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Protein

ADP-dependent glucokinase

Gene

glkA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ADP + D-glucose = AMP + D-glucose 6-phosphate.2 Publications

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

  1. KM=0.64 mM for D-glucose (at 37 degrees Celsius)2 Publications
  2. KM=0.73 mM for D-glucose (at 50 degrees Celsius)2 Publications
  3. KM=0.54 mM for D-glucosamine (at 37 degrees Celsius)2 Publications
  4. KM=8.3 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius)2 Publications
  5. KM=0.07 mM for ADP (at 37 degrees Celsius)2 Publications
  6. KM=0.033 mM for ADP (at 50 degrees Celsius)2 Publications
  7. KM=0.83 mM for CDP (at 37 degrees Celsius)2 Publications
  8. KM=0.041 mM for magnesium ions (at 37 degrees Celsius)2 Publications
  1. Vmax=249 µmol/min/mg enzyme toward glucose (at 50 degrees Celsius)2 Publications
  2. Vmax=194 µmol/min/mg enzyme toward ADP (at 50 degrees Celsius)2 Publications
  3. Vmax=160 µmol/min/mg enzyme toward glucose (at 37 degrees Celsius)2 Publications

pH dependencei

Optimum pH is about 7.5.2 Publications

Temperature dependencei

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.2 Publications

Pathwayi: glycolysis

This protein is involved in the pathway glycolysis, which is part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301Glucose1 Publication
Binding sitei34 – 341Glucose1 Publication
Binding sitei88 – 881Glucose1 Publication
Binding sitei113 – 1131Glucose1 Publication
Binding sitei176 – 1761Glucose1 Publication
Binding sitei197 – 1971Glucose1 Publication
Metal bindingi266 – 2661MagnesiumBy similarity
Binding sitei292 – 2921ADP
Metal bindingi295 – 2951MagnesiumBy similarity
Binding sitei342 – 3421ADP
Binding sitei343 – 3431ADP; via carbonyl oxygen
Binding sitei429 – 4291ADP; via carbonyl oxygen
Active sitei440 – 4401Proton acceptor
Metal bindingi440 – 4401MagnesiumBy similarity
Binding sitei440 – 4401ADP
Binding sitei440 – 4401Glucose1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi342 – 3443ADP
Nucleotide bindingi438 – 4425ADP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11804.
BRENDAi2.7.1.147. 5243.
SABIO-RKQ9V2Z6.
UniPathwayiUPA00109.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-dependent glucokinase (EC:2.7.1.147)
Short name:
ADP-GK
Short name:
ADPGK
Gene namesi
Name:glkA
Ordered Locus Names:PF0312
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 455454ADP-dependent glucokinasePRO_0000184772Add
BLAST

Proteomic databases

PRIDEiQ9V2Z6.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi186497.PF0312.

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Helixi19 – 213Combined sources
Beta strandi25 – 295Combined sources
Beta strandi32 – 387Combined sources
Helixi41 – 5111Combined sources
Helixi53 – 619Combined sources
Beta strandi65 – 673Combined sources
Helixi70 – 8314Combined sources
Beta strandi87 – 915Combined sources
Helixi94 – 10310Combined sources
Beta strandi106 – 1127Combined sources
Helixi113 – 1219Combined sources
Turni122 – 1254Combined sources
Beta strandi129 – 1313Combined sources
Helixi138 – 1414Combined sources
Beta strandi146 – 15510Combined sources
Beta strandi158 – 1625Combined sources
Helixi164 – 1663Combined sources
Beta strandi175 – 1817Combined sources
Beta strandi196 – 2016Combined sources
Helixi206 – 2083Combined sources
Helixi213 – 2153Combined sources
Helixi219 – 2224Combined sources
Helixi223 – 2253Combined sources
Beta strandi227 – 2315Combined sources
Helixi234 – 2363Combined sources
Turni239 – 2413Combined sources
Helixi243 – 25816Combined sources
Beta strandi263 – 2664Combined sources
Helixi273 – 28210Combined sources
Helixi283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Helixi293 – 30210Combined sources
Helixi306 – 3116Combined sources
Beta strandi314 – 3174Combined sources
Helixi320 – 33415Combined sources
Beta strandi337 – 3426Combined sources
Beta strandi344 – 35310Combined sources
Helixi356 – 37520Combined sources
Helixi381 – 3866Combined sources
Helixi387 – 3893Combined sources
Helixi396 – 40712Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi419 – 4257Combined sources
Helixi438 – 45215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UA4X-ray1.90A1-455[»]
ProteinModelPortaliQ9V2Z6.
SMRiQ9V2Z6. Positions 2-455.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9V2Z6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 455454ADPKAdd
BLAST

