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Q8L799 (MIOX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MIOX1
Ordered Locus Names:At1g14520
ORF Names:F14L17.30, T5E21.2, T5E21_19
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length311 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.7

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 roots, young leaves, stems, flowers and siliques. Ref.1

Sequence similarities

Belongs to the myo-inositol oxygenase family.

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.

Ontologies

Keywords
   Biological processAscorbate biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

inositol catabolic process

Inferred from electronic annotation. Source: InterPro

syncytium formation

Inferred from genetic interaction PubMed 19691674. Source: TAIR

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninositol oxygenase activity

Inferred from mutant phenotype Ref.1. Source: TAIR

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Inositol oxygenase 1
PRO_0000079154

Regions

Region109 – 1113Substrate binding By similarity
Region168 – 1692Substrate binding By similarity
Region246 – 2472Substrate binding By similarity

Sites

Metal binding1221Iron 1 By similarity
Metal binding1471Iron 1 By similarity
Metal binding1481Iron 1 By similarity
Metal binding1481Iron 2 By similarity
Metal binding2201Iron 2 By similarity
Metal binding2461Iron 2 By similarity
Metal binding2791Iron 1 By similarity
Binding site521Substrate By similarity
Binding site1511Substrate By similarity

Experimental info

Sequence conflict1111S → G in BAC42925. Ref.5
Sequence conflict1111S → G in BAD43581. Ref.6
Sequence conflict1111S → G in BAD43596. Ref.6
Sequence conflict1111S → G in BAD94364. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0BCBDE175D505F59

FASTA31136,574
        10         20         30         40         50         60 
MTILIDRHSD QNDAGDEIVE KNQGNGKEEE TELVLDAGFE APHTNSFGRT FRDYDAESER 

        70         80         90        100        110        120 
RRGVEEFYRV NHIGQTVDFV RKMREEYEKL NRTEMSIWEC CELLNEFIDE SDPDLDEPQI 

       130        140        150        160        170        180 
EHLLQTAEAI RKDYPDEDWL HLTGLIHDLG KVLLHSSFGE LPQWAVVGDT FPVGCAFDES 

       190        200        210        220        230        240 
IVHHKYFKEN PDYDNPSYNS KYGIYTEGCG LDNVLMSWGH DDYMYLVAKE NQTTLPSAGL 

       250        260        270        280        290        300 
FIIRYHSFYA LHKSEAYKHL MNNEDRENMK WLKVFNKYDL YSKSKVRVNV EEVKPYYLSL 

       310 
TNKYFPSKLK W 

« 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 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. expand/collapse author list , 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. 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].
Strain: cv. Columbia.
[5]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_172904.2. NM_101319.3. [Q8L799-1]
UniGeneAt.23143.

3D structure databases

ProteinModelPortalQ8L799.
SMRQ8L799. Positions 68-311.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ8L799.
PRIDEQ8L799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
GeneID838014.
KEGGath:AT1G14520.

Organism-specific databases

TAIRAT1G14520.

Phylogenomic databases

eggNOGNOG135479.
HOGENOMHOG000163182.
InParanoidQ8L799.
KOK00469.
OMANFYREQH.
PhylomeDBQ8L799.

Enzyme and pathway databases

BioCycARA:GQT-1164-MONOMER.
MetaCyc:AT1G14520-MONOMER.
UniPathwayUPA00111; UER00527.

Gene expression databases

GenevestigatorQ8L799.

Family and domain databases

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

Entry information

Entry nameMIOX1_ARATH
AccessionPrimary (citable) accession number: Q8L799
Secondary accession number(s): Q8GXC4, Q9M9R1, Q9MA30
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 83 of the entry and version 1 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