Q8H1S0 (MIOX4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol oxygenase 4
EC=1.13.99.1

Alternative name(s):
Myo-inositol oxygenase 4
Short name=AtMIOX4
Short name=MI oxygenase 4

Gene names

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

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
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
Coding sequence diversity	Alternative splicing
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from mutant phenotype Ref.1. Source: TAIR inositol catabolic process Inferred from electronic annotation. Source: InterPro syncytium formation Inferred from genetic interaction. Source: TAIR
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	inositol oxygenase activity Inferred from direct assay Ref.1. Source: TAIR iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8H1S0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8H1S0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: F → FE

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 317	317	Inositol oxygenase 4		PRO_0000079156
Regions
	Region	115 – 117	3	Substrate binding By similarity
	Region	174 – 175	2	Substrate binding By similarity
	Region	252 – 253	2	Substrate binding By similarity
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
	Binding site	58	1	Substrate By similarity
	Binding site	157	1	Substrate By similarity
Natural variations
	Alternative sequence	10	1	F → FE in isoform 2.		VSP_041591
Experimental info
	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)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 7D7DF0A1B996DE67	FASTA	318	37,033
	10 20 30 40 50 60 MTISVEKPIF EEEVSAFEKS GDNIGELKLD GGFSMPKMDT NDDEAFLAPE MNAFGRQFRD 70 80 90 100 110 120 YDVESERQKG VEEFYRLQHI NQTVDFVKKM RAEYGKLDKM VMSIWECCEL LNEVVDESDP 130 140 150 160 170 180 DLDEPQIQHL LQSAEAIRKD YPNEDWLHLT ALIHDLGKVI TLPQFGGLPQ WAVVGDTFPV 190 200 210 220 230 240 GCAFDESNVH HKYFVENPDF HNETYNTKNG IYSEGCGLNN VMMSWGHDDY MYLVAKENGS 250 260 270 280 290 300 TLPSAGQFII RYHSFYPLHT AGEYTHLMNE EDKENLKWLH VFNKYDLYSK SKVHVDVEKV 310 KPYYMSLIKK YFPENLRW

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] (ISOFORM 1), 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] (ISOFORM 1), 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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"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] (ISOFORM 1). Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY232552 mRNA. Translation: AAP59548.1. AL049171 Genomic DNA. Translation: CAB38955.1. AL161564 Genomic DNA. Translation: CAB79481.1. CP002687 Genomic DNA. Translation: AEE85176.1. CP002687 Genomic DNA. Translation: AEE85177.1. AY142501 mRNA. Translation: AAN13052.1.
IPI	IPI00533093. IPI00991565.
PIR	T06010.
RefSeq	NP_001190844.1. NM_001203915.1. NP_194356.2. NM_118759.4.
UniGene	At.32196.
3D structure databases
ProteinModelPortal	Q8H1S0.
SMR	Q8H1S0. Positions 57-317.
ModBase	Search...
Proteomic databases
PRIDE	Q8H1S0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G26260.1; AT4G26260.1; AT4G26260.
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
eggNOG	KOG1573.
GeneTree	EPGT00050000000001.
HOGENOM	HBG332059.
InParanoid	Q8H1S0.
OMA	DRVLMSW.
PhylomeDB	Q8H1S0.
ProtClustDB	CLSN2687348.
Enzyme and pathway databases
BRENDA	1.13.99.1. 399.
Gene expression databases
Genevestigator	Q8H1S0.
GermOnline	AT4G26260. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR007828. Inositol_oxygenase. [Graphical view]
KO	K00469.
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 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program