Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Galactokinase

Gene

galK

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 transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). Is very specific for its substrate, since it is not able to use D-glucose, D-fructose, D-mannose, 2-deoxy-D-glucose, and D-glucosamine as substrates.UniRule annotation1 Publication

Catalytic activityi

ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate.UniRule annotation1 Publication

Kineticsi

  1. KM=0.21 mM for D-galactose (at 50 degrees Celsius)1 Publication
  2. KM=0.006 mM for ATP (at 50 degrees Celsius)1 Publication
  3. KM=0.27 mM for D-galactose (at 90 degrees Celsius)1 Publication
  4. KM=0.008 mM for ATP (at 90 degrees Celsius)1 Publication
  1. Vmax=3.66 µmol/min/mg enzyme (at 50 degrees Celsius)1 Publication
  2. Vmax=43.2 µmol/min/mg enzyme (at 90 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is 90 degrees Celsius.1 Publication

Pathwayi: galactose metabolism

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei11 – 111Transition state stabilizerCurated
Binding sitei49 – 491ATP
Metal bindingi107 – 1071Magnesium
Metal bindingi139 – 1391Magnesium
Active sitei151 – 1511Proton acceptor1 Publication
Binding sitei200 – 2001SubstrateUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi101 – 1077ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Galactose metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00214.

Names & Taxonomyi

Protein namesi
Recommended name:
GalactokinaseUniRule annotation (EC:2.7.1.6UniRule annotation)
Alternative name(s):
Galactose kinaseUniRule annotation
Gene namesi
Name:galKUniRule annotation
Ordered Locus Names:PF0445
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352GalactokinasePRO_0000184641Add
BLAST

Proteomic databases

PRIDEiQ9HHB6.

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRINGi186497.PF0445.

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1510Combined sources
Helixi20 – 223Combined sources
Beta strandi28 – 3710Combined sources
Turni50 – 534Combined sources
Helixi70 – 8213Combined sources
Beta strandi94 – 985Combined sources
Beta strandi102 – 1043Combined sources
Helixi106 – 12116Combined sources
Helixi128 – 14114Combined sources
Helixi150 – 1578Combined sources
Beta strandi162 – 1676Combined sources
Turni168 – 1714Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi182 – 19211Combined sources
Helixi196 – 21419Combined sources
Helixi219 – 2213Combined sources
Helixi224 – 2285Combined sources
Helixi232 – 25625Combined sources
Helixi260 – 27617Combined sources
Helixi283 – 29412Combined sources
Beta strandi298 – 3025Combined sources
Beta strandi307 – 31610Combined sources
Helixi317 – 3193Combined sources
Helixi320 – 33415Combined sources
Beta strandi340 – 3445Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4EX-ray2.90A/B/C/D/E/F/G/H/I1-352[»]
ProteinModelPortaliQ9HHB6.
SMRiQ9HHB6. Positions 2-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HHB6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 204Substrate binding

Sequence similaritiesi

Belongs to the GHMP kinase family. GalK subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01029. Archaea.
COG0153. LUCA.
HOGENOMiHOG000241101.
KOiK00849.
OMAiDMLFHDT.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00246. Galactokinase.
InterProiIPR000705. Galactokinase.
IPR022963. Galactokinase_bac.
IPR019741. Galactokinase_CS.
IPR019539. GalKase_gal-bd.
IPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10457. PTHR10457. 1 hit.
PTHR10457:SF6. PTHR10457:SF6. 1 hit.
PfamiPF10509. GalKase_gal_bdg. 1 hit.
PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000530. Galactokinase. 1 hit.
PRINTSiPR00473. GALCTOKINASE.
PR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00131. gal_kin. 1 hit.
PROSITEiPS00106. GALACTOKINASE. 1 hit.
PS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HHB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKITVKSPG RVNLIGEHTD YTYGYVMPMA IDLYTIITAE KYDKVQLYSE
60 70 80 90 100
HFNEEKTFTL DNLTKEGSWI DYVKGVLWVL IQEGYKIGGL KGKITGDLPL
110 120 130 140 150
GAGLSSSASF EVGILEVLNQ LYNLNIDPLK KALLAKKAEN EFVGVPCGIL
160 170 180 190 200
DQFAVVFGKK DNVIFLDTQT LQYEYIPFPK DVSVLVFYTG VKRELASSEY
210 220 230 240 250
AERKRIAEES LRILGKESSK EVTEKDLGKL PPLHRKFFSY IVRENARVLE
260 270 280 290 300
VRDALKEGDI EKVGKILTTA HWDLAENYRV SCEELDFFVK KAMELGAYGA
310 320 330 340 350
RLTGAGFGGS AIALVDKDKA KTIGDAILRE YLAKFSWKAK YFVVKPSDGV

