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UniProtKB/Swiss-Prot entry Q8H1S0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MIOX4_ARATH
Primary accession number Q8H1S0
Secondary accession numbers Q6XGZ9 Q9STQ8
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 34)
Name and origin of the protein
Protein name Inositol oxygenase 4
Synonyms EC 1.13.99.1
Myo-inositol oxygenase 4
MI oxygenase 4
AtMIOX4
Gene name
Name: MIOX4
OrderedLocusNames: At4g26260
ORFNames: T25K17.70
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
DOI=10.1104/pp.103.033936; PubMed=14976233 [NCBI, ExPASy, EBI, Israel, Japan]
Lorence A., Chevone B.I., Mendes P., Nessler C.L.;
"Myo-inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis.";
Plant Physiol. 134:1200-1205(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
DOI=10.1007/s00425-004-1441-0; PubMed=15660207 [NCBI, ExPASy, EBI, Israel, Japan]
Kanter U., Usadel B., Guerineau F., Li Y., Pauly M., Tenhaken R.;
"The inositol oxygenase gene family of Arabidopsis is involved in the biosynthesis of nucleotide sugar precursors for cell-wall matrix polysaccharides.";
Planta 221:243-254(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY232552; AAP59548.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049171; CAB38955.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161564; CAB79481.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142501; AAN13052.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T06010; T06010.
RefSeq NP_194356.2; -.
UniGene At.32196
3D structure databases
ModBase Q8H1S0.
Organism-specific databases
TAIR At4g26260; -.
Gene expression databases
GermOnline AT4G26260; Arabidopsis thaliana.
Family and domain databases
InterPro IPR007828; DUF706.
Graphical view of domain structure.
PANTHER PTHR12588; DUF706; 1.
Pfam PF05153; DUF706; 1.
Pfam graphical view of domain structure.
BLOCKS Q8H1S0.
Genome annotation databases
GeneID 828732; -.
GenomeReviews CT486007_GR; AT4G26260.
KEGG ath:AT4G26260; -.
NMPDR fig|3702.1.peg.20548; -.
Other
ProtoNet Q8H1S0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Ascorbate biosynthesis; Complete proteome; Cytoplasm; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   317  317     Inositol oxygenase 4. PRO_0000079156
METAL   128   128        Iron 1 (By similarity). 
METAL   153   153        Iron 1 (By similarity). 
METAL   154   154        Iron 1 (By similarity). 
METAL   154   154        Iron 2 (By similarity). 
METAL   226   226        Iron 2 (By similarity). 
METAL   252   252        Iron 2 (By similarity). 
METAL   285   285        Iron 1 (By similarity). 
CONFLICT   10    10        F -> FE (in Ref. 3; CAB38955/CAB79481). 
CONFLICT   77    77        Q -> R (in Ref. 1; AAP59548). 
CONFLICT   300   300        K -> E (in Ref. 1; AAP59548). 
Sequence information
Length: 317 AA [This is the length of the unprocessed precursor] Molecular weight: 36904 Da [This is the MW of the unprocessed precursor] CRC64: 59485B8A05BD2497 [This is a checksum on the sequence]
        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 

Q8H1S0 in FASTA format

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