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Literature summary for 1.14.14.181 extracted from

  • Sharma, M.; Lingford, J.P.; Petricevic, M.; Snow, A.J.D.; Zhang, Y.; Jaerva, M.A.; Mui, J.W.; Scott, N.E.; Saunders, E.C.; Mao, R.; Epa, R.; da Silva, B.M.; Pires, D.E.V.; Ascher, D.B.; McConville, M.J.; Davies, G.J.; Williams, S.J.; Goddard-Borger, E.D.
    Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria (2022), Proc. Natl. Acad. Sci. USA, 119, e2116022119 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.181

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.9 A resolution. Enzyme consists of a core (alpha/beta)8 triose-phosphate isomerase barrel with three additional insertion regions Rhizobium oryzae
to 3.4 A resolution Agrobacterium fabrum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-sulfo-D-quinovose + FMNH2 + O2 Agrobacterium fabrum
-
 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
6-sulfo-D-quinovose + FMNH2 + O2 Rhizobium oryzae
-
 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
6-sulfo-D-quinovose + FMNH2 + O2 Agrobacterium fabrum C58
-
 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
additional information Agrobacterium fabrum enzyme is highly specific for 6-sulfo-D-quinovose. 6-Sulfo-D-quinovose binds SmoC with Kd of 3 microM. No activity with other sulfonates tested ?
-
-
additional information Agrobacterium fabrum C58 enzyme is highly specific for 6-sulfo-D-quinovose. 6-Sulfo-D-quinovose binds SmoC with Kd of 3 microM. No activity with other sulfonates tested ?
-
-

Organism

Organism UniProt Comment Textmining
Agrobacterium fabrum A9CEY7
-
-
Agrobacterium fabrum C58 A9CEY7
-
-
Rhizobium oryzae A0A1X7D696
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-sulfo-D-quinovose + FMNH2 + O2
-
 Agrobacterium fabrum 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
6-sulfo-D-quinovose + FMNH2 + O2
-
 Rhizobium oryzae 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
6-sulfo-D-quinovose + FMNH2 + O2
-
 Agrobacterium fabrum C58 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
additional information enzyme is highly specific for 6-sulfo-D-quinovose. 6-Sulfo-D-quinovose binds SmoC with Kd of 3 microM. No activity with other sulfonates tested Agrobacterium fabrum ?
-
-
additional information enzyme is highly specific for 6-sulfo-D-quinovose. 6-Sulfo-D-quinovose binds SmoC with Kd of 3 microM. No activity with other sulfonates tested Agrobacterium fabrum C58 ?
-
-

Subunits

Subunits Comment Organism
dimer crystallization data Agrobacterium fabrum
dimer crystallization data Rhizobium oryzae

Synonyms

Synonyms Comment Organism
SAMN02982989_5106
-
 Rhizobium oryzae
smoC
-
 Agrobacterium fabrum
smoC
-
 Rhizobium oryzae

Cofactor

Cofactor Comment Organism Structure
FMN FMN binding site is a deep hydrophobic pocket that accommodates the isoalloxazine ring system and extends out to the protein-solvent interface, which is gated by conserved phosphate-binding residues Tyr136 and Ser189 Rhizobium oryzae

General Information

General Information Comment Organism
evolution the sulfoquinovose monooxygenase pathway is distributed across Alpha- and Betaproteobacteria and is especially prevalent within the Rhizobiales order Agrobacterium fabrum
physiological function enzyme is part of a pathway for sulfoquinovose degradation. Sulfoquinovose is acted on by flavin mononucleotide-dependent sulfoquinovose monooxygenase, in concert with an NADH-dependent flavin reductase, to release sulfite and 6-oxo-glucose Agrobacterium fabrum