ADP-dependent glucokinase - Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

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Q9V2Z6 (GLKA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ADP-dependent glucokinase
Short name=ADP-GK
Short name=ADPGK
EC=2.7.1.147

Gene names

Name:	glkA
Ordered Locus Names:	PF0312

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.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 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: K_M=0.64 mM for D-glucose (at 37 degrees Celsius) Ref.2 Ref.4 K_M=0.73 mM for D-glucose (at 50 degrees Celsius) K_M=0.54 mM for D-glucosamine (at 37 degrees Celsius) K_M=8.3 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius) K_M=0.07 mM for ADP (at 37 degrees Celsius) K_M=0.033 mM for ADP (at 50 degrees Celsius) K_M=0.83 mM for CDP (at 37 degrees Celsius) K_M=0.041 mM for magnesium ions (at 37 degrees Celsius) V_max=249 µmol/min/mg enzyme toward glucose (at 50 degrees Celsius) V_max=194 µmol/min/mg enzyme toward ADP (at 50 degrees Celsius) V_max=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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ADP-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2 Ref.4

Chain

2 – 455

454

ADP-dependent glucokinase HAMAP MF_00809

PRO_0000184772

Regions

Domain

2 – 455

454

ADPK

Nucleotide binding

342 – 344

ADP HAMAP MF_00809

Nucleotide binding

438 – 442

ADP HAMAP MF_00809

Sites

Active site

440

Proton acceptor

Metal binding

266

Magnesium By similarity

Metal binding

295

Magnesium By similarity

Metal binding

440

Magnesium By similarity

Binding site

Glucose

Binding site

Glucose

Binding site

Glucose

Binding site

113

Glucose

Binding site

176

Glucose

Binding site

197

Glucose

Binding site

292

ADP

Binding site

342

ADP

Binding site

343

ADP; via carbonyl oxygen

Binding site

429

ADP; via carbonyl oxygen

Binding site

440

ADP

Binding site

440

Glucose

Secondary structure

455

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9V2Z6 [UniParc].

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

FASTA

455

51,266

        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

References

	« Hide 'large scale' referencesShow '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]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] 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.
+	Additional computationally mapped references.

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.

PIR

JC7550.

RefSeq

NP_578041.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UA4	X-ray	1.90	A	1-455	[»]

ProteinModelPortal

Q9V2Z6.

SMR

Q9V2Z6. Positions 2-455.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000004310; EBPYRP00000004171; EBPYRG00000004310.

GeneID

1468147.

GenomeReviews

Gene locus PF0312 in contig AE009950_GR.

KEGG

pfu:PF0312.

NMPDR

fig|186497.1.peg.318.

Phylogenomic databases

GeneTree

EBGT00050000022952.

HOGENOM

HBG645711.

OMA

IHYIYEF.

ProtClustDB

PRK14038.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11804.

Family and domain databases

HAMAP

MF_00809. ADP_glucokinase.
[Tree]

InterPro

IPR007666. ADP_PFK/GK.
IPR015990. ADP_PFK/GK_arc.
[Graphical view]

K00918.

PANTHER

PTHR21208. ADP_PFK/GK. 1 hit.

Pfam

PF04587. ADP_PFK_GK. 1 hit.
[Graphical view]

PIRSF

PIRSF015883. ADP-Pfk_glckin. 1 hit.

PROSITE

PS51255. ADPK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

Entry information

Entry name

GLKA_PYRFU

Accession

Primary (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:	November 16, 2011
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents