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UniProtKB/Swiss-Prot entry Q8L799


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

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Entry information
Entry name MIOX1_ARATH
Primary accession number Q8L799
Secondary accession numbers Q8GXC4 Q9M9R1 Q9MA30
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Inositol oxygenase 1
Synonyms EC 1.13.99.1
Myo-inositol oxygenase 1
MI oxygenase 1
AtMIOX1
Gene name
Name: MIOX1
OrderedLocusNames: At1g14520
ORFNames: F14L17.30, T5E21.2, T5E21_19
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], 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
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.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[6]
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).
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
AC012188; AAF43953.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010657; AAF63180.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136388; AAM97054.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000187; AAN15506.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK118307; BAC42925.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK175115; BAD42878.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK176690; BAD44453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK175818; BAD43581.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK175833; BAD43596.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK221931; BAD94364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_172904.2; -.
UniGene At.23143
3D structure databases
ModBase Q8L799.
Enzyme and pathway databases
BioCyc MetaCyc:AT1G14520-MON; -.
Organism-specific databases
TAIR At1g14520; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0050113; Molecular function: inositol oxygenase activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0019310; Biological process: inositol catabolic process (inferred from electronic annotation from InterPro).
GO:0019853; Biological process: L-ascorbic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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.
ProtoNet Q8L799.
Genome annotation databases
GeneID 838014; -.
GenomeReviews CT485782_GR; AT1G14520.
KEGG ath:AT1G14520; -.
NMPDR fig|3702.1.peg.1736; -.
Other
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   311  311     Inositol oxygenase 1. PRO_0000079154
METAL   122   122        Iron 1 (By similarity). 
METAL   147   147        Iron 1 (By similarity). 
METAL   148   148        Iron 1 (By similarity). 
METAL   148   148        Iron 2 (By similarity). 
METAL   220   220        Iron 2 (By similarity). 
METAL   246   246        Iron 2 (By similarity). 
METAL   279   279        Iron 1 (By similarity). 
CONFLICT   111   111        S -> G (in Ref. 4; BAC42925 and 5; BAD43581/BAD43596/BAD94364). 
Sequence information
Length: 311 AA [This is the length of the unprocessed precursor] Molecular weight: 36574 Da [This is the MW of the unprocessed precursor] CRC64: 0BCBDE175D505F59 [This is a checksum on the sequence]
        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 

Q8L799 in FASTA format

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