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Protein

Glycerol kinase

Gene

glpK

Organism
Enterococcus casseliflavus (Enterococcus flavescens)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.UniRule annotation1 Publication

Catalytic activityi

ATP + glycerol = ADP + sn-glycerol 3-phosphate.UniRule annotation

Enzyme regulationi

Activated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP).UniRule annotation2 Publications

Pathwayi: glycerol degradation via glycerol kinase pathway

This protein is involved in step 1 of the subpathway that synthesizes sn-glycerol 3-phosphate from glycerol.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Glycerol kinase (glpK)
This subpathway is part of the pathway glycerol degradation via glycerol kinase pathway, which is itself part of Polyol metabolism.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141SubstrateUniRule annotation
Binding sitei18 – 181ATP
Binding sitei136 – 1361Substrate
Binding sitei268 – 2681ATP
Binding sitei311 – 3111ATP; via carbonyl oxygenUniRule annotation
Binding sitei315 – 3151ATP; via amide nitrogenUniRule annotation
Binding sitei330 – 3301ATPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 163ATP
Nucleotide bindingi412 – 4165ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00618; UER00672.

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
OrganismiEnterococcus casseliflavus (Enterococcus flavescens)
Taxonomic identifieri37734 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2321H → A: Loss of phosphorylation, no effect on activity. 2 Publications
Mutagenesisi232 – 2321H → E: Loss of phosphorylation, 2.5-fold reduced activity. 2 Publications
Mutagenesisi232 – 2321H → R: Loss of phosphorylation, 3.4-fold increased activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 506505Glycerol kinasePRO_0000059454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei232 – 2321Phosphohistidine; by HPrUniRule annotation1 Publication

Post-translational modificationi

The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation of His-232, which leads to the activation of the enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiO34153.

Interactioni

Subunit structurei

Homotetramer and homodimer (in equilibrium).UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi565655.ECBG_00055.

Structurei

Secondary structure

1
506
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Beta strandi14 – 2310Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 358Combined sources
Helixi50 – 6819Combined sources
Helixi72 – 743Combined sources
Beta strandi75 – 828Combined sources
Beta strandi87 – 915Combined sources
Turni92 – 943Combined sources
Beta strandi97 – 993Combined sources
Helixi110 – 1189Combined sources
Helixi122 – 1298Combined sources
Beta strandi135 – 1373Combined sources
Helixi138 – 14811Combined sources
Beta strandi149 – 1513Combined sources
Helixi152 – 1576Combined sources
Beta strandi161 – 1644Combined sources
Helixi166 – 1749Combined sources
Turni175 – 1773Combined sources
Beta strandi181 – 1833Combined sources
Helixi184 – 1885Combined sources
Turni189 – 1913Combined sources
Beta strandi192 – 1943Combined sources
Turni195 – 1984Combined sources
Helixi202 – 2076Combined sources
Helixi212 – 2143Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 2277Combined sources
Helixi230 – 2323Combined sources
Turni233 – 2353Combined sources
Beta strandi239 – 2457Combined sources
Helixi246 – 2538Combined sources
Beta strandi262 – 27716Combined sources
Turni284 – 2863Combined sources
Beta strandi287 – 2959Combined sources
Beta strandi298 – 30710Combined sources
Helixi312 – 3198Combined sources
Beta strandi324 – 3274Combined sources
Helixi329 – 3346Combined sources
Beta strandi335 – 3395Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi349 – 3513Combined sources
Turni354 – 3563Combined sources
Beta strandi364 – 3663Combined sources
Helixi374 – 40027Combined sources
Beta strandi406 – 4116Combined sources
Helixi412 – 4154Combined sources
Helixi417 – 42711Combined sources
Beta strandi429 – 4335Combined sources
Beta strandi435 – 4373Combined sources
Helixi439 – 45113Combined sources
Helixi458 – 4625Combined sources
Beta strandi467 – 4715Combined sources
Helixi477 – 49620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R59X-ray2.50O/X2-506[»]
1XUPX-ray2.75O/X6-492[»]
3D7EX-ray2.03O/X2-506[»]
3FLCX-ray1.85O/X1-506[»]
3H3NX-ray1.73O/X1-506[»]
3H3OX-ray2.30B/C/O/X1-506[»]
3H45X-ray2.65C/D/O/X1-506[»]
3H46X-ray1.75O/X1-506[»]
ProteinModelPortaliO34153.
SMRiO34153. Positions 6-492.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34153.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 852Substrate binding
Regioni246 – 2472Substrate binding

