[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. TISSUE=Kidney; DOI=10.1073/pnas.160266197; PubMed=10944187 [NCBI, ExPASy, EBI, Israel, Japan] Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K., Kanwar Y.S.; "Identification of a renal-specific oxido-reductase in newborn diabetic mice."; Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6; TISSUE=Kidney; DOI=10.1016/j.bbrc.2004.09.209; PubMed=15504367 [NCBI, ExPASy, EBI, Israel, Japan] Arner R.J., Prabhu K.S., Reddy C.C.; "Molecular cloning, expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney."; Biochem. Biophys. Res. Commun. 324:1386-1392(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1073/pnas.0605143103; PubMed=17012379 [NCBI, ExPASy, EBI, Israel, Japan] Brown P.M., Caradoc-Davies T.T., Dickson J.M., Cooper G.J., Loomes K.M., Baker E.N.; "Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism."; Proc. Natl. Acad. Sci. U.S.A. 103:15032-15037(2006).

Comments

CATALYTIC ACTIVITY: Myo-inositol + O₂ = D-glucuronate + H₂O.
COFACTOR: Binds 2 iron ions per subunit.
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.
SIMILARITY: Belongs to the myo-inositol oxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF197127; AAF25202.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY738257; AAV65815.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013543; AAH13543.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_064361.2; -.

UniGene

Mm.158200

3D structure databases

PDB

2HUO; X-ray; 2.00 A; A=1-285.	[ExPASy / RCSB / EBI]
3BXD; X-ray; 2.00 A; A=1-285.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

2HUO; -.
3BXD; -.

2D gel databases

Q9QXN5; -.

Organism-specific databases

MGI

MGI:1891725; Miox.

Gene expression databases

ArrayExpress

Q9QXN5; -.

CleanEx

MM_MIOX; -.

GermOnline

ENSMUSG00000022613; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0016234;	Cellular component: inclusion body (inferred from sequence or structural similarity from UniProtKB).
GO:0004033;	Molecular function: aldo-keto reductase activity (inferred from direct assay from UniProtKB).
GO:0016651;	Molecular function: oxidoreductase activity, acting on NADH or NADPH (inferred from direct assay from UniProtKB).
GO:0016701;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen (inferred from sequence or structural similarity from UniProtKB).
GO:0019310;	Biological process: inositol catabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001395; Aldo/ket_red.
IPR007828; DUF706.
Graphical view of domain structure.

PANTHER

PTHR12588; DUF706; 1.

Pfam

PF05153; DUF706; 1.
Pfam graphical view of domain structure.

PROSITE

PS00063; ALDOKETO_REDUCTASE_3; 1.

BLOCKS

Q9QXN5.

Genome annotation databases

Ensembl

ENSMUSG00000022613; Mus musculus. [Contig view]

GeneID

56727; -.

KEGG

mmu:56727; -.

NMPDR

fig|10090.3.peg.30445; -.

Phylogenomic databases

HOGENOM

Q9QXN5; -.

HOVERGEN

Q9QXN5; -.

Other

Miox; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 285`	`285`	`Inositol oxygenase.`	`PRO_0000079149`
`METAL`	`98 98`		`Iron 1.`
`METAL`	`123 123`		`Iron 1.`
`METAL`	`124 124`		`Iron 1.`
`METAL`	`124 124`		`Iron 2.`
`METAL`	`194 194`		`Iron 2.`
`METAL`	`220 220`		`Iron 2.`
`METAL`	`253 253`		`Iron 1.`
`CONFLICT`	`65 65`		`S -> G (in Ref. 1; AAF25202).`
`STRAND`	`31 33`	`3`
`HELIX`	`37 50`	`14`
`HELIX`	`53 63`	`11`
`HELIX`	`73 79`	`7`
`HELIX`	`80 82`	`3`
`HELIX`	`95 109`	`15`
`HELIX`	`114 122`	`9`
`HELIX`	`125 132`	`8`
`HELIX`	`136 138`	`3`
`STRAND`	`145 148`	`4`
`TURN`	`155 159`	`5`
`HELIX`	`165 168`	`4`
`TURN`	`170 172`	`3`
`STRAND`	`173 176`	`4`
`HELIX`	`185 187`	`3`
`HELIX`	`194 204`	`11`
`HELIX`	`211 219`	`9`
`HELIX`	`223 226`	`4`
`TURN`	`232 234`	`3`
`HELIX`	`237 255`	`19`
`HELIX`	`264 278`	`15`

Sequence information

Length: 285 AA [This is the length of the unprocessed precursor]

Molecular weight: 33164 Da [This is the MW of the unprocessed precursor]

CRC64: C6877BFF2B60D1A7 [This is a checksum on the sequence]

        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

Q9QXN5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools