Reviewed, UniProtKB/Swiss-Prot Q9UGB7 (MIOX_HUMAN)

Names and origin

Protein names

Recommended name:
    Inositol oxygenase
    EC=1.13.99.1
Alternative name(s):
    Myo-inositol oxygenase
      Short name=MI oxygenase
    Aldehyde reductase-like 6
    Renal-specific oxidoreductase
    Kidney-specific protein 32

Gene names

Name:	MIOX
Synonyms:	ALDRL6, KSP32, RSOR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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-glucuronic acid; D-glucuronic acid from myo-inositol: step 1/1.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Kidney specific.
Sequence similarities	Belongs to the myo-inositol oxygenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	inositol catabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB inclusion body Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	aldo-keto reductase activity Ref.3 Inferred from sequence or structural similarity. Source: UniProtKB inositol oxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Inositol oxygenase

PRO_0000079148

Sites

Metal binding

98

1

Iron 1 By similarity

Metal binding

123

1

Iron 1 By similarity

Metal binding

124

1

Iron 1 By similarity

Metal binding

124

1

Iron 2 By similarity

Metal binding

194

1

Iron 2 By similarity

Metal binding

220

1

Iron 2 By similarity

Metal binding

253

1

Iron 1 By similarity

Experimental info

Sequence conflict

4

1

T → D in AAF25204. Ref.3

Sequence conflict

199

1

Y → F in AAK00766. Ref.2

Sequence conflict

219 – 221

3

FHS → VHF in AAK00766. Ref.2

Sequence conflict

282

1

I → T in AAF25204. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

285

Helix Strand Turn

Details...

Helix

38 – 50

13

Helix

53 – 63

11

Beta strand

68 – 71

4

Helix

73 – 79

7

Helix

80 – 82

3

Helix

95 – 109

15

Helix

114 – 122

9

Helix

125 – 127

3

Helix

128 – 131

4

Helix

136 – 138

3

Beta strand

145 – 148

4

Helix

157 – 160

4

Helix

165 – 168

4

Turn

170 – 172

3

Beta strand

173 – 176

4

Helix

185 – 187

3

Helix

194 – 205

12

Helix

211 – 219

9

Helix

223 – 226

4

Turn

232 – 234

3

Helix

237 – 253

17

Helix

264 – 278

15

Sequences

	Sequence		Length	Mass (Da)
	Q9UGB7-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: ED70B197FF267B2B	FASTA	285	33,010
	10 20 30 40 50 60 MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH 70 80 90 100 110 120 AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG 130 140 150 160 170 180 LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ 190 200 210 220 230 240 PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL 250 260 270 280 AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of human myo-inositol oxygenase (MIOX)." Parthasarathy L., Seelan R., Parthasarathy R. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification of a novel kidney specific gene, KSP32, that is down regulated in acute ischemic renal failure." Hu E., Chen Z., Fredrickson T., Gellai M., Jugus M., Contino L., Spurr N., Sims M., Halsey W., Van Horn S., Mao J., Sathe G., Brooks D. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"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: 10944187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[4]	"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: 15504367] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[9]	"Terminal substrate binding to the myo-inositol oxygenase di-iron cluster." Structural genomics consortium (SGC) Submitted (OCT-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AY064416 mRNA. Translation: AAL47192.1.
AF230095 mRNA. Translation: AAK00766.1.
AF197129 mRNA. Translation: AAF25204.1.
AY738258 mRNA. Translation: AAV65816.1.
AK000576 mRNA. Translation: BAA91266.1.
CR456478 mRNA. Translation: CAG30364.1.
AL096767 Genomic DNA. Translation: CAB63064.1.
BC073848 mRNA. Translation: AAH73848.1.

IPI

IPI00099088.

RefSeq

NP_060054.4.

UniGene

Hs.129227

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IBN	X-ray	1.50	A/B	38-285	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q9UGB7.

Genome annotation databases

Ensembl

ENSG00000100253. Homo sapiens. [Contig view]

GeneID

55586.

KEGG

hsa:55586.

NMPDR

fig|9606.3.peg.21978.

UCSC

uc003bll.1. human.

Organism-specific databases

GeneCards

GC22P049272.

H-InvDB

HIX0023329.

HGNC

HGNC:14522. MIOX.

MIM

606774. gene.

PharmGKB

PA24716.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UGB7.

HOVERGEN

Q9UGB7.

OMA

Q9UGB7. YQVMKFN.

Enzyme and pathway databases

BRENDA

1.13.99.1. 247.

Gene expression databases

ArrayExpress

Q9UGB7.

Bgee

Q9UGB7.

CleanEx

HS_MIOX.

GermOnline

ENSG00000100253. Homo sapiens.

Family and domain databases

InterPro

IPR007828. DUF706.
[Graphical view]

PANTHER

PTHR12588. DUF706. 1 hit.

Pfam

PF05153. DUF706. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

60104.

SOURCE

Search...

Entry information

Entry name

MIOX_HUMAN

Accession

Primary (citable) accession number: Q9UGB7
Secondary accession number(s): Q5S8C9, Q9BZZ1, Q9UHB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	May 1, 2000
Last modified:	July 7, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)