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Protein

Nucleoside kinase

Gene

MJ0406

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of a wide range of nucleosides to yield nucleoside monophosphates. Shows the highest activity for inosine, guanosine and cytidine, but very poor kinase activity with adenosine, thymidine, uridine and xanthosine. ATP is the best phosphate donor, but can also use ITP and GTP. Shows extremely low activity with fructose-6-phosphate.1 Publication

Catalytic activityi

ATP + cytidine = ADP + CMP.1 Publication
ATP + guanosine = ADP + GMP.1 Publication
ATP + inosine = ADP + IMP.1 Publication

Cofactori

Mg2+1 Publication1 Publication, Mn2+1 PublicationNote: Can use Mg2+ and Mn2+ with equal efficiency in vitro, and to a lesser extent, Ni2+.1 Publication

Kineticsi

  1. KM=0.25 mM for ATP (at 70 degrees Celsius)1 Publication
  2. KM=17 µM for cytidine (at 50 degrees Celsius)1 Publication
  3. KM=20 µM for cytidine (at 70 degrees Celsius)1 Publication
  4. KM=20 µM for inosine (at 70 degrees Celsius)1 Publication
  5. KM=21 µM for inosine (at 50 degrees Celsius)1 Publication
  6. KM=62 µM for guanosine (at 70 degrees Celsius)1 Publication
  7. KM=78 µM for guanosine (at 50 degrees Celsius)1 Publication
  8. KM=160 µM for adenosine (at 70 degrees Celsius)1 Publication
  9. KM=180 µM for uridine (at 50 degrees Celsius)1 Publication
  10. KM=200 µM for uridine (at 70 degrees Celsius)1 Publication
  11. KM=230 µM for adenosine (at 50 degrees Celsius)1 Publication
  12. KM=300 µM for ribose (at 70 degrees Celsius)1 Publication
  13. KM=710 µM for xanthosine (at 50 degrees Celsius)1 Publication
  14. KM=900 µM for thymidine (at 50 degrees Celsius)1 Publication
  15. KM=1000 µM for thymidine (at 70 degrees Celsius)1 Publication
  16. KM=1800 µM for fructose (at 70 degrees Celsius)1 Publication
  17. KM=2200 µM for 2-deoxy-adenosine (at 70 degrees Celsius)1 Publication
  18. KM=2500 µM for 2-deoxy-adenosine (at 50 degrees Celsius)1 Publication
  1. Vmax=120 µmol/min/mg enzyme with guanosine as substrate (at 70 degrees Celsius)1 Publication
  2. Vmax=75 µmol/min/mg enzyme with inosine as substrate (at 70 degrees Celsius)1 Publication
  3. Vmax=70 µmol/min/mg enzyme with cytidine as substrate (at 70 degrees Celsius)1 Publication
  4. Vmax=29.3 µmol/min/mg enzyme with guanosine as substrate (at 50 degrees Celsius)1 Publication
  5. Vmax=18.8 µmol/min/mg enzyme with inosine as substrate (at 50 degrees Celsius)1 Publication
  6. Vmax=9 µmol/min/mg enzyme with cytidine as substrate (at 50 degrees Celsius)1 Publication
  7. Vmax=4 µmol/min/mg enzyme with adenosine as substrate (at 70 degrees Celsius)1 Publication
  8. Vmax=1 µmol/min/mg enzyme with adenosine as substrate (at 50 degrees Celsius)1 Publication
  9. Vmax=0.25 µmol/min/mg enzyme with uridine as substrate (at 70 degrees Celsius)1 Publication
  10. Vmax=0.6 µmol/min/mg enzyme with xanthosine as substrate (at 50 degrees Celsius)1 Publication
  11. Vmax=0.6 µmol/min/mg enzyme with ribose as substrate (at 70 degrees Celsius)1 Publication
  12. Vmax=0.2 µmol/min/mg enzyme with 2-deoxy-adenosine as substrate (at 70 degrees Celsius)1 Publication
  13. Vmax=0.08 µmol/min/mg enzyme with thymidine as substrate (at 70 degrees Celsius)1 Publication
  14. Vmax=0.05 µmol/min/mg enzyme with 2-deoxy-adenosine as substrate (at 50 degrees Celsius)1 Publication
  15. Vmax=0.04 µmol/min/mg enzyme with uridine as substrate (at 50 degrees Celsius)1 Publication
  16. Vmax=0.03 µmol/min/mg enzyme with fructose as substrate (at 70 degrees Celsius)1 Publication
  17. Vmax=0.01 µmol/min/mg enzyme with thymidine as substrate (at 50 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.0. 50% of activity is found at pH 6.1 and 8.2.1 Publication

