Information on EC 2.7.1.161 - CTP-dependent riboflavin kinase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
2.7.1.161
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RECOMMENDED NAME
GeneOntology No.
CTP-dependent riboflavin kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + riboflavin = CDP + FMN
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
flavin biosynthesis II (archaea)
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Metabolic pathways
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Riboflavin metabolism
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flavin biosynthesis
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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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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?
ATP + riboflavin
ADP + riboflavin 5'-phosphate
show the reaction diagram
30% of the activity with ATP
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?
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
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?
GTP + riboflavin
GDP + riboflavin 5'-phosphate
show the reaction diagram
11% of the activity with ATP
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?
UTP + riboflavin
UDP + FMN
show the reaction diagram
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activity with UTP is at least one order of magnitude less efficient
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?
additional information
?
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ATP and GTP do not support the production of FMN at 85C
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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contains 4-5 mol of Mg2+ and 0.0013 mol of Zn2+ per mol of protein; contains 4 to 5 mol of Mg per mol of protein; the enzyme contains 4 to 5 mol of Mg
Zn2+
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contains 0.0013 mol of Zn per mol of protein; contains 4-5 mol of Mg2+ and 0.0013 mol of Zn2+ per mol of protein
additional information
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absence of a requirement for added metal ion to catalyze the formation of FMN; purified recombinant enzyme shows no requirement for added metal ion to catalyze the formation of FMN
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
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1.6 mM, 40% inhibition; 1.6 mM, 61% inhibition
Cu2+
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1.6 mM, 3% inhibition; 1.6 mM, 97% inhibition
Mg2+
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1.6 mM, 15% inhibition
Mn2+
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1.6 mM, 50% inhibition
Ni2+
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1.6 mM, 43% inhibition; 1.6 mM, 60% inhibition
Zn2+
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1.6 mM, 17% inhibition; 1.6 mM, 83% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
CTP
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; pH 7.2, 70C
0.159
riboflavin
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; pH 7.2, 70C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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riboflavin kinase is induced by acriflavin
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
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1 * 15000, SDS-PAGE
15218
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1 * 15218, electrospray mass spectrometry
19700
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gel filtration
additional information
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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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 15000, SDS-PAGE; 1 * 15218, electrospray mass spectrometry; 1 * 19700
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
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10 min at room temperature, 60% loss of activity
680522
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
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10 min, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 min at room temperature, followed by dilution in acetate buffer (pH 6.0)
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant; recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; 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
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