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Information on EC 2.7.7.2 - FAD synthase and Organism(s) Bacillus subtilis and UniProt Accession P54575

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.2 FAD synthase
IUBMB Comments
Requires Mg2+ and is highly specific for ATP as phosphate donor . 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 FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].
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This record set is specific for:
Bacillus subtilis
UNIPROT: P54575
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Word Map
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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ATP
+
FMN
=
diphosphate
+
FAD
+
=
+
Synonyms
fads1, flad1, fad synthase, fad pyrophosphorylase, flavin adenine dinucleotide synthetase, atribf2, atp:fmn adenylyltransferase, atribf1, mj1179, fmn:atp adenylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine triphosphate-riboflavin mononucleotide transadenylase
-
-
-
-
adenosine triphosphate-riboflavine mononucleotide transadenylase
-
-
-
-
FAD pyrophosphorylase
-
-
-
-
FMN adenylyltransferase
-
-
-
-
FMN pyrophosphorylase
-
-
-
-
lysZ
-
-
-
-
riboflavin adenine dinucleotide pyrophosphorylase
-
-
-
-
riboflavin mononucleotide adenylyltransferase
-
-
-
-
riboflavine adenine dinucleotide adenylyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:FMN adenylyltransferase
Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. 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 [3]. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].
CAS REGISTRY NUMBER
COMMENTARY hide
9026-37-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + FMN
diphosphate + FAD
show the reaction diagram
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
ATP + FMN
diphosphate + FAD
show the reaction diagram
essential for flavin metabolism
-
r
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
1012
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34180
wild-type, gel filtration
34200
gel filtration, nondenaturing conditions
34230
mutant RibC, gel filtration
35670
36000
wild-type, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 36000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 2 weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ribC encodes a bifunctional flavokinase/FAD-synthetase, cloned and overexpressed in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Bacillus subtilis 168 (P54575)
Manually annotated by BRENDA team