Sequence similaritiesi

Belongs to the ADP-dependent glucokinase family.Curated

Phylogenomic databases

eggNOGiarCOG03371. Archaea.
COG4809. LUCA.
HOGENOMiHOG000254055.
KOiK00918.
OMAiLAYNTNI.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_00809. ADP_glucokinase.
InterProiIPR031299. ADP_GK.
IPR007666. ADP_PFK/GK.
IPR015990. ADP_PFK/GK_arc.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERiPTHR21208. PTHR21208. 1 hit.
PfamiPF04587. ADP_PFK_GK. 1 hit.
[Graphical view]
PIRSFiPIRSF015883. ADP-Pfk_glckin. 1 hit.
SUPFAMiSSF53613. SSF53613. 1 hit.
PROSITEiPS51255. ADPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9V2Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTWEELYKN AIEKAIKSVP KVKGVLLGYN TNIDAIKYLD SKDLEERIIK
60 70 80 90 100
AGKEEVIKYS EELPDKINTV SQLLGSILWS IRRGKAAELF VESCPVRFYM
110 120 130 140 150
KRWGWNELRM GGQAGIMANL LGGVYGVPVI VHVPQLSRLQ ANLFLDGPIY
160 170 180 190 200
VPTLENGEVK LIHPKEFSGD EENCIHYIYE FPRGFRVFEF EAPRENRFIG
210 220 230 240 250
SADDYNTTLF IREEFRESFS EVIKNVQLAI LSGLQALTKE NYKEPFEIVK
260 270 280 290 300
SNLEVLNERE IPVHLEFAFT PDEKVREEIL NVLGMFYSVG LNEVELASIM
310 320 330 340 350
EILGEKKLAK ELLAHDPVDP IAVTEAMLKL AKKTGVKRIH FHTYGYYLAL
360 370 380 390 400
TEYKGEHVRD ALLFAALAAA AKAMKGNITS LEEIREATSV PVNEKATQVE
410 420 430 440 450
EKLRAEYGIK EGIGEVEGYQ IAFIPTKIVA KPKSTVGIGD TISSSAFIGE

FSFTL
Length:455
Mass (Da):51,266
Last modified:January 23, 2007 - v3
Checksum:i8262ACBF19BED113
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127910 Genomic DNA. Translation: AAD48401.1.
E14588 Unassigned DNA. No translation available.
AE009950 Genomic DNA. Translation: AAL80436.1.
PIRiJC7550.
RefSeqiWP_011011427.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80436; AAL80436; PF0312.
GeneIDi1468147.
KEGGipfu:PF0312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127910 Genomic DNA. Translation: AAD48401.1.
E14588 Unassigned DNA. No translation available.
AE009950 Genomic DNA. Translation: AAL80436.1.
PIRiJC7550.
RefSeqiWP_011011427.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UA4X-ray1.90A1-455[»]
ProteinModelPortaliQ9V2Z6.
SMRiQ9V2Z6. Positions 2-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0312.

Proteomic databases

PRIDEiQ9V2Z6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80436; AAL80436; PF0312.
GeneIDi1468147.
KEGGipfu:PF0312.

Phylogenomic databases

eggNOGiarCOG03371. Archaea.
COG4809. LUCA.
HOGENOMiHOG000254055.
KOiK00918.
OMAiLAYNTNI.

Enzyme and pathway databases

UniPathwayiUPA00109.
BioCyciMetaCyc:MONOMER-11804.
BRENDAi2.7.1.147. 5243.
SABIO-RKQ9V2Z6.

Miscellaneous databases

EvolutionaryTraceiQ9V2Z6.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_00809. ADP_glucokinase.
InterProiIPR031299. ADP_GK.
IPR007666. ADP_PFK/GK.
IPR015990. ADP_PFK/GK_arc.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERiPTHR21208. PTHR21208. 1 hit.
PfamiPF04587. ADP_PFK_GK. 1 hit.
[Graphical view]
PIRSFiPIRSF015883. ADP-Pfk_glckin. 1 hit.
SUPFAMiSSF53613. SSF53613. 1 hit.
PROSITEiPS51255. ADPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH AMP AND GLUCOSE, SUBUNIT.

Entry informationi

Entry nameiGLKA_PYRFU
AccessioniPrimary (citable) accession number: Q9V2Z6
Secondary accession number(s): Q7LX13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.