Q8L799 · MIOX1_ARATH

Function

function

Catalyzes the oxygenative cleavage of myo-inositol to D-glucuronate. 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

Cofactor

Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Note: Binds 2 iron ions per subunit.

Pathway

Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site52substrate
Binding site109-111substrate
Binding site122Fe cation 1 (UniProtKB | ChEBI)
Binding site147Fe cation 1 (UniProtKB | ChEBI)
Binding site148Fe cation 1 (UniProtKB | ChEBI)
Binding site148Fe cation 2 (UniProtKB | ChEBI)
Binding site151substrate
Binding site168-169substrate
Binding site220Fe cation 2 (UniProtKB | ChEBI)
Binding site246Fe cation 2 (UniProtKB | ChEBI)
Binding site246-247substrate
Binding site279Fe cation 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioninositol oxygenase activity
Molecular Functioniron ion binding
Biological Processinositol catabolic process
Biological ProcessL-ascorbic acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inositol oxygenase 1
  • EC number
  • Alternative names
    • Myo-inositol oxygenase 1
      (AtMIOX1
      ; MI oxygenase 1)

Gene names

    • Name
      MIOX1
    • ORF names
      F14L17.30, T5E21.2, T5E21_19
    • Ordered locus names
      At1g14520

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8L799
  • Secondary accessions
    • Q8GXC4
    • Q9M9R1
    • Q9MA30

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Incorporation of the inositol pathway-derived monosaccharides is strongly reduced in knockout AtMIOX1 seedling walls.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000791541-311Inositol oxygenase 1

Proteomic databases

Expression

Tissue specificity

Expressed in roots, young leaves, stems, flowers and siliques.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-29Disordered
Compositional bias9-29Basic and acidic residues

Sequence similarities

Belongs to the myo-inositol oxygenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.

Q8L799-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    311
  • Mass (Da)
    36,574
  • Last updated
    2002-10-01 v1
  • Checksum
    0BCBDE175D505F59
MTILIDRHSDQNDAGDEIVEKNQGNGKEEETELVLDAGFEAPHTNSFGRTFRDYDAESERRRGVEEFYRVNHIGQTVDFVRKMREEYEKLNRTEMSIWECCELLNEFIDESDPDLDEPQIEHLLQTAEAIRKDYPDEDWLHLTGLIHDLGKVLLHSSFGELPQWAVVGDTFPVGCAFDESIVHHKYFKENPDYDNPSYNSKYGIYTEGCGLDNVLMSWGHDDYMYLVAKENQTTLPSAGLFIIRYHSFYALHKSEAYKHLMNNEDRENMKWLKVFNKYDLYSKSKVRVNVEEVKPYYLSLTNKYFPSKLKW

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8APC9A0A1P8APC9_ARATHMIOX1341
Q3EDC6Q3EDC6_ARATHAt1g14630226
A0A1P8AWY2A0A1P8AWY2_ARATHAt1g14630166
F4HW72F4HW72_ARATHMIOX1309

Sequence caution

The sequence AAF43953.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence AAF63180.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias9-29Basic and acidic residues
Sequence conflict111in Ref. 5; BAC42925 and 6; BAD43581/BAD43596/BAD94364

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC010657
EMBL· GenBank· DDBJ
AAF63180.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AC012188
EMBL· GenBank· DDBJ
AAF43953.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002684
EMBL· GenBank· DDBJ
AEE29174.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM58508.1
EMBL· GenBank· DDBJ
Genomic DNA
AY136388
EMBL· GenBank· DDBJ
AAM97054.1
EMBL· GenBank· DDBJ
mRNA
BT000187
EMBL· GenBank· DDBJ
AAN15506.1
EMBL· GenBank· DDBJ
mRNA
AK118307
EMBL· GenBank· DDBJ
BAC42925.1
EMBL· GenBank· DDBJ
mRNA
AK175115
EMBL· GenBank· DDBJ
BAD42878.1
EMBL· GenBank· DDBJ
mRNA
AK175818
EMBL· GenBank· DDBJ
BAD43581.1
EMBL· GenBank· DDBJ
mRNA
AK175833
EMBL· GenBank· DDBJ
BAD43596.1
EMBL· GenBank· DDBJ
mRNA
AK176690
EMBL· GenBank· DDBJ
BAD44453.1
EMBL· GenBank· DDBJ
mRNA
AK221931
EMBL· GenBank· DDBJ
BAD94364.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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