Reviewed, UniProtKB/Swiss-Prot Q9FJU4 (MIOX5_ARATH)

Names and origin

Protein names

Recommended name:
    Inositol oxygenase 5
    EC=1.13.99.1
Alternative name(s):
    Myo-inositol oxygenase 5
      Short name=MI oxygenase 5
      Short name=AtMIOX5

Gene names

Name:	MIOX5
Ordered Locus Names:	At5g56640
ORF Names:	MIK19.9

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.4
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. 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
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	inositol oxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	Inositol oxygenase 5		PRO_0000079157
Sites
	Metal binding	125	1	Iron 1 By similarity
	Metal binding	150	1	Iron 1 By similarity
	Metal binding	151	1	Iron 1 By similarity
	Metal binding	151	1	Iron 2 By similarity
	Metal binding	223	1	Iron 2 By similarity
	Metal binding	249	1	Iron 2 By similarity
	Metal binding	282	1	Iron 1 By similarity
Experimental info
	Sequence conflict	107	1	S → L in AAM61190. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9FJU4-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: ABCF484CC1CDA23C	FASTA	314	36,544
	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

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]	"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." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed: 9734815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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].
[4]	"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
EMBLGenBankDDBJ	AB013392 Genomic DNA. Translation: BAB09882.1. AY084627 mRNA. Translation: AAM61190.1.
IPI	IPI00532202.
RefSeq	NP_200475.1.
UniGene	At.29372
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FJU4.
Proteomic databases
PRIDE	Q9FJU4.
Genome annotation databases
GeneID	835765.
GenomeReviews	Gene locus AT5G56640 in contig BA000015_GR.
KEGG	ath:AT5G56640.
NMPDR	fig|3702.1.peg.27604.
Organism-specific databases
TAIR	At5g56640.
Phylogenomic databases
OMA	DESAFDS.
Enzyme and pathway databases
BRENDA	1.13.99.1. 302.
Gene expression databases
Genevestigator	Q9FJU4.
GermOnline	AT5G56640. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR007828. DUF706. [Graphical view]
PANTHER	PTHR12588. DUF706. 1 hit.
Pfam	PF05153. DUF706. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MIOX5_ARATH

Accession

Primary (citable) accession number: Q9FJU4
Secondary accession number(s): Q8LFV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)