GV
Length:352
Mass (Da):39,375
Last modified:March 1, 2001 - v1
Checksum:i44413EAEDEE518B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195244 Genomic DNA. Translation: AAG28454.1.
AE009950 Genomic DNA. Translation: AAL80569.1.
RefSeqiWP_011011563.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80569; AAL80569; PF0445.
GeneIDi1468286.
KEGGipfu:PF0445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195244 Genomic DNA. Translation: AAG28454.1.
AE009950 Genomic DNA. Translation: AAL80569.1.
RefSeqiWP_011011563.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4EX-ray2.90A/B/C/D/E/F/G/H/I1-352[»]
ProteinModelPortaliQ9HHB6.
SMRiQ9HHB6. Positions 2-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0445.

Proteomic databases

PRIDEiQ9HHB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80569; AAL80569; PF0445.
GeneIDi1468286.
KEGGipfu:PF0445.

Phylogenomic databases

eggNOGiarCOG01029. Archaea.
COG0153. LUCA.
HOGENOMiHOG000241101.
KOiK00849.
OMAiDMLFHDT.

Enzyme and pathway databases

UniPathwayiUPA00214.

Miscellaneous databases

EvolutionaryTraceiQ9HHB6.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPiMF_00246. Galactokinase.
InterProiIPR000705. Galactokinase.
IPR022963. Galactokinase_bac.
IPR019741. Galactokinase_CS.
IPR019539. GalKase_gal-bd.
IPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10457. PTHR10457. 1 hit.
PTHR10457:SF6. PTHR10457:SF6. 1 hit.
PfamiPF10509. GalKase_gal_bdg. 1 hit.
PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000530. Galactokinase. 1 hit.
PRINTSiPR00473. GALCTOKINASE.
PR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00131. gal_kin. 1 hit.
PROSITEiPS00106. GALACTOKINASE. 1 hit.
PS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Verhees C.H.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "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.
  3. "Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus."
    Verhees C.H., Koot D.G., Ettema T.J., Dijkema C., de Vos W.M., van der Oost J.
    Biochem. J. 366:121-127(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  4. "Cloning, purification, crystallization and preliminary crystallographic analysis of galactokinase from Pyrococcus furiosus."
    de Geus D., Hartley A.P., Sedelnikova S.E., Glynn S.E., Baker P.J., Verhees C.H., van der Oost J., Rice D.W.
    Acta Crystallogr. D 59:1819-1821(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, SUBUNIT.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  5. "Substrate specificity and mechanism from the structure of Pyrococcus furiosus galactokinase."
    Hartley A., Glynn S.E., Barynin V., Baker P.J., Sedelnikova S.E., Verhees C.H., de Geus D., van der Oost J., Timson D.J., Reece R.J., Rice D.W.
    J. Mol. Biol. 337:387-398(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH MG-ADP AND SUBSTRATE, ACTIVE SITE, REACTION MECHANISM, SUBUNIT.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Entry informationi

Entry nameiGAL1_PYRFU
AccessioniPrimary (citable) accession number: Q9HHB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2001
Last modified: February 17, 2016
This is version 102 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.