Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7M537 (GLKA_THELI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-dependent glucokinase
Short name=ADP-GK
Short name=ADPGK
EC=2.7.1.147
Gene names
Name:glkA
OrganismThermococcus litoralis
Taxonomic identifier2265 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.1

Catalytic activity

ADP + D-glucose = AMP + D-glucose 6-phosphate. Ref.1

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00809

Pathway

Carbohydrate degradation; glycolysis. HAMAP MF_00809

Subunit structure

Monomer. Ref.3

Subcellular location

Cytoplasm By similarity HAMAP MF_00809.

Sequence similarities

Belongs to the ADP-dependent glucokinase family.

Contains 1 ADPK (ADP-dependent kinase) domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.4 mM for D-glucose (at 37 degrees Celsius) Ref.1

KM=1.9 mM for D-glucosamine (at 37 degrees Celsius)

KM=2.0 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius)

KM=0.057 mM for ADP (at 37 degrees Celsius)

KM=0.56 mM for CDP (at 37 degrees Celsius)

KM=0.037 mM for magnesium ions (at 37 degrees Celsius)

Vmax=73 µmol/min/mg enzyme with glucose and ADP as substrates (at 37 degrees Celsius)

pH dependence:

Optimum pH is about 7.5.

Temperature dependence:

Optimum temperature may be above 100 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 min and more than 95% of the full activity at 100 degrees Celsius for 10 min.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionADP-specific glucokinase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467ADP-dependent glucokinase HAMAP MF_00809
PRO_0000184775

Regions

Domain10 – 467458ADPK
Nucleotide binding352 – 3543ADP HAMAP MF_00809
Nucleotide binding449 – 4535ADP HAMAP MF_00809

Sites

Active site4511Proton acceptor
Metal binding2791Magnesium By similarity
Metal binding3081Magnesium By similarity
Metal binding4511Magnesium By similarity
Binding site381Glucose By similarity
Binding site421Glucose By similarity
Binding site961Glucose By similarity
Binding site1211Glucose By similarity
Binding site1841Glucose By similarity
Binding site2051Glucose By similarity
Binding site3051ADP
Binding site3521ADP
Binding site3531ADP; via carbonyl oxygen
Binding site4401ADP; via carbonyl oxygen
Binding site4511ADP
Binding site4511Glucose By similarity

Experimental info

Mutagenesis4511D → A, N or S: Complete loss of activity. Ref.2

Secondary structure

1 ............................................................................... 467
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7M537 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 8E8245E8C07212F1

FASTA46753,621
        10         20         30         40         50         60 
MKESLKDRIR LWKRLYVNAF ENALNAIPNV KGVLLAYNTN IDAIKYLDKD DLEKRVTEIG 

        70         80         90        100        110        120 
KEKVFEIIEN PPEKISSIEE LLGGILRSIK LGKAMEWFVE SEEVRRYLRE WGWDELRIGG 

       130        140        150        160        170        180 
QAGIMANLLG GVYRIPTIVH VPQNPKLQAE LFVDGPIYVP VFEGNKLKLV HPKDAIAEEE 

       190        200        210        220        230        240 
ELIHYIYEFP RGFQVFDVQA PRENRFIANA DDYNARVYMR REFREGFEEI TRNVELAIIS 

       250        260        270        280        290        300 
GLQVLKEYYP DGTTYRDVLD RVESHLNILN RYNVKSHFEF AYTANRRVRE ALVELLPKFT 

       310        320        330        340        350        360 
SVGLNEVELA SIMEIIGDEE LAKEVLEGHI FSVIDAMNVL MDETGIERIH FHTYGYYLAL 

       370        380        390        400        410        420 
TQYRGEEVRD ALLFASLAAA AKAMKGNLER IEQIRDALSV PTNERAIVLE EELEKEFTEF 

       430        440        450        460 
ENGLIDMVDR QLAFVPTKIV ASPKSTVGIG DTISSSAFVS EFGMRKR

« Hide

References

[1]"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], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DSM 5473.
[2]"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: MUTAGENESIS OF ASP-451.
[3]"Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon."
Ito S., Fushinobu S., Yoshioka I., Koga S., Matsuzawa H., Wakagi T.
Structure 9:205-214(2001) [PubMed: 11286887] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		E14589 Unassigned DNA. No translation available.
PIRJC7551.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GC5X-ray2.30A1-467[»]
ProteinModelPortalQ7M537.
SMRQ7M537. Positions 1-467.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameGLKA_THELI
AccessionPrimary (citable) accession number: Q7M537
Secondary accession number(s): Q7SIF2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 15, 2003
Last modified: May 31, 2011
This is version 49 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents