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Protein

ADP-dependent glucokinase

Gene

glkA

Organism
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
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.1 Publication

Catalytic activityi

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

Cofactori

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

Kineticsi

  1. KM=0.4 mM for D-glucose (at 37 degrees Celsius)1 Publication
  2. KM=1.9 mM for D-glucosamine (at 37 degrees Celsius)1 Publication
  3. KM=2.0 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius)1 Publication
  4. KM=0.057 mM for ADP (at 37 degrees Celsius)1 Publication
  5. KM=0.56 mM for CDP (at 37 degrees Celsius)1 Publication
  6. KM=0.037 mM for magnesium ions (at 37 degrees Celsius)1 Publication
  1. Vmax=73 µmol/min/mg enzyme with glucose and ADP as substrates (at 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is about 7.5.1 Publication

Temperature dependencei

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.1 Publication

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)DescriptionActionsGraphical viewLength
Binding sitei38GlucoseBy similarity1
Binding sitei42GlucoseBy similarity1
Binding sitei96GlucoseBy similarity1
Binding sitei121GlucoseBy similarity1
Binding sitei184GlucoseBy similarity1
Binding sitei205GlucoseBy similarity1
Metal bindingi279MagnesiumBy similarity1
Binding sitei305ADP1 Publication1
Metal bindingi308MagnesiumBy similarity1
Binding sitei352ADP1 Publication1
Binding sitei353ADP; via carbonyl oxygen1 Publication1
Binding sitei440ADP; via carbonyl oxygen1 Publication1
Active sitei451Proton acceptor1
Metal bindingi451MagnesiumBy similarity1
Binding sitei451ADP1 Publication1
Binding sitei451GlucoseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi352 – 354ADP1 Publication3
Nucleotide bindingi449 – 453ADP1 Publication5

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

BRENDAi2.7.1.147. 6302.
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
ORF Names:OCC_09701
OrganismiThermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Taxonomic identifieri523849 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
Proteomesi
  • UP000015502 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi451D → A, N or S: Complete loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001847751 – 467ADP-dependent glucokinaseAdd BLAST467

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1467
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 26Combined sources22
Helixi27 – 29Combined sources3
Beta strandi33 – 37Combined sources5
Beta strandi40 – 46Combined sources7
Helixi49 – 59Combined sources11
Helixi61 – 69Combined sources9
Beta strandi73 – 75Combined sources3
Helixi78 – 91Combined sources14
Beta strandi95 – 99Combined sources5
Helixi102 – 111Combined sources10
Beta strandi114 – 120Combined sources7
Helixi121 – 129Combined sources9
Turni130 – 132Combined sources3
Beta strandi137 – 139Combined sources3
Helixi146 – 149Combined sources4
Beta strandi154 – 163Combined sources10
Beta strandi166 – 170Combined sources5
Helixi172 – 175Combined sources4
Beta strandi183 – 189Combined sources7
Beta strandi204 – 210Combined sources7
Turni212 – 217Combined sources6
Helixi221 – 225Combined sources5
Helixi227 – 231Combined sources5
Beta strandi235 – 239Combined sources5
Helixi242 – 244Combined sources3
Helixi256 – 271Combined sources16
Beta strandi275 – 279Combined sources5
Helixi286 – 293Combined sources8
Helixi294 – 298Combined sources5
Beta strandi300 – 304Combined sources5
Helixi306 – 316Combined sources11
Helixi319 – 326Combined sources8
Helixi330 – 344Combined sources15
Beta strandi347 – 352Combined sources6
Beta strandi354 – 363Combined sources10
Helixi367 – 385Combined sources19
Helixi391 – 399Combined sources9
Helixi404 – 416Combined sources13
Beta strandi419 – 421Combined sources3
Beta strandi424 – 426Combined sources3
Beta strandi431 – 436Combined sources6
Helixi449 – 465Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GC5X-ray2.30A1-467[»]
4B8RX-ray2.05A1-467[»]
4B8SX-ray2.58A1-467[»]
ProteinModelPortaliQ7M537.
SMRiQ7M537.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7M537.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 467ADPKAdd BLAST458

Sequence similaritiesi

Belongs to the ADP-dependent glucokinase family.Curated

Phylogenomic databases

KOiK00918.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_00809. ADP_glucokinase. 1 hit.
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.

Q7M537-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKESLKDRIR LWKRLYVNAF ENALNAIPNV KGVLLAYNTN IDAIKYLDKD
60 70 80 90 100
DLEKRVTEIG KEKVFEIIEN PPEKISSIEE LLGGILRSIK LGKAMEWFVE
110 120 130 140 150
SEEVRRYLRE WGWDELRIGG QAGIMANLLG GVYRIPTIVH VPQNPKLQAE
160 170 180 190 200
LFVDGPIYVP VFEGNKLKLV HPKDAIAEEE ELIHYIYEFP RGFQVFDVQA
210 220 230 240 250
PRENRFIANA DDYNARVYMR REFREGFEEI TRNVELAIIS GLQVLKEYYP
260 270 280 290 300
DGTTYRDVLD RVESHLNILN RYNVKSHFEF AYTANRRVRE ALVELLPKFT
310 320 330 340 350
SVGLNEVELA SIMEIIGDEE LAKEVLEGHI FSVIDAMNVL MDETGIERIH
360 370 380 390 400
FHTYGYYLAL TQYRGEEVRD ALLFASLAAA AKAMKGNLER IEQIRDALSV
410 420 430 440 450
PTNERAIVLE EELEKEFTEF ENGLIDMVDR QLAFVPTKIV ASPKSTVGIG
460
DTISSSAFVS EFGMRKR
Length:467
Mass (Da):53,621
Last modified:December 15, 2003 - v1
Checksum:i8E8245E8C07212F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
E14589 Unassigned DNA. No translation available.
CP006670 Genomic DNA. Translation: EHR77687.1.
PIRiJC7551.
RefSeqiWP_004069859.1. NC_022084.1.

Genome annotation databases

EnsemblBacteriaiEHR77687; EHR77687; OCC_09701.
GeneIDi16549063.
KEGGitlt:OCC_09701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
E14589 Unassigned DNA. No translation available.
CP006670 Genomic DNA. Translation: EHR77687.1.
PIRiJC7551.
RefSeqiWP_004069859.1. NC_022084.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GC5X-ray2.30A1-467[»]
4B8RX-ray2.05A1-467[»]
4B8SX-ray2.58A1-467[»]
ProteinModelPortaliQ7M537.
SMRiQ7M537.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEHR77687; EHR77687; OCC_09701.
GeneIDi16549063.
KEGGitlt:OCC_09701.

Phylogenomic databases

KOiK00918.

Enzyme and pathway databases

UniPathwayiUPA00109.
BRENDAi2.7.1.147. 6302.

Miscellaneous databases

EvolutionaryTraceiQ7M537.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_00809. ADP_glucokinase. 1 hit.
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...

Entry informationi

Entry nameiGLKA_THELN
AccessioniPrimary (citable) accession number: Q7M537
Secondary accession number(s): H3ZQW1, Q7SIF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.