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Information on EC 3.1.3.102 - FMN hydrolase
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3.1.3.102 FMN hydrolaseIUBMB Comments
Requires Mg2+. The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily. Most of the isoforms have a wide substrate specificity , but isoforms specific for FMN also exist .
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Word Map
- 3.1.3.102
- riboflavin
- flavin
-
dehalogenase
-
haloacid
- fad
- mononucleotide
-
pyrophosphatase
- plastid
- chloroplasts
-
3.1.3.2
-
mg2+-dependent
- 5'-phosphate
-
protoplasts
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fmn hydrolase, atcpfhy1, fmn phosphohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
At4g21470
AtFMN/FHy
At4g21470
gene name, bifunctional riboflavin kinase/FMN phosphatase
At4g21470
gene name, bifunctional riboflavin kinase/FMN phosphatase
-
AtFMN/FHy
bifunctional riboflavin kinase/FMN phosphatase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMN + H2O = riboflavin + phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
FMN phosphohydrolase
Requires Mg2+. The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily. Most of the isoforms have a wide substrate specificity [2], but isoforms specific for FMN also exist [3].
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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
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
25% of the activity with 4-nitrophenyl phosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
47% of the activity with 4-nitrophenyl phosphate
-
-
?
FMN + H2O
riboflavin + phosphate
high specificity for FMN. The enzyme does not hydrolyze the following substrates: ADP, AMP, ATP, CTP, GTP, IMP, UTP, xanthosine 5'-monophosphate, dATP, glucose 1-phosphate, glucose 6-phosphate, glucose 1,6-bisphosphate, and fructose 1,6-bisphosphate, pyridoxal 5'-phosphate and NADP+
-
-
?
FMN + H2O
riboflavin + phosphate
-
most important physiological substrate, 87% of the activity with 4-nitrophenyl phosphate
-
-
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays
phosphate
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase is inhibited
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tween 20
enzyme activity increases and temperature optimum shifts to 510°C higher temperature in the presence of Tween 20
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
pH 5.0: about 90% of maximal activity, pH 8.0: about 60% of maximal activity
6 - 8.5
pH 6.0: about 90% of maximal activity, pH 8.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
30°C: about 65% of maximal activity, 50°C: about 55% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional riboflavin kinase/FMN phosphatase
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
inhibition of 14C-riboflavin uptake by FMN and FAD in everted rings of rat intestine is directly related to the amount of conversion of these coenzymes to free riboflavin by intestinal enzymes. When FMN and FAD conversion to riboflavin is inhibited by EDTA, competition with 14C-riboflavin for transport is correspondingly decreased, best explained by a sequential process in which hydrolysis of FMN and FAD by enzymes of the intestinal brush border is followed by absorption of free riboflavin
physiological function
-
not only de novo riboflavin synthesis but also the hydrolysis of FMN contributes to riboflavin secretion under conditions of Fe deficiency. Respiration activity is also enhanced after 3 days under Fe deficiency
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FHY1C_ARATH
245
0
27695
Swiss-Prot
Chloroplast (Reliability: 2)
FHYRK_ARATH
379
0
42110
Swiss-Prot
Secretory Pathway (Reliability: 5)
A0A3B0M6Y3_9GAMM
185
0
20639
TrEMBL
-
A0A3B1DUA5_9GAMM
237
0
27059
TrEMBL
-
A0A5B6Z361_DAVIN
251
0
27492
TrEMBL
other Location (Reliability: 3)
A0A5B6Z6C3_DAVIN
253
0
28072
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25700
FMN hydrolase domains of the bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
43600
bifunctional riboflavin kinase/FMN phosphatase, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 42100, bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
monomer
-
1 * 42100, bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of the bifunctional riboflavin kinase/FMN phosphatase (AtFMN/FHy). Riboflavin kinase and FMN hydrolase domains of AtFMN/FHy can be physically separated, with little change in their kinetic properties
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in Fe-deficient root cultures, FMN hydrolase activity is substantially increased after 3 days, when riboflavin secretion becomes detectable
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akiyama, T.; Selhub, J.; Rosenberg, J.H.
FMN phosphatase and FAD pyrophosphatase in rat intestinal brush borders: Role in intestinal absorption of dietary riboflavin
J. Nutr.
112
263-268
1982
Rattus norvegicus
brenda
Barile, M.; Brizio, C.; de Virgilio, C.; Delfine, S.; Quagliariello, E.; Passarella, S.
Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver: The occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
Eur. J. Biochem.
249
777-785
1997
Rattus norvegicus
brenda
Sandoval, F.J.; Roje, S.
An FMN hydrolase is fused to a riboflavin kinase homolog in plants
J. Biol. Chem.
280
38337-38345
2005
Arabidopsis thaliana (Q84MD8), Arabidopsis thaliana ecotype Columbia (Q84MD8)
brenda
Higa, A.; Khandakar, J.; Mori, Y.; Kitamura, Y.
Increased de novo riboflavin synthesis and hydrolysis of FMN are involved in riboflavin secretion from Hyoscyamus albus hairy roots under iron deficiency
Plant Physiol. Biochem.
58
166-173
2012
Hyoscyamus albus
brenda
Rawat, R.; Sandoval, F.J.; Wei, Z.; Winkler, R.; Roje, S.
An FMN hydrolase of the haloacid dehalogenase superfamily is active in plant chloroplasts
J. Biol. Chem.
286
42091-42098
2011
Pisum sativum cv. Bohatyr, Arabidopsis thaliana (F4HQA8), Arabidopsis thaliana
brenda
Mallik, S.; Dey, M.; Dutta, M.; Ghosh, A.; Bandyopadhyay, D.
Flavin mononucleotide phosphatase from goat liver: A possible target for divalent heavy metal cations
Int. J. Pharm. Pharm. Sci.
6
708-714
2014
Capra hircus
-
brenda
Kuznetsova, E.; Proudfoot, M.; Gonzalez, C.F.; Brown, G.; Omelchenko, M.V.; Borozan, I.; Carmel, L.; Wolf, Y.I.; Mori, H.; Savchenko, A.V.; Arrowsmith, C.H.; Koonin, E.V.; Edwards, A.M.; Yakunin, A.F.
Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family
J. Biol. Chem.
281
36149-36161
2006
Escherichia coli
brenda
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