Sulfur Containing Compound Database
Gene name | FMOGS-OX1 |
AGI ID | AT1G65860 |
Gene length | 457 |
Uniprot ID | Q9SS04 |
Protein Name | Flavin-containing monooxygenase FMO GS-OX1 |
Synonym | F12P19.2 |
EC number | EC 1.8.-.- |
Entrez Gene | 88765 |
Refseq mrna | NM_105258 |
Refseq protein | NP_176761 |
Function | Flavin-monooxygenase (FMO) enzyme; FMOGS-OX1 catalyzes the conversion of methylthioalkyl GSLs into methylsulfinylalkyl GSLs. This is evidenced by biochemical characterization of the recombinant protein and analyses of the GSL content in FMOGS-OX1 overexpression lines and an FMOGS-OX1 knock-out mutant of Arabidopsis. The FMOGS-OX1 overexpression lines show almost complete conversion of methylthioalkyl into methylsulfinylalkyl GSLs with an approximately fivefold increase in 4-methylsulfinylbutyl GSL in seeds. Identification of FMOGS-OX1 provides a molecular tool for breeding of Brassica vegetable crops with increased levels of this important GSL which has implications for production of functional foods enriched with the cancer-preventive sulforaphane (Hansen et al. 2007) |
Group | GSL side chain modificatian |
Reference | Hansen et al. (2007); Li et al. (2008); Li et al. (2011) |
Organism | AGI ID | Gene Name | Protein Name | Identity | E-Value | Description |
---|---|---|---|---|---|---|
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
78 |
0.00E+00 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
69 |
0.00E+00 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
65 |
0.00E+00 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
67 |
0.00E+00 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
66 |
0.00E+00 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
63 |
0.00E+00 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
63 |
0.00E+00 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
62 |
0.00E+00 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
63 |
0.00E+00 |
||
Papaya |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
60 |
0.00E+00 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
59 |
4.00E-179 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
58 |
6.00E-177 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
45 |
3.00E-120 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
44 |
1.00E-116 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
44 |
7.00E-116 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
43 |
2.00E-114 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
43 |
5.00E-114 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
43 |
2.00E-111 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
40 |
1.00E-102 |
||
Papaya |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
47 |
1.00E-91 |
||
Cabbage |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
47 |
8.00E-90 |
||
Broccoli |
FMOGS-OX1 |
Flavin-containing monooxygenase FMO GS-OX1 |
42 |
3.00E-71 |
GO ID | Ontology | GO Term | Description |
---|---|---|---|
MF |
monooxygenase activity |
Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water. |
|
MF |
N,N-dimethylaniline monooxygenase activity |
Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O. |
|
CC |
nucleus |
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some |
|
BP |
glucosinolate biosynthetic process from homomethionine |
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including homomethionine. |
|
MF |
flavin adenine dinucleotide binding |
Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
|
MF |
NADP binding |
Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
|
BP |
oxidation-reduction process |
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
|
MF |
3-methylthiopropyl glucosinolate S-oxygenase activity |
Catalysis of the reaction: 3-methylthiopropyl-glucosinolate = 3-methylsulfinylpropyl-glucosinolate. |
|
MF |
4-methylthiopropyl glucosinolate S-oxygenase activity |
Catalysis of the reaction: 4-methylthiopropyl-glucosinolate = 4-methylsulfinylpropyl-glucosinolate. |
|
MF |
5-methylthiopropyl glucosinolate S-oxygenase activity |
Catalysis of the reaction: 5-methylthiopropyl-glucosinolate = 5-methylsulfinylpropyl-glucosinolate. |
|
MF |
6-methylthiopropyl glucosinolate S-oxygenase activity |
Catalysis of the reaction: 6-methylthiopropyl-glucosinolate = 6-methylsulfinylpropyl-glucosinolate. |
|
MF |
7-methylthiopropyl glucosinolate S-oxygenase activity |
Catalysis of the reaction: 7-methylthiopropyl-glucosinolate = 7-methylsulfinylpropyl-glucosinolate. |
|
MF |
8-methylthiopropyl glucosinolate S-oxygenase activity |
Catalysis of the reaction: 8-methylthiopropyl-glucosinolate = 8-methylsulfinylpropyl-glucosinolate. |
Pubmed ID | Authors | Year | Title | Journal | Description |
---|---|---|---|---|---|
Hansen, B.G., Kliebenstein, D.J., Halkier, B.A. & Ave, O.S. |
2007 |
Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis |
Plant Journal |
||
Li, J., Hansen, B.G., Ober, J.A., Kliebenstein, D.J. & Halkier, B.A. |
2008 |
Subclade of flavin-monooxygenases involved in aliphatic glucosinolate biosynthesis |
Plant Physiology |
||
Li, J., Kristiansen, K.A., Hansen, B.G. & Halkier, B.A. |
2011 |
Cellular and subcellular localization of flavin- monooxygenases involved in glucosinolate biosynthesis |
Journal of Experimental Botany |