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Information on EC 2.7.7.2 - FAD synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38913

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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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Saccharomyces cerevisiae
UNIPROT: P38913
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Word Map
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
ATP
+
FMN
=
diphosphate
+
FAD
+
=
+
Synonyms
fads1, flad1, fad synthase, fad pyrophosphorylase, flavin adenine dinucleotide synthetase, atp:fmn adenylyltransferase, atribf1, atribf2, fmn:atp adenylyltransferase, mj1179, 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
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
diphosphate + FAD
ATP + FMN
show the reaction diagram
-
-
-
r
additional information
?
-
-
in the reverse reaction diphosphate cannot be replaced by orthophosphate or metaphosphate
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
no FAD synthesis in absence of ATP, ADP cannot replace ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for FAD synthesis, optimal concentration 1.5 mM, inhibition at higher levels
additional information
-
Zn2+ cannot replace Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
inhibits FAD cleavage completely
NAD+
-
inhibits FAD cleavage completely
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
presence of mitochondrial FAD synthetase activity in strains transformed with FAD1 on a high-copy-number plasmid, but not in mitochondria of wild-type strains
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
recombinant enzyme, expressed in E. coli, PAGE
36000
recombinant enzyme, expressed in E. coli, PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with FAD, hanging drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.4
-
at pH 6.0 10% as active as at pH 7.5, at pH 8.4 64%
642993
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is instable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
3°C, loses 20-30% of its activity in 4 days, 58% in 11 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
structural gene FAD1, essential yeast protein, disruption of the gene induces a lethal phenotype, cloned from a genomic library, vector pATH26 transformed into Saccharomyces cerevisiae and Escherichia coli RR1 on a multicopy plasmid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schrecker, A.W.; Kornberg, A.
Reversible enzymatic synthesis of flavin-adenine dinucleotide
J. Biol. Chem.
182
795-803
1950
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Wu, M.; Repetto, B.; Glerum, D.M.; Tzagoloff, A.
Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae
Mol. Cell. Biol.
15
264-271
1995
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38913)
Manually annotated by BRENDA team
Leulliot, N.; Blondeau, K.; Keller, J.; Ulryck, N.; Quevillon-Cheruel, S.; van Tilbeurgh, H.
Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD
J. Mol. Biol.
398
641-646
2010
Saccharomyces cerevisiae (P38913)
Manually annotated by BRENDA team