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Information on EC 3.1.3.102 - FMN hydrolase and Organism(s) Arabidopsis thaliana and UniProt Accession Q84MD8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.102 FMN hydrolase
IUBMB 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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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q84MD8
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
fmn hydrolase, atcpfhy1, fmn phosphohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
At4g21470
gene name, bifunctional riboflavin kinase/FMN phosphatase
AtFMN/FHy
bifunctional riboflavin kinase/FMN phosphatase
PATHWAY SOURCE
PATHWAYS
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FMN + H2O
riboflavin + phosphate
show the reaction diagram
-
-
-
?
FMN + H2O
riboflavin + phosphate
show the reaction diagram
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
FMN + H2O
riboflavin + phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tween 20
enzyme activity increases and temperature optimum shifts to 5–10°C higher temperature in the presence of Tween 20
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
FMN
pH 7.5, 30°C
0.0142
FMN
pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.822
FMN
pH 7.5, 30°C
0.59
FMN
pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1028
FMN
pH 7.5, 30°C
41.5
FMN
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.1
pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
30°C: about 65% of maximal activity, 50°C: about 55% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional riboflavin kinase/FMN phosphatase
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FHYRK_ARATH
379
0
42110
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25700
FMN hydrolase domains of the bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
43600
bifunctional riboflavin kinase/FMN phosphatase, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 42100, bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Arabidopsis thaliana (F4HQA8), Arabidopsis thaliana, Pisum sativum cv. Bohatyr
Manually annotated by BRENDA team