Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inositol oxygenase 1

Gene

MIOX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.2 Publications

Catalytic activityi

Myo-inositol + O2 = D-glucuronate + H2O.

Cofactori

Fe cationBy similarityNote: Binds 2 iron ions per subunit.By similarity

Pathway:imyo-inositol degradation into D-glucuronate

This protein is involved in step 1 of the subpathway that synthesizes D-glucuronate from myo-inositol.
Proteins known to be involved in this subpathway in this organism are:
  1. Inositol oxygenase 2 (MIOX2), Inositol oxygenase 4 (MIOX4), Inositol oxygenase 1 (MIOX1), Inositol oxygenase 5 (MIOX5)
This subpathway is part of the pathway myo-inositol degradation into D-glucuronate, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glucuronate from myo-inositol, the pathway myo-inositol degradation into D-glucuronate and in Polyol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521SubstrateBy similarity
Metal bindingi122 – 1221Iron 1By similarity
Metal bindingi147 – 1471Iron 1By similarity
Metal bindingi148 – 1481Iron 1By similarity
Metal bindingi148 – 1481Iron 2By similarity
Binding sitei151 – 1511SubstrateBy similarity
Metal bindingi220 – 2201Iron 2By similarity
Metal bindingi246 – 2461Iron 2By similarity
Metal bindingi279 – 2791Iron 1By similarity

GO - Molecular functioni

  • inositol oxygenase activity Source: TAIR
  • iron ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:GQT-1164-MONOMER.
MetaCyc:AT1G14520-MONOMER.
BRENDAi1.13.99.1. 399.
UniPathwayiUPA00111; UER00527.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol oxygenase 1 (EC:1.13.99.1)
Alternative name(s):
Myo-inositol oxygenase 1
Short name:
AtMIOX1
Short name:
MI oxygenase 1
Gene namesi
Name:MIOX1
Ordered Locus Names:At1g14520
ORF Names:F14L17.30, T5E21.2, T5E21_19
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G14520.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Inositol oxygenase 1PRO_0000079154Add
BLAST

Proteomic databases

PaxDbiQ8L799.
PRIDEiQ8L799.

Expressioni

Tissue specificityi

Expressed in roots, young leaves, stems, flowers and siliques.1 Publication

Gene expression databases

ExpressionAtlasiQ8L799. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G14520.1.

Structurei

3D structure databases

ProteinModelPortaliQ8L799.
SMRiQ8L799. Positions 68-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1113Substrate bindingBy similarity
Regioni168 – 1692Substrate bindingBy similarity
Regioni246 – 2472Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the myo-inositol oxygenase family.Curated

Phylogenomic databases

eggNOGiNOG135479.
HOGENOMiHOG000163182.
InParanoidiQ8L799.
OMAiNFYREQH.
PhylomeDBiQ8L799.

Family and domain databases

InterProiIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8L799-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTILIDRHSD QNDAGDEIVE KNQGNGKEEE TELVLDAGFE APHTNSFGRT
60 70 80 90 100
FRDYDAESER RRGVEEFYRV NHIGQTVDFV RKMREEYEKL NRTEMSIWEC
110 120 130 140 150
CELLNEFIDE SDPDLDEPQI EHLLQTAEAI RKDYPDEDWL HLTGLIHDLG
160 170 180 190 200
KVLLHSSFGE LPQWAVVGDT FPVGCAFDES IVHHKYFKEN PDYDNPSYNS
210 220 230 240 250
KYGIYTEGCG LDNVLMSWGH DDYMYLVAKE NQTTLPSAGL FIIRYHSFYA
260 270 280 290 300
LHKSEAYKHL MNNEDRENMK WLKVFNKYDL YSKSKVRVNV EEVKPYYLSL
310
TNKYFPSKLK W
Length:311
Mass (Da):36,574
Last modified:October 1, 2002 - v1
Checksum:i0BCBDE175D505F59
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111S → G in BAC42925 (PubMed:11910074).Curated
Sequence conflicti111 – 1111S → G in BAD43581 (Ref. 6) Curated
Sequence conflicti111 – 1111S → G in BAD43596 (Ref. 6) Curated
Sequence conflicti111 – 1111S → G in BAD94364 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010657 Genomic DNA. Translation: AAF63180.1. Sequence problems.
AC012188 Genomic DNA. Translation: AAF43953.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29174.1.
AY136388 mRNA. Translation: AAM97054.1.
BT000187 mRNA. Translation: AAN15506.1.
AK118307 mRNA. Translation: BAC42925.1.
AK175115 mRNA. Translation: BAD42878.1.
AK175818 mRNA. Translation: BAD43581.1.
AK175833 mRNA. Translation: BAD43596.1.
AK176690 mRNA. Translation: BAD44453.1.
AK221931 mRNA. Translation: BAD94364.1.
RefSeqiNP_172904.2. NM_101319.3. [Q8L799-1]
UniGeneiAt.23143.

Genome annotation databases

EnsemblPlantsiAT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
GeneIDi838014.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010657 Genomic DNA. Translation: AAF63180.1. Sequence problems.
AC012188 Genomic DNA. Translation: AAF43953.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29174.1.
AY136388 mRNA. Translation: AAM97054.1.
BT000187 mRNA. Translation: AAN15506.1.
AK118307 mRNA. Translation: BAC42925.1.
AK175115 mRNA. Translation: BAD42878.1.
AK175818 mRNA. Translation: BAD43581.1.
AK175833 mRNA. Translation: BAD43596.1.
AK176690 mRNA. Translation: BAD44453.1.
AK221931 mRNA. Translation: BAD94364.1.
RefSeqiNP_172904.2. NM_101319.3. [Q8L799-1]
UniGeneiAt.23143.

3D structure databases

ProteinModelPortaliQ8L799.
SMRiQ8L799. Positions 68-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G14520.1.

Proteomic databases

PaxDbiQ8L799.
PRIDEiQ8L799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
GeneIDi838014.

Organism-specific databases

TAIRiAT1G14520.

Phylogenomic databases

eggNOGiNOG135479.
HOGENOMiHOG000163182.
InParanoidiQ8L799.
OMAiNFYREQH.
PhylomeDBiQ8L799.

Enzyme and pathway databases

UniPathwayiUPA00111; UER00527.
BioCyciARA:GQT-1164-MONOMER.
MetaCyc:AT1G14520-MONOMER.
BRENDAi1.13.99.1. 399.

Miscellaneous databases

PROiQ8L799.

Gene expression databases

ExpressionAtlasiQ8L799. baseline and differential.

Family and domain databases

InterProiIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "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.

Entry informationi

Entry nameiMIOX1_ARATH
AccessioniPrimary (citable) accession number: Q8L799
Secondary accession number(s): Q8GXC4, Q9M9R1, Q9MA30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2002
Last modified: July 22, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.