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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381GlucoseBy similarity
Binding sitei42 – 421GlucoseBy similarity
Binding sitei96 – 961GlucoseBy similarity
Binding sitei121 – 1211GlucoseBy similarity
Binding sitei184 – 1841GlucoseBy similarity
Binding sitei205 – 2051GlucoseBy similarity
Metal bindingi279 – 2791MagnesiumBy similarity
Binding sitei305 – 3051ADP1 Publication
Metal bindingi308 – 3081MagnesiumBy similarity
Binding sitei352 – 3521ADP1 Publication
Binding sitei353 – 3531ADP; via carbonyl oxygen1 Publication
Binding sitei440 – 4401ADP; via carbonyl oxygen1 Publication
Active sitei451 – 4511Proton acceptor
Metal bindingi451 – 4511MagnesiumBy similarity
Binding sitei451 – 4511ADP1 Publication
Binding sitei451 – 4511GlucoseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi352 – 3543ADP1 Publication
Nucleotide bindingi449 – 4535ADP1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi451 – 4511D → A, N or S: Complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467ADP-dependent glucokinasePRO_0000184775Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2622Combined sources
Helixi27 – 293Combined sources
Beta strandi33 – 375Combined sources
Beta strandi40 – 467Combined sources
Helixi49 – 5911Combined sources
Helixi61 – 699Combined sources
Beta strandi73 – 753Combined sources
Helixi78 – 9114Combined sources
Beta strandi95 – 995Combined sources
Helixi102 – 11110Combined sources
Beta strandi114 – 1207Combined sources
Helixi121 – 1299Combined sources
Turni130 – 1323Combined sources
Beta strandi137 – 1393Combined sources
Helixi146 – 1494Combined sources
Beta strandi154 – 16310Combined sources
Beta strandi166 – 1705Combined sources
Helixi172 – 1754Combined sources
Beta strandi183 – 1897Combined sources
Beta strandi204 – 2107Combined sources
Turni212 – 2176Combined sources
Helixi221 – 2255Combined sources
Helixi227 – 2315Combined sources
Beta strandi235 – 2395Combined sources
Helixi242 – 2443Combined sources
Helixi256 – 27116Combined sources
Beta strandi275 – 2795Combined sources
Helixi286 – 2938Combined sources
Helixi294 – 2985Combined sources
Beta strandi300 – 3045Combined sources
Helixi306 – 31611Combined sources
Helixi319 – 3268Combined sources
Helixi330 – 34415Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi354 – 36310Combined sources
Helixi367 – 38519Combined sources
Helixi391 – 3999Combined sources
Helixi404 – 41613Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi424 – 4263Combined sources
Beta strandi431 – 4366Combined sources
Helixi449 – 46517Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7M537.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 467458ADPKAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1GC5X-ray2.30A1-467[»]
4B8RX-ray2.05A1-467[»]
4B8SX-ray2.58A1-467[»]
ProteinModelPortaliQ7M537.
SMRiQ7M537. Positions 1-467.
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: May 11, 2016
This is version 73 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.