Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycerol kinase

Gene

glpK

Organism
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

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 annotation

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 sitei12 – 121SubstrateUniRule annotation
Binding sitei16 – 161ATPUniRule annotation
Binding sitei134 – 1341SubstrateUniRule annotation
Binding sitei266 – 2661ATPUniRule annotation
Binding sitei309 – 3091ATP; via carbonyl oxygenUniRule annotation
Binding sitei313 – 3131ATP; via amide nitrogenUniRule annotation
Binding sitei328 – 3281ATPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 143ATPUniRule annotation
Nucleotide bindingi410 – 4145ATPUniRule 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

BioCyciBCYT315749:GH2A-918-MONOMER.
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
Ordered Locus Names:Bcer98_0807
OrganismiBacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Taxonomic identifieri315749 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002300 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Glycerol kinasePRO_1000077409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301Phosphohistidine; by HPrUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homotetramer and homodimer (in equilibrium).UniRule annotation

Protein-protein interaction databases

STRINGi315749.Bcer98_0807.

Structurei

3D structure databases

ProteinModelPortaliA7GLY7.
SMRiA7GLY7. Positions 4-489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 832Substrate bindingUniRule annotation
Regioni244 – 2452Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the FGGY kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108HMR. Bacteria.
COG0554. LUCA.
HOGENOMiHOG000222134.
KOiK00864.
OMAiGWVEHEP.
OrthoDBiEOG6RZB46.

Family and domain databases

HAMAPiMF_00186. Glycerol_kin.
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.

A7GLY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METYILSLDQ GTTSSRAILF NKKGEIVHSA QKEFTQYFPK PGWVEHNAQE
60 70 80 90 100
IWGSILAVIA TCLSEADVKP EQIAGIGITN QRETAVVWEK ATGKPVYNAI
110 120 130 140 150
VWQSRQTAEI CEELKEKGYG DMVREKTGLL IDAYFSGTKV KWILDNVEGA
160 170 180 190 200
REKAERGELL FGTIDTWLVW KLSGGKAHVT DYSNASRTLM FNIHDLKWDD
210 220 230 240 250
ELLEILTVPK SMLPEVRPSS EVYGHTVDYH FFSQNVPIAG VAGDQQAALF
260 270 280 290 300
GQACFSEGMA KNTYGTGCFM LMNTGETAVN SNHGLLTTIA WGLNGKVNYA
310 320 330 340 350
LEGSIFVAGS AIQWLRDGMR MVNDASESEE YASRVESTDG VYVVPAFVGL
360 370 380 390 400
GTPYWDSEVR GAVFGVTRGT TKEHFIRATL ESLGYQTRDV LCAMEADSGI
410 420 430 440 450
ELKTLRVDGG AVKNNFLMQF QSDMLQVPVE RPMISETTAL GAAYLAGLAV
460 470 480 490
GYWESQEEIK AQWDMDRSFT PEMEKERSEE LYSGWKKAIE ATKAFK
Length:496
Mass (Da):55,071
Last modified:September 11, 2007 - v1
Checksum:iA7EC4F5C7FC6C9FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS21145.1.
RefSeqiWP_011983899.1. NC_009674.1.

Genome annotation databases

EnsemblBacteriaiABS21145; ABS21145; Bcer98_0807.
KEGGibcy:Bcer98_0807.
PATRICi18930019. VBIBacCyt128034_0855.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS21145.1.
RefSeqiWP_011983899.1. NC_009674.1.

3D structure databases

ProteinModelPortaliA7GLY7.
SMRiA7GLY7. Positions 4-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315749.Bcer98_0807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS21145; ABS21145; Bcer98_0807.
KEGGibcy:Bcer98_0807.
PATRICi18930019. VBIBacCyt128034_0855.

Phylogenomic databases

eggNOGiENOG4108HMR. Bacteria.
COG0554. LUCA.
HOGENOMiHOG000222134.
KOiK00864.
OMAiGWVEHEP.
OrthoDBiEOG6RZB46.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00672.
BioCyciBCYT315749:GH2A-918-MONOMER.

Family and domain databases

HAMAPiMF_00186. Glycerol_kin.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 22905 / CIP 110041 / 391-98 / NVH 391-98.

Entry informationi

Entry nameiGLPK_BACCN
AccessioniPrimary (citable) accession number: A7GLY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: May 11, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.