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Reviewed, UniProtKB/Swiss-Prot Q9V2Z6 (GLKA_PYRFU)

Last modified January 19, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    ADP-dependent glucokinase
      Short name=ADPGK
      Short name=ADP-GK
    EC=2.7.1.147
Gene names
Name: glkA
Ordered Locus Names: PF0312
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. Can also use CDP as the phosphoryl group donor and D-glucosamine and D-1,5-anhydroglucitol as the phosphoryl group acceptor. Ref.2 Ref.4

Catalytic activity

ADP + D-glucose = AMP + D-glucose 6-phosphate. Ref.2 Ref.4

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00809

Pathway

Carbohydrate degradation; glycolysis. HAMAP MF_00809

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm Probable HAMAP MF_00809.

Sequence similarities

Belongs to the ADP-dependent glucokinase family.

Contains 1 ADPK (ADP-dependent kinase) domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.64 mM for D-glucose (at 37 degrees Celsius) HAMAP MF_00809

KM=0.73 mM for D-glucose (at 50 degrees Celsius)

KM=0.54 mM for D-glucosamine (at 37 degrees Celsius)

KM=8.3 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius)

KM=0.07 mM for ADP (at 37 degrees Celsius)

KM=0.033 mM for ADP (at 50 degrees Celsius)

KM=0.83 mM for CDP (at 37 degrees Celsius)

KM=0.041 mM for magnesium ions (at 37 degrees Celsius)

Vmax=249 µmol/min/mg enzyme toward glucose (at 50 degrees Celsius)

Vmax=194 µmol/min/mg enzyme toward ADP (at 50 degrees Celsius)

Vmax=160 µmol/min/mg enzyme toward glucose (at 37 degrees Celsius)

pH dependence:

Optimum pH is about 7.5.

Temperature dependence:

Optimum temperature is 105 degrees Celsius. Activity observed at 100 degrees Celsius is about 8 times that at 37 degrees Celsius. Thermostable up to 95 degrees Celsius. Retains full activity after heating at 90 degrees Celsius for 10 minutes and more than 95% of the full activity at 100 degrees Celsius for 10 minutes. Has a half-life of 220 minutes at 100 degrees Celsius. Inactive after heating at 110 degrees Celsius for 30 minutes.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Glycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionADP-specific glucokinase activity

Inferred from electronic annotation. Source: EC

glucokinase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.4
Chain2 – 455454ADP-dependent glucokinase HAMAP MF_00809
PRO_0000184772

Regions

Domain2 – 455454ADPK
Nucleotide binding342 – 3443ADP HAMAP MF_00809
Nucleotide binding438 – 4425ADP HAMAP MF_00809

Sites

Active site4401Proton acceptor HAMAP MF_00809
Metal binding2661Magnesium By similarity
Metal binding2951Magnesium By similarity
Metal binding4401Magnesium By similarity
Binding site301Glucose HAMAP MF_00809
Binding site341Glucose HAMAP MF_00809
Binding site881Glucose HAMAP MF_00809
Binding site1131Glucose HAMAP MF_00809
Binding site1761Glucose HAMAP MF_00809
Binding site1971Glucose HAMAP MF_00809
Binding site2921ADP HAMAP MF_00809
Binding site3421ADP HAMAP MF_00809
Binding site3431ADP; via carbonyl oxygen HAMAP MF_00809
Binding site4291ADP; via carbonyl oxygen HAMAP MF_00809
Binding site4401ADP HAMAP MF_00809
Binding site4401Glucose HAMAP MF_00809

Secondary structure

1 ..................................................................................... 455
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9V2Z6-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8262ACBF19BED113

FASTA45551,266
        10         20         30         40         50         60 
MPTWEELYKN AIEKAIKSVP KVKGVLLGYN TNIDAIKYLD SKDLEERIIK AGKEEVIKYS 

        70         80         90        100        110        120 
EELPDKINTV SQLLGSILWS IRRGKAAELF VESCPVRFYM KRWGWNELRM GGQAGIMANL 

       130        140        150        160        170        180 
LGGVYGVPVI VHVPQLSRLQ ANLFLDGPIY VPTLENGEVK LIHPKEFSGD EENCIHYIYE 

       190        200        210        220        230        240 
FPRGFRVFEF EAPRENRFIG SADDYNTTLF IREEFRESFS EVIKNVQLAI LSGLQALTKE 

       250        260        270        280        290        300 
NYKEPFEIVK SNLEVLNERE IPVHLEFAFT PDEKVREEIL NVLGMFYSVG LNEVELASIM 

       310        320        330        340        350        360 
EILGEKKLAK ELLAHDPVDP IAVTEAMLKL AKKTGVKRIH FHTYGYYLAL TEYKGEHVRD 

       370        380        390        400        410        420 
ALLFAALAAA AKAMKGNITS LEEIREATSV PVNEKATQVE EKLRAEYGIK EGIGEVEGYQ 

       430        440        450 
IAFIPTKIVA KPKSTVGIGD TISSSAFIGE FSFTL

« Hide

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References

« Hide 'large scale' references
[1]"Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus."
Tuininga J.E., Verhees C.H., van der Oost J., Kengen S.W.M., Stams A.J.M., de Vos W.M.
J. Biol. Chem. 274:21023-21028(1999) [PubMed: 10409652] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis."
Koga S., Yoshioka I., Sakuraba H., Takahashi M., Sakasegawa S., Shimizu S., Ohshima T.
J. Biochem. 128:1079-1085(2000) [PubMed: 11098152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[4]"Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus."
Kengen S.W.M., Tuininga J.E., de Bok F.A.M., Stams A.J.M., de Vos W.M.
J. Biol. Chem. 270:30453-30457(1995) [PubMed: 8530474] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[5]"Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase."
Ito S., Fushinobu S., Jeong J.-J., Yoshioka I., Koga S., Shoun H., Wakagi T.
J. Mol. Biol. 331:871-883(2003) [PubMed: 12909015] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH AMP AND GLUCOSE, SUBUNIT.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF127910 Genomic DNA. Translation: AAD48401.1.
E14588 Unassigned DNA. No translation available.
AE009950 Genomic DNA. Translation: AAL80436.1.
PIRJC7550.
RefSeqNP_578041.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UA4X-ray1.90A1-455[»]
ModBaseSearch...

Genome annotation databases

GeneID1468147.
GenomeReviewsGene locus PF0312 in contig AE009950_GR.
KEGGpfu:PF0312.
NMPDRfig|186497.1.peg.318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG645711.
OMARIHFHTY.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11804.
BRENDA2.7.1.147. 321.

Family and domain databases

HAMAPMF_00809. ADP_glucokinase.
[Tree]
InterProIPR007666. ADP_PFK/GK.
IPR015990. ADP_PFK/GK_arc.
[Graphical view]
PANTHERPTHR21208. ADP_PFK/GK. 1 hit.
PfamPF04587. ADP_PFK_GK. 1 hit.
[Graphical view]
PIRSFPIRSF015883. ADP-Pfk_glckin. 1 hit.
PROSITEPS51255. ADPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.

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Entry information

Entry nameGLKA_PYRFU
AccessionPrimary (citable) accession number: Q9V2Z6
Secondary accession number(s): Q7LX13
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 59 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents