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Q9QXN5 (MIOX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol oxygenase

EC=1.13.99.1
Alternative name(s):
Aldehyde reductase-like 6
Myo-inositol oxygenase
Short name=MI oxygenase
Renal-specific oxidoreductase
Gene names
Name:Miox
Synonyms:Aldrl6, Rsor
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 iron ions per subunit. Ref.4 Ref.5

Pathway

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

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Kidney specific. Renal proximal tubules. Ref.1

Sequence similarities

Belongs to the myo-inositol oxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Inositol oxygenase
PRO_0000079149

Regions

Region85 – 884Substrate binding
Region141 – 1422Substrate binding
Region220 – 2212Substrate binding

Sites

Metal binding981Iron 1
Metal binding1231Iron 1
Metal binding1241Iron 1
Metal binding1241Iron 2
Metal binding1941Iron 2
Metal binding2201Iron 2
Metal binding2531Iron 1
Binding site291Substrate
Binding site1271Substrate

Experimental info

Sequence conflict651S → G in AAF25202. Ref.1

Secondary structure

......................................... 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QXN5 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: C6877BFF2B60D1A7

FASTA28533,164
        10         20         30         40         50         60 
MKVDVGPDPS LVYRPDVDPE MAKSKDSFRN YTSGPLLDRV FTTYKLMHTH QTVDFVSRKR 

        70         80         90        100        110        120 
IQYGSFSYKK MTIMEAVGML DDLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG 

       130        140        150        160        170        180 
LLHDLGKIMA LWGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ 

       190        200        210        220        230        240 
PHCGLENVLM SWGHDEYLYQ MMKFNKFSLP SEAFYMIRFH SFYPWHTGGD YRQLCSQQDL 

       250        260        270        280 
DMLPWVQEFN KFDLYTKCPD LPDVESLRPY YQGLIDKYCP GTLSW 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a renal-specific oxido-reductase in newborn diabetic mice."
Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K., Kanwar Y.S.
Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Molecular cloning, expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney."
Arner R.J., Prabhu K.S., Reddy C.C.
Biochem. Biophys. Res. Commun. 324:1386-1392(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism."
Brown P.M., Caradoc-Davies T.T., Dickson J.M., Cooper G.J., Loomes K.M., Baker E.N.
Proc. Natl. Acad. Sci. U.S.A. 103:15032-15037(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND MYO-INOSITOL, COFACTOR.
[5]"Structural and biophysical characterization of human myo-inositol oxygenase."
Thorsell A.G., Persson C., Voevodskaya N., Busam R.D., Hammarstrom M., Graslund S., Graslund A., Hallberg B.M.
J. Biol. Chem. 283:15209-15216(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND MYO-INOSITOL, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF197127 mRNA. Translation: AAF25202.1.
AY738257 mRNA. Translation: AAV65815.1.
BC013543 mRNA. Translation: AAH13543.1.
RefSeqNP_064361.2. NM_019977.2.
UniGeneMm.158200.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUOX-ray2.00A1-285[»]
3BXDX-ray2.00A1-285[»]
ProteinModelPortalQ9QXN5.
SMRQ9QXN5. Positions 28-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QXN5. 1 interaction.
MINTMINT-4102022.

PTM databases

PhosphoSiteQ9QXN5.

2D gel databases

REPRODUCTION-2DPAGEQ9QXN5.

Proteomic databases

PaxDbQ9QXN5.
PRIDEQ9QXN5.

Protocols and materials databases

DNASU56727.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023282; ENSMUSP00000023282; ENSMUSG00000022613.
GeneID56727.
KEGGmmu:56727.
UCSCuc007xgc.1. mouse.

Organism-specific databases

CTD55586.
MGIMGI:1891725. Miox.

Phylogenomic databases

eggNOGNOG135479.
GeneTreeENSGT00390000016211.
HOGENOMHOG000163182.
HOVERGENHBG039556.
InParanoidQ9QXN5.
KOK00469.
OMANFYREQH.
OrthoDBEOG7DZ8KD.
PhylomeDBQ9QXN5.
TreeFamTF300089.

Enzyme and pathway databases

BRENDA1.13.99.1. 3474.
SABIO-RKQ9QXN5.
UniPathwayUPA00111; UER00527.

Gene expression databases

BgeeQ9QXN5.
CleanExMM_MIOX.
GenevestigatorQ9QXN5.

Family and domain databases

InterProIPR018170. Aldo/ket_reductase_CS.
IPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERPTHR12588. PTHR12588. 1 hit.
PfamPF05153. DUF706. 1 hit.
[Graphical view]
PROSITEPS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9QXN5.
NextBio313210.
PROQ9QXN5.
SOURCESearch...

Entry information

Entry nameMIOX_MOUSE
AccessionPrimary (citable) accession number: Q9QXN5
Secondary accession number(s): Q5S8D0, Q91WQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot