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Protein

Inositol oxygenase

Gene

Miox

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Fe cation2 PublicationsNote: Binds 2 iron ions per subunit.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Substrate
Metal bindingi98 – 981Iron 12 Publications
Metal bindingi123 – 1231Iron 12 Publications
Metal bindingi124 – 1241Iron 12 Publications
Metal bindingi124 – 1241Iron 22 Publications
Binding sitei127 – 1271Substrate
Metal bindingi194 – 1941Iron 22 Publications
Metal bindingi220 – 2201Iron 22 Publications
Metal bindingi253 – 2531Iron 12 Publications

GO - Molecular functioni

  1. aldo-keto reductase (NADP) activity Source: UniProtKB
  2. ferric iron binding Source: UniProtKB
  3. inositol oxygenase activity Source: UniProtKB
  4. NADP binding Source: Ensembl
  5. oxidoreductase activity Source: MGI
  6. oxidoreductase activity, acting on NAD(P)H Source: UniProtKB
  7. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen Source: UniProtKB

GO - Biological processi

  1. inositol catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.99.1. 3474.
SABIO-RKQ9QXN5.
UniPathwayiUPA00111; UER00527.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Miox
Synonyms:Aldrl6, Rsor
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1891725. Miox.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: MGI
  3. inclusion body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Inositol oxygenasePRO_0000079149Add
BLAST

Proteomic databases

MaxQBiQ9QXN5.
PaxDbiQ9QXN5.
PRIDEiQ9QXN5.

2D gel databases

REPRODUCTION-2DPAGEQ9QXN5.

PTM databases

PhosphoSiteiQ9QXN5.

Expressioni

Tissue specificityi

Kidney specific. Renal proximal tubules.1 Publication

Gene expression databases

BgeeiQ9QXN5.
CleanExiMM_MIOX.
ExpressionAtlasiQ9QXN5. baseline.
GenevestigatoriQ9QXN5.

Interactioni

Protein-protein interaction databases

IntActiQ9QXN5. 1 interaction.
MINTiMINT-4102022.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Helixi37 – 5014Combined sources
Helixi53 – 6311Combined sources
Helixi73 – 797Combined sources
Helixi80 – 823Combined sources
Helixi95 – 10915Combined sources
Helixi114 – 1229Combined sources
Helixi125 – 1328Combined sources
Helixi136 – 1383Combined sources
Beta strandi145 – 1484Combined sources
Turni155 – 1595Combined sources
Helixi165 – 1684Combined sources
Turni170 – 1723Combined sources
Beta strandi173 – 1764Combined sources
Helixi185 – 1873Combined sources
Helixi194 – 20411Combined sources
Helixi211 – 2199Combined sources
Helixi223 – 2264Combined sources
Turni232 – 2343Combined sources
Helixi237 – 25519Combined sources
Helixi264 – 27815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUOX-ray2.00A1-285[»]
3BXDX-ray2.00A1-285[»]
ProteinModelPortaliQ9QXN5.
SMRiQ9QXN5. Positions 28-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QXN5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 884Substrate binding
Regioni141 – 1422Substrate binding
Regioni220 – 2212Substrate binding

Sequence similaritiesi

Belongs to the myo-inositol oxygenase family.Curated

Phylogenomic databases

eggNOGiNOG135479.
GeneTreeiENSGT00390000016211.
HOGENOMiHOG000163182.
HOVERGENiHBG039556.
InParanoidiQ9QXN5.
KOiK00469.
OMAiPEAFYMI.
OrthoDBiEOG7DZ8KD.
PhylomeDBiQ9QXN5.
TreeFamiTF300089.

Family and domain databases

InterProiIPR018170. Aldo/ket_reductase_CS.
IPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 1 hit.
[Graphical view]
PROSITEiPS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVDVGPDPS LVYRPDVDPE MAKSKDSFRN YTSGPLLDRV FTTYKLMHTH
60 70 80 90 100
QTVDFVSRKR IQYGSFSYKK MTIMEAVGML DDLVDESDPD VDFPNSFHAF
110 120 130 140 150
QTAEGIRKAH PDKDWFHLVG LLHDLGKIMA LWGEPQWAVV GDTFPVGCRP
160 170 180 190 200
QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLENVLM SWGHDEYLYQ
210 220 230 240 250
MMKFNKFSLP SEAFYMIRFH SFYPWHTGGD YRQLCSQQDL DMLPWVQEFN
260 270 280
KFDLYTKCPD LPDVESLRPY YQGLIDKYCP GTLSW
Length:285
Mass (Da):33,164
Last modified:November 8, 2005 - v2
Checksum:iC6877BFF2B60D1A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651S → G in AAF25202 (PubMed:10944187).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF197127 mRNA. Translation: AAF25202.1.
AY738257 mRNA. Translation: AAV65815.1.
BC013543 mRNA. Translation: AAH13543.1.
CCDSiCCDS27745.1.
RefSeqiNP_064361.2. NM_019977.2.
UniGeneiMm.158200.

Genome annotation databases

EnsembliENSMUST00000023282; ENSMUSP00000023282; ENSMUSG00000022613.
GeneIDi56727.
KEGGimmu:56727.
UCSCiuc007xgc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF197127 mRNA. Translation: AAF25202.1.
AY738257 mRNA. Translation: AAV65815.1.
BC013543 mRNA. Translation: AAH13543.1.
CCDSiCCDS27745.1.
RefSeqiNP_064361.2. NM_019977.2.
UniGeneiMm.158200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUOX-ray2.00A1-285[»]
3BXDX-ray2.00A1-285[»]
ProteinModelPortaliQ9QXN5.
SMRiQ9QXN5. Positions 28-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QXN5. 1 interaction.
MINTiMINT-4102022.

PTM databases

PhosphoSiteiQ9QXN5.

2D gel databases

REPRODUCTION-2DPAGEQ9QXN5.

Proteomic databases

MaxQBiQ9QXN5.
PaxDbiQ9QXN5.
PRIDEiQ9QXN5.

Protocols and materials databases

DNASUi56727.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023282; ENSMUSP00000023282; ENSMUSG00000022613.
GeneIDi56727.
KEGGimmu:56727.
UCSCiuc007xgc.1. mouse.

Organism-specific databases

CTDi55586.
MGIiMGI:1891725. Miox.

Phylogenomic databases

eggNOGiNOG135479.
GeneTreeiENSGT00390000016211.
HOGENOMiHOG000163182.
HOVERGENiHBG039556.
InParanoidiQ9QXN5.
KOiK00469.
OMAiPEAFYMI.
OrthoDBiEOG7DZ8KD.
PhylomeDBiQ9QXN5.
TreeFamiTF300089.

Enzyme and pathway databases

UniPathwayiUPA00111; UER00527.
BRENDAi1.13.99.1. 3474.
SABIO-RKQ9QXN5.

Miscellaneous databases

EvolutionaryTraceiQ9QXN5.
NextBioi313210.
PROiQ9QXN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXN5.
CleanExiMM_MIOX.
ExpressionAtlasiQ9QXN5. baseline.
GenevestigatoriQ9QXN5.

Family and domain databases

InterProiIPR018170. Aldo/ket_reductase_CS.
IPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 1 hit.
[Graphical view]
PROSITEiPS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND MYO-INOSITOL, COFACTOR.

Entry informationi

Entry nameiMIOX_MOUSE
AccessioniPrimary (citable) accession number: Q9QXN5
Secondary accession number(s): Q5S8D0, Q91WQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: November 8, 2005
Last modified: February 4, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.