BRENDA - Enzyme Database
show all sequences of 1.14.13.111

Methanesulfonate (MSA) catabolic genes from marine and estuarine bacteria

Henriques, A.C.; De Marco, P.; PLoS ONE 10, e0125735 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Hyphomicrobium sp. P2
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Methylobacterium sp. P1
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Methylobacterium sp. RD4.1
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Methylosulfonomonas methylovora
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha; gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Candidatus Filomicrobium marinum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
;
Candidatus Filomicrobium marinum
5737
-
cytoplasm
-
Hyphomicrobium sp. P2
5737
-
cytoplasm
-
Methylobacterium sp. P1
5737
-
cytoplasm
-
Methylobacterium sp. RD4.1
5737
-
cytoplasm
-
Methylosulfonomonas methylovora
5737
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
two iron ions per enzyme molecule; two iron ions per enzyme molecule
Candidatus Filomicrobium marinum
Fe2+
two iron ions per enzyme molecule
Hyphomicrobium sp. P2
Fe2+
two iron ions per enzyme molecule
Methylobacterium sp. P1
Fe2+
two iron ions per enzyme molecule
Methylobacterium sp. RD4.1
Fe2+
two iron ions per enzyme molecule
Methylosulfonomonas methylovora
[2Fe-2S] cluster
the predicted gene product of gene msmA reveals a unique sequence in the region associated to the Rieske-type [2Fe-2S] cluster, with a longer-than-usual 26-amino acid spacer between the two highly conserved cysteine-histidine groups in the CXH-Xn-CXXH conserved motif
Methylosulfonomonas methylovora
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methanesulfonate + NADH + H+ + O2
Candidatus Filomicrobium marinum
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylobacterium sp. P1
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylobacterium sp. RD4.1
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Hyphomicrobium sp. P2
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylosulfonomonas methylovora
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Candidatus Filomicrobium marinum W
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylosulfonomonas methylovora M2
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Candidatus Filomicrobium marinum Y
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Candidatus Filomicrobium marinum
A0A0D6JGB8
alpha-subunit of the hydroxylase; from ocean surface water sample collected roughly 5 Km off the coast of Matosinhos, Portugal
-
Candidatus Filomicrobium marinum
A0A0G2RHR1
from ocean surface water sample collected roughly 5 Km off the coast of Matosinhos, Portugal
-
Candidatus Filomicrobium marinum W
A0A0G2RHR1
from ocean surface water sample collected roughly 5 Km off the coast of Matosinhos, Portugal
-
Candidatus Filomicrobium marinum Y
A0A0D6JGB8
alpha-subunit of the hydroxylase; from ocean surface water sample collected roughly 5 Km off the coast of Matosinhos, Portugal
-
Hyphomicrobium sp. P2
A0A0G2RHB5
-
-
Methylobacterium sp. P1
A0A0G2RG68
-
-
Methylobacterium sp. RD4.1
A0A0G2RI26
-
-
Methylosulfonomonas methylovora
Q9X404
alpha-subunit of the hydroxylase
-
Methylosulfonomonas methylovora M2
Q9X404
alpha-subunit of the hydroxylase
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
methanesulfonate + NADH + H+ + O2
-
746182
Candidatus Filomicrobium marinum
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylobacterium sp. P1
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylobacterium sp. RD4.1
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Hyphomicrobium sp. P2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylosulfonomonas methylovora
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Candidatus Filomicrobium marinum W
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylosulfonomonas methylovora M2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Candidatus Filomicrobium marinum Y
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Candidatus Filomicrobium marinum
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Hyphomicrobium sp. P2
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Methylobacterium sp. P1
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Methylobacterium sp. RD4.1
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
Methylosulfonomonas methylovora
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Candidatus Filomicrobium marinum
5737
-
cytoplasm
-
Hyphomicrobium sp. P2
5737
-
cytoplasm
-
Methylobacterium sp. P1
5737
-
cytoplasm
-
Methylobacterium sp. RD4.1
5737
-
cytoplasm
-
Methylosulfonomonas methylovora
5737
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
two iron ions per enzyme molecule
Candidatus Filomicrobium marinum
Fe2+
two iron ions per enzyme molecule
Hyphomicrobium sp. P2
Fe2+
two iron ions per enzyme molecule
Methylobacterium sp. P1
Fe2+
two iron ions per enzyme molecule
Methylobacterium sp. RD4.1
Fe2+
two iron ions per enzyme molecule
Methylosulfonomonas methylovora
[2Fe-2S] cluster
