O82200 (MIOX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol oxygenase 2
EC=1.13.99.1

Alternative name(s):
Myo-inositol oxygenase 2
Short name=AtMIOX2
Short name=MI oxygenase 2

Gene names

Name:	MIOX2
Ordered Locus Names:	At2g19800
ORF Names:	F6F22.17

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis. Ref.1 Ref.6
Catalytic activity	Myo-inositol + O2 = D-glucuronate + H2O.
Cofactor	Binds 2 iron ions per subunit By similarity.
Pathway	Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular location	Cytoplasm Probable.
Tissue specificity	Expressed mainly in roots, stems, flowers and siliques. Low expression in leaves. Ref.1
Sequence similarities	Belongs to the myo-inositol oxygenase family.

Ontologies

Keywords
Biological process	Ascorbate biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW inositol catabolic process Inferred from electronic annotation. Source: InterPro syncytium formation Inferred from genetic interaction. Source: TAIR
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	inositol oxygenase activity Inferred from mutant phenotype Ref.1. Source: TAIR iron ion 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 – 317	317	Inositol oxygenase 2		PRO_0000079155
Regions
	Region	115 – 117	3	Substrate binding By similarity
	Region	174 – 175	2	Substrate binding By similarity
	Region	252 – 253	2	Substrate binding By similarity
Sites
	Metal binding	128	1	Iron 1 By similarity
	Metal binding	153	1	Iron 1 By similarity
	Metal binding	154	1	Iron 1 By similarity
	Metal binding	154	1	Iron 2 By similarity
	Metal binding	226	1	Iron 2 By similarity
	Metal binding	252	1	Iron 2 By similarity
	Metal binding	285	1	Iron 1 By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	157	1	Substrate By similarity
Experimental info
	Sequence conflict	62	1	G → D in AAM63498. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O82200 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: 857EF7C180F00662	FASTA	317	37,048
	10 20 30 40 50 60 MTILVEHFVP DSRVDEKKVI EERDNELVLD GGFVVPKSKE TDAFDAPDMN FLGHSFRDYE 70 80 90 100 110 120 NGESERQQGV EEFYRMQHIH QTYDFVKKMR KEYGKLNKME MSIWECCELL NNVVDESDPD 130 140 150 160 170 180 LDEPQIQHLL QTAEAIRRDY PDEDWLHLTA LIHDLGKVLL LPEFGGLPQW AVVGDTFPVG 190 200 210 220 230 240 CTFDSANIHH KYFKGNHDIN NPKYNTKNGV YTEGCGLDNV LMSWGHDDYM YLVAKKNGTT 250 260 270 280 290 300 LPHAGLFIIR YHSFYPLHKA GAYTHLMNDE DRDDLKWLHV FNKYDLYSKS KVLVDVEQVK 310 PYYISLINKY FPAKLKW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The inositol oxygenase gene family of Arabidopsis is involved in the biosynthesis of nucleotide sugar precursors for cell-wall matrix polysaccharides." Kanter U., Usadel B., Guerineau F., Li Y., Pauly M., Tenhaken R. Planta 221:243-254(2005) [PubMed: 15660207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-317. Strain: cv. Columbia.
[6]	"Myo-inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis." Lorence A., Chevone B.I., Mendes P., Nessler C.L. Plant Physiol. 134:1200-1205(2004) [PubMed: 14976233] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC005169 Genomic DNA. Translation: AAC62136.2. CP002685 Genomic DNA. Translation: AEC06927.1. AY086497 mRNA. Translation: AAM63498.1. AF370587 mRNA. Translation: AAK43906.1.
IPI	IPI00517564.
PIR	C84581.
RefSeq	NP_565459.1. NM_127538.3.
UniGene	At.12894.
3D structure databases
ProteinModelPortal	O82200.
SMR	O82200. Positions 56-317.
ModBase	Search...
Protein-protein interaction databases
STRING	O82200.
Proteomic databases
PRIDE	O82200.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G19800.1; AT2G19800.1; AT2G19800.
GeneID	816499.
GenomeReviews	Gene locus AT2G19800 in contig CT485783_GR.
KEGG	ath:AT2G19800.
NMPDR	fig|3702.1.peg.8974.
Organism-specific databases
TAIR	At2g19800.
Phylogenomic databases
GeneTree	EPGT00050000000001.
HOGENOM	HBG332059.
InParanoid	O82200.
OMA	VMEAVDM.
PhylomeDB	O82200.
ProtClustDB	CLSN2687348.
Gene expression databases
ArrayExpress	O82200.
Genevestigator	O82200.
GermOnline	AT2G19800. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR007828. Inositol_oxygenase. [Graphical view]
KO	K00469.
PANTHER	PTHR12588. DUF706. 1 hit.
Pfam	PF05153. DUF706. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MIOX2_ARATH

Accession

Primary (citable) accession number: O82200
Secondary accession number(s): Q8LCN3, Q94JX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	June 1, 2002
Last modified:	November 16, 2011
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program