DIPi | DIP-36011N |
IntActi | P0A6F3, 15 interactors |
STRINGi | 511145.b3926 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A6F3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6F3 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 84 – 85 | Substrate binding | 2 | |
Regioni | 234 – 236 | Allosteric FBP inhibitor binding | 3 | |
Regioni | 246 – 247 | Substrate binding | 2 |
Sequence similaritiesi
Belongs to the FGGY kinase family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0554, Bacteria |
HOGENOMi | CLU_009281_2_3_6 |
InParanoidi | P0A6F3 |
PhylomeDBi | P0A6F3 |
Family and domain databases
HAMAPi | MF_00186, Glycerol_kin, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR000577, Carb_kinase_FGGY IPR018485, Carb_kinase_FGGY_C IPR018483, Carb_kinase_FGGY_CS IPR018484, Carb_kinase_FGGY_N IPR005999, Glycerol_kin |
Pfami | View protein in Pfam PF02782, FGGY_C, 1 hit PF00370, FGGY_N, 1 hit |
PIRSFi | PIRSF000538, GlpK, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
TIGRFAMsi | TIGR01311, glycerol_kin, 1 hit |
PROSITEi | View protein in PROSITE PS00933, FGGY_KINASES_1, 1 hit PS00445, FGGY_KINASES_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A6F3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTEKKYIVAL DQGTTSSRAV VMDHDANIIS VSQREFEQIY PKPGWVEHDP
60 70 80 90 100
MEIWATQSST LVEVLAKADI SSDQIAAIGI TNQRETTIVW EKETGKPIYN
110 120 130 140 150
AIVWQCRRTA EICEHLKRDG LEDYIRSNTG LVIDPYFSGT KVKWILDHVE
160 170 180 190 200
GSRERARRGE LLFGTVDTWL IWKMTQGRVH VTDYTNASRT MLFNIHTLDW
210 220 230 240 250
DDKMLEVLDI PREMLPEVRR SSEVYGQTNI GGKGGTRIPI SGIAGDQQAA
260 270 280 290 300
LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPTGEVN
310 320 330 340 350
YALEGAVFMA GASIQWLRDE MKLINDAYDS EYFATKVQNT NGVYVVPAFT
360 370 380 390 400
GLGAPYWDPY ARGAIFGLTR GVNANHIIRA TLESIAYQTR DVLEAMQADS
410 420 430 440 450
GIRLHALRVD GGAVANNFLM QFQSDILGTR VERPEVREVT ALGAAYLAGL
460 470 480 490 500
AVGFWQNLDE LQEKAVIERE FRPGIETTER NYRYAGWKKA VKRAMAWEEH
DE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18393 Genomic DNA Translation: AAA23913.1 M55990 Genomic DNA Translation: AAA23887.1 L19201 Genomic DNA Translation: AAB03058.1 U00096 Genomic DNA Translation: AAC76908.1 AP009048 Genomic DNA Translation: BAE77384.1 X15054 Genomic DNA Translation: CAA33154.1 U41468 Genomic DNA Translation: AAB60196.1 |
PIRi | A27339, KIECGL |
RefSeqi | NP_418361.1, NC_000913.3 WP_000136788.1, NZ_SSZK01000014.1 |
Genome annotation databases
EnsemblBacteriai | AAC76908; AAC76908; b3926 BAE77384; BAE77384; BAE77384 |
GeneIDi | 58459839 948423 |
KEGGi | ecj:JW3897 eco:b3926 |
PATRICi | fig|1411691.4.peg.2779 |
Similar proteinsi
Cross-referencesi
Web resourcesi
Worthington enzyme manual |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18393 Genomic DNA Translation: AAA23913.1 M55990 Genomic DNA Translation: AAA23887.1 L19201 Genomic DNA Translation: AAB03058.1 U00096 Genomic DNA Translation: AAC76908.1 AP009048 Genomic DNA Translation: BAE77384.1 X15054 Genomic DNA Translation: CAA33154.1 U41468 Genomic DNA Translation: AAB60196.1 |
