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O34153 (GLPK_ENTCA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol kinase
EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name=GK
Gene names
Name:glpK
OrganismEnterococcus casseliflavus (Enterococcus flavescens)
Taxonomic identifier37734 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism. HAMAP MF_00186

Catalytic activity

ATP + glycerol = ADP + sn-glycerol 3-phosphate. HAMAP MF_00186

Enzyme regulation

Activated by phosphorylation; inhibited by fructose 1,6-biphosphate (FBP). HAMAP MF_00186

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. HAMAP MF_00186

Subunit structure

Homotetramer. Ref.2

Post-translational modification

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. HAMAP MF_00186

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processglycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycerol kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 506505Glycerol kinase HAMAP MF_00186
PRO_0000059454

Regions

Nucleotide binding412 – 4165ATP By similarity

Sites

Binding site141Substrate By similarity
Binding site181ATP By similarity
Binding site841Substrate
Binding site1361Substrate By similarity
Binding site2461Substrate By similarity
Binding site2681ATP By similarity
Binding site3111ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue2321Phosphohistidine; by HPr Ref.1

Experimental info

Mutagenesis2321H → A: Loss of phosphorylation, no effect on activity. Ref.1
Mutagenesis2321H → E: Loss of phosphorylation, 2.5-fold reduced activity. Ref.1
Mutagenesis2321H → R: Loss of phosphorylation, 3.4-fold increased activity. Ref.1

Secondary structure

1 .................................................................................................... 506
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34153 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F0B557C6F5AF3B3E

FASTA50655,760
        10         20         30         40         50         60 
MAEKNYVMAI DQGTTSSRAI IFDRNGKKIG SSQKEFPQYF PKSGWVEHNA NEIWNSVQSV 

        70         80         90        100        110        120 
IAGAFIESGI RPEAIAGIGI TNQRETTVVW DKTTGQPIAN AIVWQSRQSS PIADQLKVDG 

       130        140        150        160        170        180 
HTEMIHEKTG LVIDAYFSAT KVRWLLDNIE GAQEKADNGE LLFGTIDSWL VWKLTDGQVH 

       190        200        210        220        230        240 
VTDYSNASRT MLYNIHKLEW DQEILDLLNI PSSMLPEVKS NSEVYGHTRS YHFYGSEVPI 

       250        260        270        280        290        300 
AGMAGDQQAA LFGQMAFEKG MIKNTYGTGA FIVMNTGEEP QLSDNDLLTT IGYGINGKVY 

       310        320        330        340        350        360 
YALEGSIFVA GSAIQWLRDG LRMIETSPQS EELAAKAKGD NEVYVVPAFT GLGAPYWDSE 

       370        380        390        400        410        420 
ARGAVFGLTR GTTKEDFVRA TLQAVAYQSK DVIDTMKKDS GIDIPLLKVD GGAAKNDLLM 

       430        440        450        460        470        480 
QFQADILDID VQRAANLETT ALGAAYLAGL AVGFWKDLDE LKSMAEEGQM FTPEMPAEER 

       490        500 
DNLYEGWKQA VAATQTFKFK AKKEGE

« Hide

References

[1]"Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue."
Charrier V., Buckley E., Parsonage D., Galinier A., Darbon E., Jaquinod M., Forest E., Deutscher J., Claiborne A.
J. Biol. Chem. 272:14166-14174(1997) [PubMed: 9162046] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHOSPHORYLATION AT HIS-232, MUTAGENESIS OF HIS-232.
Strain: ATCC 12755 / DSM 4841 / NCFB 2725.
[2]"Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation."
Yeh J.I., Charrier V., Paulo J., Hou L., Darbon E., Claiborne A., Hol W.G.J., Deutscher J.
Biochemistry 43:362-373(2004) [PubMed: 14717590] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLYCEROL, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U94355 Genomic DNA. Translation: AAB69985.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO34153.
SMRO34153. Positions 6-492.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC46747690. VBIEntCas170983_2829.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PANTHERPTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. Glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPK_ENTCA
AccessionPrimary (citable) accession number: O34153
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

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

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