Reviewed, UniProtKB/Swiss-Prot Q8L799 (MIOX1_ARATH)

Names and origin

Protein names

Recommended name:
    Inositol oxygenase 1
    EC=1.13.99.1
Alternative name(s):
    Myo-inositol oxygenase 1
      Short name=MI oxygenase 1
      Short name=AtMIOX1

Gene names

Name:	MIOX1
Ordered Locus Names:	At1g14520
ORF Names:	F14L17.30, T5E21.2, T5E21_19

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.6
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 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 process	Ascorbate biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW inositol catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	inositol oxygenase activity Ref.1 Inferred from mutant phenotype. Source: TAIR 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 – 311	311	Inositol oxygenase 1		PRO_0000079154
Sites
	Metal binding	122	1	Iron 1 By similarity
	Metal binding	147	1	Iron 1 By similarity
	Metal binding	148	1	Iron 1 By similarity
	Metal binding	148	1	Iron 2 By similarity
	Metal binding	220	1	Iron 2 By similarity
	Metal binding	246	1	Iron 2 By similarity
	Metal binding	279	1	Iron 1 By similarity
Experimental info
	Sequence conflict	111	1	S → G in BAC42925. Ref.4
	Sequence conflict	111	1	S → G in BAD43581. Ref.5
	Sequence conflict	111	1	S → G in BAD43596. Ref.5
	Sequence conflict	111	1	S → G in BAD94364. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8L799-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 0BCBDE175D505F59	FASTA	311	36,574
	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

References

	« Hide 'large scale' referencesShow '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: 15660207] [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. , 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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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. , 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.
[6]	"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: 14976233] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC012188 Genomic DNA. Translation: AAF43953.1. Sequence problems. AC010657 Genomic DNA. Translation: AAF63180.1. Sequence problems. AY136388 mRNA. Translation: AAM97054.1. BT000187 mRNA. Translation: AAN15506.1. AK118307 mRNA. Translation: BAC42925.1. AK175115 mRNA. Translation: BAD42878.1. AK176690 mRNA. Translation: BAD44453.1. AK175818 mRNA. Translation: BAD43581.1. AK175833 mRNA. Translation: BAD43596.1. AK221931 mRNA. Translation: BAD94364.1.
IPI	IPI00531494.
RefSeq	NP_172904.2.
UniGene	At.23143
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q8L799.
Genome annotation databases
GeneID	838014.
GenomeReviews	Gene locus AT1G14520 in contig CT485782_GR.
KEGG	ath:AT1G14520.
NMPDR	fig|3702.1.peg.1736.
Organism-specific databases
TAIR	At1g14520.
Phylogenomic databases
OMA	Q8L799. YQVMKFN.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G14520-MON.
BRENDA	1.13.99.1. 302.
Family and domain databases
InterPro	IPR007828. DUF706. [Graphical view]
PANTHER	PTHR12588. DUF706. 1 hit.
Pfam	PF05153. DUF706. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MIOX1_ARATH

Accession

Primary (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:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)