SuCComBase

SCC Gene Description

Gene name	FMOGS-OX2
AGI ID	AT1G62540
Gene length	457
Uniprot ID	Q94K43
Protein Name	Flavin-containing monooxygenase FMO GS-OX2
Synonym	T3P18.10
EC number	EC 1.8.-.-
Entrez Gene	88716
Refseq mrna	NM_104933
Refseq protein	NP_564796
Function	Four uncharacterized FMOs designated FMOGS-OX2 to FMOGS-OX5 were found to involve in biosynthesis aliphatic GSL. Biochemical characterization of the recombinant protein combined with the analysis of GSL content in knockout mutants and overexpression lines show that FMOGS-OX2; FMOGS-OX3; and FMOGS-OX4 have broad substrate specificity and catalyze the conversion from methylthioalkyl GSL to the corresponding methylsulfinylalkyl GSL independent of chain length. In contrast; FMOGS-OX5 shows substrate specificity toward the long-chain 8-methylthiooctyl GSL. Identification of the FMOGS-OX subclade will generate better understanding of the evolution of biosynthetic activities and specificities in secondary metabolism and provides an important tool for breeding plants with improved cancer prevention characteristics as provided by the methylsulfinylalkyl GSL (Li et al. 2008)
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
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	82	0.00E+00
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	66	0.00E+00
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	69	0.00E+00
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	70	0.00E+00
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	68	0.00E+00
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	64	0.00E+00
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	64	0.00E+00
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	63	0.00E+00
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	63	0.00E+00
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	60	0.00E+00
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	60	0.00E+00
Papaya	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	62	0.00E+00
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	46	2.00E-124
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	45	5.00E-123
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	45	1.00E-121
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	46	8.00E-121
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	45	3.00E-119
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	46	2.00E-118
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	43	5.00E-111
Papaya	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	40	4.00E-97
Cabbage	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	48	1.00E-91
Broccoli	AT1G62540	FMOGS-OX2	Flavin-containing monooxygenase FMO GS-OX2	44	4.00E-72

GO ID	Ontology	GO Term	Description
GO:0004497	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.
GO:0004499	MF	N,N-dimethylaniline monooxygenase activity	Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
GO:0005634	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
GO:0019761	BP	glucosinolate biosynthetic process	The chemical reactions and pathways resulting in the formation of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
GO:0050660	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.
GO:0050661	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.
GO:0055114	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.
GO:0080102	MF	3-methylthiopropyl glucosinolate S-oxygenase activity	Catalysis of the reaction: 3-methylthiopropyl-glucosinolate = 3-methylsulfinylpropyl-glucosinolate.
GO:0080103	MF	4-methylthiopropyl glucosinolate S-oxygenase activity	Catalysis of the reaction: 4-methylthiopropyl-glucosinolate = 4-methylsulfinylpropyl-glucosinolate.
GO:0080104	MF	5-methylthiopropyl glucosinolate S-oxygenase activity	Catalysis of the reaction: 5-methylthiopropyl-glucosinolate = 5-methylsulfinylpropyl-glucosinolate.
GO:0080106	MF	7-methylthiopropyl glucosinolate S-oxygenase activity	Catalysis of the reaction: 7-methylthiopropyl-glucosinolate = 7-methylsulfinylpropyl-glucosinolate.
GO:0080107	MF	8-methylthiopropyl glucosinolate S-oxygenase activity	Catalysis of the reaction: 8-methylthiopropyl-glucosinolate = 8-methylsulfinylpropyl-glucosinolate.

Pubmed ID	Authors	Year	Title	Journal
17461789	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
18799661	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
21078824	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