Temperature dependencei

Optimum temperature is 85 degrees Celsius. Thermostable.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei17SubstrateCombined sources1 Publication1
Binding sitei33SubstrateCombined sources1 Publication1
Binding sitei43Substrate; via amide nitrogenCombined sources1 Publication1
Binding sitei47SubstrateCombined sources1 Publication1
Binding sitei109ATPCombined sources1 Publication1
Binding sitei163SubstrateCombined sources1 Publication1
Binding sitei186ATPCombined sources1 Publication1
Active sitei247Proton acceptor1 Publication1
Binding sitei247SubstrateCombined sources1 Publication1
Sitei250Transition state stabilizer1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 219ATPCombined sources1 Publication6

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • carbohydrate kinase activity Source: GO_Central
  • inosine kinase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • nucleoside kinase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
LigandATP-binding, Magnesium, Manganese, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.B20. 3260.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside kinase1 Publication
Short name:
NK1 Publication
Alternative name(s):
ATP-dependent nucleoside monophosphokinaseCurated
Cytidine kinase1 Publication (EC:2.7.1.2131 Publication)
Guanosine kinase1 Publication (EC:2.7.1.-1 Publication)
Inosine kinase1 Publication (EC:2.7.1.731 Publication)
Gene namesi
Ordered Locus Names:MJ0406
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000801522 – 302Nucleoside kinaseAdd BLAST301

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi243232.MJ_0406.

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi15 – 21Combined sources7
Beta strandi28 – 35Combined sources8
Beta strandi37 – 42Combined sources6
Helixi44 – 54Combined sources11
Beta strandi58 – 62Combined sources5
Turni67 – 71Combined sources5
Helixi73 – 80Combined sources8
Beta strandi92 – 94Combined sources3
Beta strandi98 – 103Combined sources6
Beta strandi109 – 114Combined sources6
Helixi116 – 123Combined sources8
Beta strandi131 – 136Combined sources6
Helixi141 – 151Combined sources11
Beta strandi155 – 159Combined sources5
Helixi162 – 167Combined sources6
Helixi170 – 178Combined sources9
Beta strandi181 – 186Combined sources6
Helixi187 – 197Combined sources11
Helixi201 – 205Combined sources5
Beta strandi209 – 214Combined sources6
Helixi216 – 218Combined sources3
Beta strandi220 – 223Combined sources4
Beta strandi228 – 231Combined sources4
Helixi245 – 258Combined sources14
Helixi263 – 277Combined sources15
Beta strandi280 – 284Combined sources5
Helixi290 – 299Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C49X-ray1.92A/B1-302[»]
2C4EX-ray1.70A1-302[»]
ProteinModelPortaliQ57849.
SMRiQ57849.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57849.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 113Substrate bindingCombined sources1 Publication3

Sequence similaritiesi

Belongs to the carbohydrate kinase PfkB family.Curated

Phylogenomic databases

eggNOGiarCOG00014. Archaea.
COG0524. LUCA.
InParanoidiQ57849.
OMAiGCQTNLP.
OrthoDBiPOG093Z05O0.
PhylomeDBiQ57849.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiView protein in InterPro
IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
IPR002139. Ribo/fructo_kinase.
IPR029056. Ribokinase-like.
PfamiView protein in Pfam
PF00294. PfkB. 1 hit.
PRINTSiPR00990. RIBOKINASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
PROSITEiView protein in PROSITE
PS00583. PFKB_KINASES_1. 1 hit.
PS00584. PFKB_KINASES_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q57849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGKMEKITC VGHTALDYIF NVEKFPEPNT SIQIPSARKY YGGAAANTAV
60 70 80 90 100
GIKKLGVNSE LLSCVGYDFK NSGYERYLKN LDINISKLYY SEEEETPKAW
110 120 130 140 150
IFTDKDNNQI TFFLWGAAKH YKELNPPNFN TEIVHIATGD PEFNLKCAKK
160 170 180 190 200
AYGNNLVSFD PGQDLPQYSK EMLLEIIEHT NFLFMNKHEF ERASNLLNFE
210 220 230 240 250
IDDYLERVDA LIVTKGSKGS VIYTKDKKIE IPCIKAGKVI DPTGAGDSYR
260 270 280 290 300
AGFLSAYVKG YDLEKCGLIG AATASFVVEA KGCQTNLPTW DKVVERLEKH

RI
Length:302
Mass (Da):33,920
Last modified:November 1, 1996 - v1
Checksum:i6A535606CC7D3260
GO

Mass spectrometryi

Molecular mass is 33937 Da from positions 2 - 302. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98396.1.
PIRiF64350.

Genome annotation databases

EnsemblBacteriaiAAB98396; AAB98396; MJ_0406.
KEGGimja:MJ_0406.

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.

Entry informationi

Entry nameiNK_METJA
AccessioniPrimary (citable) accession number: Q57849
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 5, 2017
This is version 102 of the entry and version 1 of the sequence. See 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families