[1]	NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION. DOI=10.1007/s00425-004-1441-0; PubMed=15660207 [NCBI, ExPASy, EBI, Israel, Japan] Kanter U., Usadel B., Guerineau F., Li Y., Pauly M., Tenhaken R.; "The inositol oxygenase gene family of Arabidopsis is involved in the biosynthesis of nucleotide sugar precursors for cell-wall matrix polysaccharides."; Planta 221:243-254(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/5.3.203; PubMed=9734815 [NCBI, ExPASy, EBI, Israel, Japan] Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."; DNA Res. 5:203-216(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]	FUNCTION. DOI=10.1104/pp.103.033936; PubMed=14976233 [NCBI, ExPASy, EBI, Israel, Japan] Lorence A., Chevone B.I., Mendes P., Nessler C.L.; "Myo-inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis."; Plant Physiol. 134:1200-1205(2004).

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.
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 in flowers and siliques.
SIMILARITY: Belongs to the myo-inositol oxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB013392; BAB09882.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084627; AAM61190.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_200475.1; -.

UniGene

At.29372

3D structure databases

ModBase

Q9FJU4.

Organism-specific databases

TAIR

At5g56640; -.

Gene expression databases

GermOnline

AT5G56640; Arabidopsis thaliana.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0019853;	Biological process: L-ascorbic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007828; DUF706.
Graphical view of domain structure.

PANTHER

PTHR12588; DUF706; 1.

Pfam

PF05153; DUF706; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

835765; -.

GenomeReviews

BA000015_GR; AT5G56640.

KEGG

ath:AT5G56640; -.

NMPDR

fig|3702.1.peg.27604; -.

Other

LinkHub

Q9FJU4; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Ascorbate biosynthesis; Complete proteome; Cytoplasm; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 314`	`314`	`Inositol oxygenase 5.`	`PRO_0000079157`
`METAL`	`125 125`		`Iron 1 (By similarity).`
`METAL`	`150 150`		`Iron 1 (By similarity).`
`METAL`	`151 151`		`Iron 1 (By similarity).`
`METAL`	`151 151`		`Iron 2 (By similarity).`
`METAL`	`223 223`		`Iron 2 (By similarity).`
`METAL`	`249 249`		`Iron 2 (By similarity).`
`METAL`	`282 282`		`Iron 1 (By similarity).`
`CONFLICT`	`107 107`		`S -> L (in Ref. 3; AAM61190).`

Sequence information

Length: 314 AA [This is the length of the unprocessed precursor]

Molecular weight: 36544 Da [This is the MW of the unprocessed precursor]

CRC64: ABCF484CC1CDA23C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNISVENPVF VHEDSTTQKT GELRLDSDIP MSKISSDDEV FLAPEMNAFG RQFRDYTDTN 

        70         80         90        100        110        120 
SERQKSVEHF YATQHTNQTL DFVQKMRSEY GKLDKMVMNI WECCELSKEV VDESDPDLDE 

       130        140        150        160        170        180 
PQIQHLLQSA EAIRKDYPNE DWLHLTALIH DLGKVLTLPQ FGGLPQWAVV GDTFPVGCAF 

       190        200        210        220        230        240 
DESNVHHKYF MENPDFNNPK YNTKAGIYSE GCGLENVLMS WGHDDYMYLV AKENGSTLPS 

       250        260        270        280        290        300 
PGLFIIRYHS FYPLHKAGAY THLMNEEDKE NLKWLHVFNK YDLYSKSKVH VNVEKVKPYY 

       310 
MSLIKKYFPE NLRW

Q9FJU4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools