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Information on EC 2.7.1.26 - riboflavin kinase and Organism(s) Bacillus subtilis and UniProt Accession P54575
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2.7.1.26 riboflavin kinaseIUBMB Comments
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates . While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase . A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP .
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Word Map
- 2.7.1.26
- mononucleotide
- ammoniagenes
-
fadss
- isoalloxazine
-
kyphoplasty
-
flavocoenzyme
-
flavinogenic
-
ribityl
- davawensis
- roseoflavin
- famata
-
ctp-dependent
- synthesis
- drug development
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
rfk, flavokinase, riboflavin kinase, fad synthetase, fmnat, cafads, fmn adenylyltransferase, hsrfk, atfmn/fhy, flavokinase/fad synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FK
-
-
-
-
flavokinase
-
-
-
-
flavokinase/flavin adenine dinucleotide synthetase
-
bifunctional enzyme EC 2.7.1.26/EC 2.7.2.2
kinase, riboflavin
-
-
-
-
riboflavine kinase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:riboflavin 5'-phosphotransferase
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6].
CAS REGISTRY NUMBER
COMMENTARY
9032-82-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + riboflavin
CDP + riboflavin 5'-phosphate
-
50% of the activity with ATP
-
-
?
ATP + riboflavin
ADP + FMN
ribC is essential for growth of Bacillus subtilis. RibC is not directly involved in the riboflavin regulatory system
-
-
?
ATP + riboflavin
ADP + FMN
-
specific for the reduced form of riboflavin
-
-
?
ATP + riboflavin
ADP + FMN
-
the flavokinase activity appears to be localized to the N-terminal domain of the protein. RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. In RibR itself, interaction was localized to the carboxy-terminate part of the protein
-
-
?
additional information
?
-
ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity
-
-
?
additional information
?
-
-
ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity
-
-
?
additional information
?
-
-
the riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + riboflavin
ADP + FMN
ribC is essential for growth of Bacillus subtilis. RibC is not directly involved in the riboflavin regulatory system
-
-
?
additional information
?
-
-
the riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
-
-
?
ATP + riboflavin
ADP + FMN
-
the flavokinase activity appears to be localized to the N-terminal domain of the protein. RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. In RibR itself, interaction was localized to the carboxy-terminate part of the protein
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
RibC from wild-type strain 1012 and RibC820 from riboflavin-overproducing mitant strain RB52.ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity
Uniprot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kearny, E.B.; Goldenberg, J.; Lipsick, J.; Perl, M.
Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins
J. Biol. Chem.
254
9551-9557
1979
Bacillus subtilis
Solovieva, I.M.; Tarasov, K.V.; Perumov, D.A.
Main physicochemical features of monofunctional flavokinase from Bacillus subtilis
Biochemistry
68
177-181
2003
Bacillus subtilis
Mack, M.; van Loon, A.P.; Hohmann, H.P.
Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC
J. Bacteriol.
180
950-955
1998
Bacillus subtilis (P54575), Bacillus subtilis
Solovieva, I.M.; Kreneva, R.A.; Leak, D.J.; Perumov, D.A.
The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon
Microbiology
145
67-73
1999
Bacillus subtilis
Solovieva, I.M.; Kreneva, R.A.; Errais Lopes, L.; Perumov, D.A.
The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
FEMS Microbiol. Lett.
243
51-58
2005
Bacillus subtilis
Higashitsuji, Y.; Angerer, A.; Berghaus, S.; Hobl, B.; Mack, M.
RibR, a possible regulator of the Bacillus subtilis riboflavin biosynthetic operon, in vivo interacts with the 5-untranslated leader of rib mRNA
FEMS Microbiol. Lett.
274
48-54
2007
Bacillus subtilis
Grill, S.; Busenbender, S.; Pfeiffer, M.; Koehler, U.; Mack, M.
The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
J. Bacteriol.
190
1546-1553
2008
Bacillus subtilis, Streptomyces davaonensis (A3FM23), Streptomyces davaonensis
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