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Literature summary for 1.14.13.111 extracted from

  • Henriques, A.C.; De Marco, P.
    Methanesulfonate (MSA) catabolic genes from marine and estuarine bacteria (2015), PLoS ONE, 10, e0125735 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) 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 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 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 Methylosulfonomonas methylovora

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Candidatus Filomicrobium marinum 5737
-
cytoplasm
-
Methylobacterium sp. P1 5737
-
cytoplasm
-
Methylobacterium sp. RD4.1 5737
-
cytoplasm
-
Hyphomicrobium sp. P2 5737
-
cytoplasm
-
Methylosulfonomonas methylovora 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ two iron ions per enzyme molecule Candidatus Filomicrobium marinum
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 Hyphomicrobium sp. P2
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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?

Synonyms

Synonyms Comment Organism
methanesulfonate monooxygenase
-
Candidatus Filomicrobium marinum
methanesulfonate monooxygenase
-
Methylobacterium sp. P1
methanesulfonate monooxygenase
-
Methylobacterium sp. RD4.1
methanesulfonate monooxygenase
-
Hyphomicrobium sp. P2
methanesulfonate monooxygenase
-
Methylosulfonomonas methylovora
MSAMO
-
Candidatus Filomicrobium marinum
MSAMO
-
Methylobacterium sp. P1
MSAMO
-
Methylobacterium sp. RD4.1
MSAMO
-
Hyphomicrobium sp. P2
MSAMO
-
Methylosulfonomonas methylovora
MsmA
-
Candidatus Filomicrobium marinum
MsmA
-
Methylobacterium sp. P1
MsmA
-
Methylobacterium sp. RD4.1
MsmA
-
Hyphomicrobium sp. P2
MsmA
-
Methylosulfonomonas methylovora

General Information

General Information Comment 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 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 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 Methylosulfonomonas methylovora