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Q8H1S0 (MIOX4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAscorbate biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

inositol catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninositol oxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Inositol oxygenase 4
PRO_0000079156

Regions

Region115 – 1173Substrate binding By similarity
Region174 – 1752Substrate binding By similarity
Region252 – 2532Substrate binding By similarity

Sites

Metal binding1281Iron 1 By similarity
Metal binding1531Iron 1 By similarity
Metal binding1541Iron 1 By similarity
Metal binding1541Iron 2 By similarity
Metal binding2261Iron 2 By similarity
Metal binding2521Iron 2 By similarity
Metal binding2851Iron 1 By similarity
Binding site581Substrate By similarity
Binding site1571Substrate By similarity

Natural variations

Alternative sequence101F → FE in isoform 2.
VSP_041591

Experimental info

Sequence conflict771Q → R in AAP59548. Ref.1
Sequence conflict3001K → E in AAP59548. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 59485B8A05BD2497

FASTA31736,904
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7D7DF0A1B996DE67
Show »

FASTA31837,033

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.

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.
PIRT06010.
RefSeqNP_001190844.1. NM_001203915.1.
NP_194356.2. NM_118759.4.
UniGeneAt.32196.

3D structure databases

ProteinModelPortalQ8H1S0.
SMRQ8H1S0. Positions 74-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14019. 1 interaction.
STRING3702.AT4G26260.1-P.

Proteomic databases

PaxDbQ8H1S0.
PRIDEQ8H1S0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G26260.1; AT4G26260.1; AT4G26260. [Q8H1S0-1]
GeneID828732.
KEGGath:AT4G26260.

Organism-specific databases

TAIRAT4G26260.

Phylogenomic databases

eggNOGNOG135479.
HOGENOMHOG000163182.
InParanoidQ8H1S0.
KOK00469.
OMANNVMMSW.
PhylomeDBQ8H1S0.
ProtClustDBCLSN2687348.

Enzyme and pathway databases

BioCycARA:GQT-847-MONOMER.
BRENDA1.13.99.1. 399.
UniPathwayUPA00111; UER00527.

Gene expression databases

GenevestigatorQ8H1S0.

Family and domain databases

InterProIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERPTHR12588. PTHR12588. 1 hit.
PfamPF05153. DUF706. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMIOX4_ARATH
AccessionPrimary (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: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names