the predicted gene product of gene msmA reveals a unique sequence in the region associated to the Rieske-type [2Fe-2S] cluster, with a longer-than-usual 26-amino acid spacer between the two highly conserved cysteine-histidine groups in the CXH-Xn-CXXH conserved motif
Methylosulfonomonas methylovora
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methanesulfonate + NADH + H+ + O2
Candidatus Filomicrobium marinum
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylobacterium sp. P1
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylobacterium sp. RD4.1
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Hyphomicrobium sp. P2
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylosulfonomonas methylovora
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Candidatus Filomicrobium marinum W
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Methylosulfonomonas methylovora M2
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
methanesulfonate + NADH + H+ + O2
Candidatus Filomicrobium marinum Y
-
formaldehyde + NAD+ + sulfite + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
methanesulfonate + NADH + H+ + O2
-
746182
Candidatus Filomicrobium marinum
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylobacterium sp. P1
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylobacterium sp. RD4.1
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Hyphomicrobium sp. P2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylosulfonomonas methylovora
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Candidatus Filomicrobium marinum W
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Methylosulfonomonas methylovora M2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
-
746182
Candidatus Filomicrobium marinum Y
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
evolution
the two msm operons in Filomicrobium sp. strains Y and W are divergently transcribed, like in Methylosulfonomonas methylovora str. M2; the two msm operons in Filomicrobium sp. strains Y and W are divergently transcribed, like in Methylosulfonomonas methylovora str. M2
Candidatus Filomicrobium marinum
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy; the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Candidatus Filomicrobium marinum
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Hyphomicrobium sp. P2
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Methylobacterium sp. P1
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Methylobacterium sp. RD4.1
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Methylosulfonomonas methylovora
General Information (protein specific)
General Information
Commentary
Organism
evolution
the two msm operons in Filomicrobium sp. strains Y and W are divergently transcribed, like in Methylosulfonomonas methylovora str. M2
Candidatus Filomicrobium marinum
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Candidatus Filomicrobium marinum
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Hyphomicrobium sp. P2
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Methylobacterium sp. P1
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Methylobacterium sp. RD4.1
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
Methylosulfonomonas methylovora
Other publictions for EC 1.14.13.111
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746182
Henriques
Methanesulfonate (MSA) catabo ...
Candidatus Filomicrobium marinum, Candidatus Filomicrobium marinum W, Candidatus Filomicrobium marinum Y, Hyphomicrobium sp. P2, Methylobacterium sp. P1, Methylobacterium sp. RD4.1, Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
PLoS ONE
10
e0125735
2015
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694958
Jamshad
Purification and crystallizati ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
Protein Expr. Purif.
52
472-477
2007
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692108
Moosvi
Isolation and properties of me ...
Afipia felis
Environ. Microbiol.
7
22-23
2005
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738122
Moosvi
Isolation and properties of me ...
Afipia felis
Environ. Microbiol.
7
22-33
2005
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690515
Baxter
Duplicate copies of genes enco ...
Marinosulfonomonas methylotropha, Marinosulfonomonas methylotropha TR3
Appl. Environ. Microbiol.
68
289-296
2002
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692154
Reichenbecher
Purification and partial chara ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
Eur. J. Biochem.
267
4763-4769
2000
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690638
Kelly
Microbial metabolism of methan ...
Methylosulfonomonas methylovora
Arch. Microbiol.
172
341-348
1999
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692819
de Marco
Molecular analysis of a novel ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
J. Bacteriol.
181
2244-2251
1999
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692817
Higgins
Purification and molecular cha ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
J. Bacteriol.
179
1974-1979
1979
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2
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-