Q9SS04 (GSOX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Flavin-containing monooxygenase FMO GS-OX1
EC=1.8.-.-

Alternative name(s):
Flavin-monooxygenase glucosinolate S-oxygenase 1
Putative flavin-containing monooxygenase 3

Gene names

Name:	FMOGS-OX1
Synonyms:	FMO3
Ordered Locus Names:	At1g65860
ORF Names:	F12P19.2

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the conversion of methylthioalkyl glucosinolates into methylsulfinylalkyl glucosinolates. Able to S-oxygenate both desulfo- and intact 4-methylthiobutyl glucosinolates, but no activity with methionine, dihomomethionine or 5-methylthiopentaldoxime. Ref.4
Cofactor	FAD By similarity.
Tissue specificity	Mainly expressed in leaves. Low levels in flowers and seeds. Ref.4
Disruption phenotype	Increased accumulation of methylthiobutyl, -pentyl and -heptyl glucosinolates in leaves. No effects in seeds. Ref.4
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucosinolate biosynthetic process from homomethionine Inferred from mutant phenotype Ref.4. Source: TAIR
Molecular_function	3-methylthiopropyl glucosinolate S-oxygenase activity Inferred from mutant phenotype Ref.4. Source: TAIR 4-methylthiopropyl glucosinolate S-oxygenase activity Inferred from direct assay Ref.4. Source: TAIR 5-methylthiopropyl glucosinolate S-oxygenase activity Inferred from mutant phenotype Ref.4. Source: TAIR 6-methylthiopropyl glucosinolate S-oxygenase activity Inferred from mutant phenotype Ref.4. Source: TAIR 7-methylthiopropyl glucosinolate S-oxygenase activity Inferred from mutant phenotype Ref.4. Source: TAIR 8-methylthiopropyl glucosinolate S-oxygenase activity Inferred from direct assay Ref.4. Source: TAIR N,N-dimethylaniline monooxygenase activity Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 459	459	Flavin-containing monooxygenase FMO GS-OX1		PRO_0000360991
Regions
	Nucleotide binding	17 – 22	6	FAD Potential
	Nucleotide binding	211 – 216	6	NADP Potential
	Compositional bias	206 – 209	4	Poly-Val
	Compositional bias	431 – 434	4	Poly-Asp

Sequences

	Sequence		Length	Mass (Da)
	Q9SS04 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D5115E9CDEA57E0C	FASTA	459	52,309
	10 20 30 40 50 60 MAPTQNTICS KHVAVIGAGA AGLVTARELR REGHTVVVFD REKQVGGLWN YSSKADSDPL 70 80 90 100 110 120 SLDTTRTIVH TSIYESLRTN LPRECMGFTD FPFVPRIHDI SRDSRRYPSH REVLAYLQDF 130 140 150 160 170 180 AREFKIEEMV RFETEVVCVE PVNGKWSVRS KNSVGFAAHE IFDAVVVCSG HFTEPNVAHI 190 200 210 220 230 240 PGIKSWPGKQ IHSHNYRVPG PFNNEVVVVI GNYASGADIS RDIAKVAKEV HIASRASESD 250 260 270 280 290 300 TYQKLPVPQN NLWVHSEIDF AHQDGSILFK NGKVVYADTI VHCTGYKYYF PFLETNGYIN 310 320 330 340 350 360 INENRVEPLY KHVFLPALAP SLSFIGLPGM AIQFVMFEIQ SKWVAAVLSG RVILPSQDKM 370 380 390 400 410 420 MEDIIEWYAT LDVLGIPKRH THKLGKISCE YLNWIAEECH CSPVENWRIQ EVERGFQRMV 430 440 450 SHPEIYRDEW DDDDLMEEAY KDFARKKLIS SHPSYFLES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis." Hansen B.G., Kliebenstein D.J., Halkier B.A. Plant J. 50:902-910(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, GENE FAMILY. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC009513 Genomic DNA. Translation: AAF06046.1. CP002684 Genomic DNA. Translation: AEE34434.1. BT000473 mRNA. Translation: AAN17450.1. BT002190 mRNA. Translation: AAN72201.1.
IPI	IPI00536385.
PIR	F96682.
RefSeq	NP_176761.1. NM_105258.2.
UniGene	At.35830.
3D structure databases
ProteinModelPortal	Q9SS04.
SMR	Q9SS04. Positions 10-362.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G65860.1-P.
Proteomic databases
PaxDb	Q9SS04.
PRIDE	Q9SS04.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G65860.1; AT1G65860.1; AT1G65860.
GeneID	842897.
KEGG	ath:AT1G65860.
Organism-specific databases
TAIR	At1g65860.
Phylogenomic databases
eggNOG	COG2072.
HOGENOM	HOG000237857.
InParanoid	Q9SS04.
OMA	NINENRV.
PhylomeDB	Q9SS04.
ProtClustDB	PLN02172.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G65860-MONOMER.
Gene expression databases
Genevestigator	Q9SS04.
Family and domain databases
InterPro	IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. [Graphical view]
Pfam	PF00743. FMO-like. 2 hits. [Graphical view]
PRINTS	PR00370. FMOXYGENASE.
ProtoNet	Search...

Entry information

Entry name

GSOX1_ARATH

Accession

Primary (citable) accession number: Q9SS04

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program