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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)DescriptionActionsGraphical viewLength
Binding sitei14SubstrateUniRule annotation1
Binding sitei18ATP1
Binding sitei136Substrate1
Binding sitei268ATP1
Binding sitei311ATP; via carbonyl oxygenUniRule annotation1
Binding sitei315ATP; via amide nitrogenUniRule annotation1
Binding sitei330ATPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 16ATP3
Nucleotide bindingi412 – 416ATPUniRule annotation5

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)DescriptionActionsGraphical viewLength
Mutagenesisi232H → A: Loss of phosphorylation, no effect on activity. 2 Publications1
Mutagenesisi232H → E: Loss of phosphorylation, 2.5-fold reduced activity. 2 Publications1
Mutagenesisi232H → R: Loss of phosphorylation, 3.4-fold increased activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000594542 – 506Glycerol kinaseAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei232Phosphohistidine; by HPrUniRule annotation1 Publication1

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

1506
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Beta strandi14 – 23Combined sources10
Beta strandi24 – 26Combined sources3
Beta strandi28 – 35Combined sources8
Helixi50 – 68Combined sources19
Helixi72 – 74Combined sources3
Beta strandi75 – 82Combined sources8
Beta strandi87 – 91Combined sources5
Turni92 – 94Combined sources3
Beta strandi97 – 99Combined sources3
Helixi110 – 118Combined sources9
Helixi122 – 129Combined sources8
Beta strandi135 – 137Combined sources3
Helixi138 – 148Combined sources11
Beta strandi149 – 151Combined sources3
Helixi152 – 157Combined sources6
Beta strandi161 – 164Combined sources4
Helixi166 – 174Combined sources9
Turni175 – 177Combined sources3
Beta strandi181 – 183Combined sources3
Helixi184 – 188Combined sources5
Turni189 – 191Combined sources3
Beta strandi192 – 194Combined sources3
Turni195 – 198Combined sources4
Helixi202 – 207Combined sources6
Helixi212 – 214Combined sources3
Beta strandi217 – 219Combined sources3
Beta strandi221 – 227Combined sources7
Helixi230 – 232Combined sources3
Turni233 – 235Combined sources3
Beta strandi239 – 245Combined sources7
Helixi246 – 253Combined sources8
Beta strandi262 – 277Combined sources16
Turni284 – 286Combined sources3
Beta strandi287 – 295Combined sources9
Beta strandi298 – 307Combined sources10
Helixi312 – 319Combined sources8
Beta strandi324 – 327Combined sources4
Helixi329 – 334Combined sources6
Beta strandi335 – 339Combined sources5
Beta strandi344 – 346Combined sources3
Beta strandi349 – 351Combined sources3
Turni354 – 356Combined sources3
Beta strandi364 – 366Combined sources3
Helixi374 – 400Combined sources27
Beta strandi406 – 411Combined sources6
Helixi412 – 415Combined sources4
Helixi417 – 427Combined sources11
Beta strandi429 – 433Combined sources5
Beta strandi435 – 437Combined sources3
Helixi439 – 451Combined sources13
Helixi458 – 462Combined sources5
Beta strandi467 – 471Combined sources5
Helixi477 – 496Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34153.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 85Substrate binding2
Regioni246 – 247Substrate binding2

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
PDB 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.
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: November 2, 2016
This is version 98 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.