Reviewed, UniProtKB/Swiss-Prot Q8H1S0 (MIOX4_ARATH)

Names and origin

Protein names

Recommended name:
    Inositol oxygenase 4
    EC=1.13.99.1
Alternative name(s):
    Myo-inositol oxygenase 4
      Short name=MI oxygenase 4
      Short name=AtMIOX4

Gene names

Name:	MIOX4
Ordered Locus Names:	At4g26260
ORF Names:	T25K17.70

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	317 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.2
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-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular location	Cytoplasm Probable.
Tissue specificity	Expressed in flowers and siliques. Ref.2
Sequence similarities	Belongs to the myo-inositol oxygenase family.

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 Ref.1 Inferred from mutant phenotype. Source: TAIR 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 direct assay. 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 – 317	317	Inositol oxygenase 4		PRO_0000079156
Sites
	Metal binding	128	1	Iron 1 By similarity
	Metal binding	153	1	Iron 1 By similarity
	Metal binding	154	1	Iron 1 By similarity
	Metal binding	154	1	Iron 2 By similarity
	Metal binding	226	1	Iron 2 By similarity
	Metal binding	252	1	Iron 2 By similarity
	Metal binding	285	1	Iron 1 By similarity
Experimental info
	Sequence conflict	10	1	F → FE in CAB38955. Ref.3
	Sequence conflict	10	1	F → FE in CAB79481. Ref.3
	Sequence conflict	77	1	Q → R in AAP59548. Ref.1
	Sequence conflict	300	1	K → E in AAP59548. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8H1S0-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 59485B8A05BD2497	FASTA	317	36,904
	10 20 30 40 50 60 MTISVEKPIF EEVSAFEKSG DNIGELKLDG GFSMPKMDTN DDEAFLAPEM NAFGRQFRDY 70 80 90 100 110 120 DVESERQKGV EEFYRLQHIN QTVDFVKKMR AEYGKLDKMV MSIWECCELL NEVVDESDPD 130 140 150 160 170 180 LDEPQIQHLL QSAEAIRKDY PNEDWLHLTA LIHDLGKVIT LPQFGGLPQW AVVGDTFPVG 190 200 210 220 230 240 CAFDESNVHH KYFVENPDFH NETYNTKNGI YSEGCGLNNV MMSWGHDDYM YLVAKENGST 250 260 270 280 290 300 LPSAGQFIIR YHSFYPLHTA GEYTHLMNEE DKENLKWLHV FNKYDLYSKS KVHVDVEKVK 310 PYYMSLIKKY FPENLRW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"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.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY232552 mRNA. Translation: AAP59548.1. AL049171 Genomic DNA. Translation: CAB38955.1. AL161564 Genomic DNA. Translation: CAB79481.1. AY142501 mRNA. Translation: AAN13052.1.
IPI	IPI00533093.
PIR	T06010.
RefSeq	NP_194356.2.
UniGene	At.32196
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8H1S0.
Proteomic databases
PRIDE	Q8H1S0.
Genome annotation databases
GeneID	828732.
GenomeReviews	Gene locus AT4G26260 in contig CT486007_GR.
KEGG	ath:AT4G26260.
NMPDR	fig|3702.1.peg.20548.
Organism-specific databases
TAIR	At4g26260.
Phylogenomic databases
OMA	DTFPLGC.
Enzyme and pathway databases
BRENDA	1.13.99.1. 302.
Gene expression databases
Genevestigator	Q8H1S0.
GermOnline	AT4G26260. Arabidopsis thaliana.
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

MIOX4_ARATH

Accession

Primary (citable) accession number: Q8H1S0
Secondary accession number(s): Q6XGZ9, Q9STQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)