PIRi | A27339, KIECGL |
RefSeqi | NP_418361.1, NC_000913.3 WP_000136788.1, NZ_SSZK01000014.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BO5 | X-ray | 3.20 | O/Z | 2-502 | [»] | |
1BOT | X-ray | 3.05 | O/Z | 2-502 | [»] | |
1BU6 | X-ray | 2.37 | O/X/Y/Z | 2-502 | [»] | |
1BWF | X-ray | 3.00 | O/Y | 2-502 | [»] | |
1GLA | X-ray | 2.60 | G | 2-502 | [»] | |
1GLB | X-ray | 2.60 | G | 2-502 | [»] | |
1GLC | X-ray | 2.65 | G | 2-502 | [»] | |
1GLD | X-ray | 2.93 | G | 2-502 | [»] | |
1GLE | X-ray | 2.94 | G | 2-502 | [»] | |
1GLF | X-ray | 2.62 | O/X/Y/Z | 2-502 | [»] | |
1GLJ | X-ray | 3.00 | O/Y | 2-502 | [»] | |
1GLL | X-ray | 3.00 | O/Y | 2-502 | [»] | |
3EZW | X-ray | 2.00 | A/B/C/D/E/F/G/H | 2-501 | [»] | |
SMRi | P0A6F3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263162, 380 interactors |
DIPi | DIP-36011N |
IntActi | P0A6F3, 15 interactors |
STRINGi | 511145.b3926 |
Chemistry databases
DrugBanki | DB04551, beta-D-fructofuranose 1,6-bisphosphate DB02937, Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate |
SwissLipidsi | SLP:000001805 |
2D gel databases
SWISS-2DPAGEi | P0A6F3 |
Proteomic databases
jPOSTi | P0A6F3 |
PaxDbi | P0A6F3 |
PRIDEi | P0A6F3 |
Genome annotation databases
EnsemblBacteriai | AAC76908; AAC76908; b3926 BAE77384; BAE77384; BAE77384 |
GeneIDi | 58459839 948423 |
KEGGi | ecj:JW3897 eco:b3926 |
PATRICi | fig|1411691.4.peg.2779 |
Organism-specific databases
EchoBASEi | EB0393 |
Phylogenomic databases
eggNOGi | COG0554, Bacteria |
HOGENOMi | CLU_009281_2_3_6 |
InParanoidi | P0A6F3 |
PhylomeDBi | P0A6F3 |
Enzyme and pathway databases
UniPathwayi | UPA00618;UER00672 |
BioCyci | EcoCyc:GLYCEROL-KIN-MONOMER MetaCyc:GLYCEROL-KIN-MONOMER |
BRENDAi | 2.7.1.30, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0A6F3 |
PROi | PR:P0A6F3 |
Family and domain databases
HAMAPi | MF_00186, Glycerol_kin, 1 hit |
InterProi | View protein in InterPro IPR043129, ATPase_NBD IPR000577, Carb_kinase_FGGY IPR018485, Carb_kinase_FGGY_C IPR018483, Carb_kinase_FGGY_CS IPR018484, Carb_kinase_FGGY_N IPR005999, Glycerol_kin |
Pfami | View protein in Pfam PF02782, FGGY_C, 1 hit PF00370, FGGY_N, 1 hit |
PIRSFi | PIRSF000538, GlpK, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
TIGRFAMsi | TIGR01311, glycerol_kin, 1 hit |
PROSITEi | View protein in PROSITE PS00933, FGGY_KINASES_1, 1 hit PS00445, FGGY_KINASES_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GLPK_ECOLI | |
Accessioni | P0A6F3Primary (citable) accession number: P0A6F3 Secondary accession number(s): P08859, Q2M8M2, Q59381 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 29, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 133 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families