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O82200 (MIOX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Inositol oxygenase 2
PRO_0000079155

Regions

Region115 – 1173Substrate binding By similarity
Region174 – 1752Substrate binding By similarity
Region252 – 2532Substrate binding By similarity

Sites

Metal binding1281Iron 1 By similarity
Metal binding1531Iron 1 By similarity
Metal binding1541Iron 1 By similarity
Metal binding1541Iron 2 By similarity
Metal binding2261Iron 2 By similarity
Metal binding2521Iron 2 By similarity
Metal binding2851Iron 1 By similarity
Binding site571Substrate By similarity
Binding site1571Substrate By similarity

Experimental info

Sequence conflict621G → D in AAM63498. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O82200 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: 857EF7C180F00662

FASTA31737,048
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] 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] [Europe PMC] [Abstract]
Cited for: FUNCTION.

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.
PIRC84581.
RefSeqNP_565459.1. NM_127538.3.
UniGeneAt.12894.

3D structure databases

ProteinModelPortalO82200.
SMRO82200. Positions 56-317.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbO82200.
PRIDEO82200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G19800.1; AT2G19800.1; AT2G19800.
GeneID816499.
KEGGath:AT2G19800.

Organism-specific databases

TAIRAT2G19800.

Phylogenomic databases

eggNOGNOG135479.
HOGENOMHOG000163182.
InParanoidO82200.
KOK00469.
OMACQFSDKI.
PhylomeDBO82200.
ProtClustDBCLSN2687348.

Enzyme and pathway databases

UniPathwayUPA00111; UER00527.

Gene expression databases

ArrayExpressO82200.
GenevestigatorO82200.

Family and domain databases

InterProIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERPTHR12588. PTHR12588. 1 hit.
PfamPF05153. DUF706. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMIOX2_ARATH
AccessionPrimary (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: February 19, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names