Sequence similaritiesi

Belongs to the FGGY kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108HMR. Bacteria.
COG0554. LUCA.

Family and domain databases

HAMAPiMF_00186. Glycerol_kin. 1 hit.
InterProiIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000538. GlpK. 1 hit.
TIGRFAMsiTIGR01311. glycerol_kin. 1 hit.
PROSITEiPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O34153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKNYVMAI DQGTTSSRAI IFDRNGKKIG SSQKEFPQYF PKSGWVEHNA
60 70 80 90 100
NEIWNSVQSV IAGAFIESGI RPEAIAGIGI TNQRETTVVW DKTTGQPIAN
110 120 130 140 150
AIVWQSRQSS PIADQLKVDG HTEMIHEKTG LVIDAYFSAT KVRWLLDNIE
160 170 180 190 200
GAQEKADNGE LLFGTIDSWL VWKLTDGQVH VTDYSNASRT MLYNIHKLEW
210 220 230 240 250
DQEILDLLNI PSSMLPEVKS NSEVYGHTRS YHFYGSEVPI AGMAGDQQAA
260 270 280 290 300
LFGQMAFEKG MIKNTYGTGA FIVMNTGEEP QLSDNDLLTT IGYGINGKVY
310 320 330 340 350
YALEGSIFVA GSAIQWLRDG LRMIETSPQS EELAAKAKGD NEVYVVPAFT
360 370 380 390 400
GLGAPYWDSE ARGAVFGLTR GTTKEDFVRA TLQAVAYQSK DVIDTMKKDS
410 420 430 440 450
GIDIPLLKVD GGAAKNDLLM QFQADILDID VQRAANLETT ALGAAYLAGL
460 470 480 490 500
AVGFWKDLDE LKSMAEEGQM FTPEMPAEER DNLYEGWKQA VAATQTFKFK

AKKEGE
Length:506
Mass (Da):55,760
Last modified:January 23, 2007 - v3
Checksum:iF0B557C6F5AF3B3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94355 Genomic DNA. Translation: AAB69985.1.

Genome annotation databases

PATRICi46747690. VBIEntCas170983_2829.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94355 Genomic DNA. Translation: AAB69985.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R59X-ray2.50O/X2-506[»]
1XUPX-ray2.75O/X6-492[»]
3D7EX-ray2.03O/X2-506[»]
3FLCX-ray1.85O/X1-506[»]
3H3NX-ray1.73O/X1-506[»]
3H3OX-ray2.30B/C/O/X1-506[»]
3H45X-ray2.65C/D/O/X1-506[»]
3H46X-ray1.75O/X1-506[»]
ProteinModelPortaliO34153.
SMRiO34153. Positions 6-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi565655.ECBG_00055.

PTM databases

iPTMnetiO34153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi46747690. VBIEntCas170983_2829.

Phylogenomic databases

eggNOGiENOG4108HMR. Bacteria.
COG0554. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00672.

Miscellaneous databases

EvolutionaryTraceiO34153.

Family and domain databases

HAMAPiMF_00186. Glycerol_kin. 1 hit.
InterProiIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000538. GlpK. 1 hit.
TIGRFAMsiTIGR01311. glycerol_kin. 1 hit.
PROSITEiPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLPK_ENTCA
AccessioniPrimary (citable) accession number: O34153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.