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Information on EC 2.7.1.161 - CTP-dependent riboflavin kinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q60365

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EC Tree
IUBMB Comments
This archaeal enzyme differs from EC 2.7.1.26, riboflavin kinase, in using CTP as the donor nucleotide. UTP, but not ATP or GTP, can also act as a phosphate donor but it is at least an order of magnitude less efficient than CTP.
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Methanocaldococcus jannaschii
UNIPROT: Q60365
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
hide
CTP
+
riboflavin
=
CDP
+
FMN
+
=
+
Synonyms
mj0056, ctp-dependent riboflavin kinase, methanocaldococcus jannaschii mj0056, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
riboflavin kinase
UniProt
CTP-dependent riboflavin kinase
-
-
Methanocaldococcus jannaschii Mj0056
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:riboflavin 5′-phosphotransferase
This archaeal enzyme differs from EC 2.7.1.26, riboflavin kinase, in using CTP as the donor nucleotide. UTP, but not ATP or GTP, can also act as a phosphate donor but it is at least an order of magnitude less efficient than CTP.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-82-0
c.f. EC 2.7.1.26
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + riboflavin
ADP + FMN
show the reaction diagram
30% of the activity with CTP
-
-
?
ATP + riboflavin
ADP + riboflavin 5'-phosphate
show the reaction diagram
30% of the activity with ATP
-
-
?
CTP + riboflavin
CDP + FMN
show the reaction diagram
CTP + riboflavin
CDP + riboflavin 5'-phosphate
show the reaction diagram
GTP + riboflavin
GDP + FMN
show the reaction diagram
11% of the activity with CTP
-
-
?
GTP + riboflavin
GDP + riboflavin 5'-phosphate
show the reaction diagram
11% of the activity with ATP
-
-
?
CTP + riboflavin
CDP + FMN
show the reaction diagram
at reaction temperatures of up to 85°C (the temperature of the natural habitat of Methanocaldococcus jannaschii) riboflavin is completely converted to FMN
-
-
?
UTP + riboflavin
UDP + FMN
show the reaction diagram
activity with UTP is at least one order of magnitude less efficient
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP + riboflavin
CDP + FMN
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg2+
1.6 mM, 15% inhibition
Mn2+
1.6 mM, 50% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
CTP
0.159
riboflavin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
RbkRs genetic and sequence comparisons
physiological function
riboflavin kinase is an essential enzyme required for synthesis of FMN cofactor from vitamin B2. The bifunctional riboflavin kinase/regulator (RbkR) controls riboflavin biosynthesis and transport genes in major lineages of Crenarchaeota, Euryarchaeota and Thaumarchaeota. RbkR proteins are composed of the riboflavin kinase domain and a DNA-binding winged helix-turn-helix-like domain
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
1 * 15000, SDS-PAGE
15218
1 * 15218, electrospray mass spectrometry
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Mj0056 has sequence properties intermediate between basal cradle-loop barrels and ATP-dependent riboflavin kinases. It is proposed that it represents an evolutionary bridge between the two groups of proteins
Mj0056-MgCDP and Mj0056-MgCDP-FMN, in complex with natural reaction products and, Mj0056-NaCDP-PO4, with inorganic phosphate bound in a similar position as the FMN phosphate
structures, Mj0056-MgCDP and Mj0056-MgCDP-FMN, in complex with natural reaction products and a third, Mj0056-NaCDP-PO4, with inorganic phosphate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
10 min at room temperature, 60% loss of activity
680522
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 min at room temperature, followed by dilution in acetate buffer (pH 6.0)
the enzyme retains 40% (0.13 nmol/min) of its activity compared to the control (0.32 nmol/min) after treatment with 0.1 M HCl (pH 1.05) for
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene ribK, genomic organization
recombinant expression of the MJ0056 gene in Escherichia coli
recombinant expression of the MJ0056 gene in Escherichia coli led to a large increase in the amount of flavin mononucleotide in the Escherichia coli cell extract
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mashhadi, Z.; Zhang, H.; Xu, H.; White, R.H.
Identification and characterization of an archaeon-specific riboflavin kinase
J. Bacteriol.
190
2615-2618
2008
Methanocaldococcus jannaschii (Q60365), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Ammelburg, M.; Hartmann, M.D.; Djuranovic, S.; Alva, V.; Koretke, K.K.; Martin, J.; Sauer, G.; Truffault, V.; Zeth, K.; Lupas, A.N.; Coles, M.
A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels
Structure
15
1577-1590
2007
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q60365)
Manually annotated by BRENDA team
Rodionova, I.A.; Vetting, M.W.; Li, X.; Almo, S.C.; Osterman, A.L.; Rodionov, D.A.
A novel bifunctional transcriptional regulator of riboflavin metabolism in Archaea
Nucleic Acids Res.
45
3785-3799
2017
Metallosphaera yellowstonensis (H2C8H2), Metallosphaera yellowstonensis MK1 (H2C8H2), Methanocaldococcus jannaschii (Q60365), Methanocaldococcus jannaschii ATCC 43067 (Q60365), Methanocaldococcus jannaschii DSM 2661 (Q60365), Methanocaldococcus jannaschii JAL-1 (Q60365), Methanocaldococcus jannaschii JCM 10045 (Q60365), Methanocaldococcus jannaschii NBRC 100440 (Q60365), Pyrobaculum sp. WP30 (A0A0K1E2F9), Thermoplasma acidophilum (Q9HJA6), Thermoplasma acidophilum, Thermoplasma acidophilum AMRC-C165 (Q9HJA6), Thermoplasma acidophilum ATCC 25905 (Q9HJA6), Thermoplasma acidophilum JCM 9062 (Q9HJA6), Thermoplasma acidophilum NBRC 15155 (Q9HJA6)
Manually annotated by BRENDA team