ID MIOX2_ARATH Reviewed; 317 AA. AC O82200; Q8LCN3; Q94JX0; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 2. DT 04-NOV-2008, entry version 46. DE RecName: Full=Inositol oxygenase 2; DE EC=1.13.99.1; DE AltName: Full=Myo-inositol oxygenase 2; DE Short=MI oxygenase 2; DE Short=AtMIOX2; GN Name=MIOX2; OrderedLocusNames=At2g19800; ORFNames=F6F22.17; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=15660207; DOI=10.1007/s00425-004-1441-0; RA Kanter U., Usadel B., Guerineau F., Li Y., Pauly M., Tenhaken R.; RT "The inositol oxygenase gene family of Arabidopsis is involved in the RT biosynthesis of nucleotide sugar precursors for cell-wall matrix RT polysaccharides."; RL Planta 221:243-254(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-317. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP FUNCTION. RX PubMed=14976233; DOI=10.1104/pp.103.033936; RA Lorence A., Chevone B.I., Mendes P., Nessler C.L.; RT "Myo-inositol oxygenase offers a possible entry point into plant RT ascorbate biosynthesis."; RL Plant Physiol. 134:1200-1205(2004). CC -!- FUNCTION: Involved in the biosynthesis of UDP-glucuronic acid CC (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. CC May be also involved in plant ascorbate biosynthesis. CC -!- CATALYTIC ACTIVITY: Myo-inositol + O(2) = D-glucuronate + H(2)O. CC -!- COFACTOR: Binds 2 iron ions per subunit (By similarity). CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D- CC glucuronate; D-glucuronate from myo-inositol: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- TISSUE SPECIFICITY: Expressed mainly in roots, stems, flowers and CC siliques. Low expression in leaves. CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC005169; AAC62136.2; -; Genomic_DNA. DR EMBL; AY086497; AAM63498.1; -; mRNA. DR EMBL; AF370587; AAK43906.1; -; mRNA. DR PIR; C84581; C84581. DR RefSeq; NP_565459.1; -. DR UniGene; At.12894; -. DR GeneID; 816499; -. DR GenomeReviews; CT485783_GR; AT2G19800. DR KEGG; ath:AT2G19800; -. DR NMPDR; fig|3702.1.peg.8974; -. DR TAIR; At2g19800; -. DR ArrayExpress; O82200; -. DR GermOnline; AT2G19800; Arabidopsis thaliana. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR007828; DUF706. DR PANTHER; PTHR12588; DUF706; 1. DR Pfam; PF05153; DUF706; 1. PE 2: Evidence at transcript level; KW Ascorbate biosynthesis; Complete proteome; Cytoplasm; Iron; KW Metal-binding; Oxidoreductase. FT CHAIN 1 317 Inositol oxygenase 2. FT /FTId=PRO_0000079155. FT METAL 128 128 Iron 1 (By similarity). FT METAL 153 153 Iron 1 (By similarity). FT METAL 154 154 Iron 1 (By similarity). FT METAL 154 154 Iron 2 (By similarity). FT METAL 226 226 Iron 2 (By similarity). FT METAL 252 252 Iron 2 (By similarity). FT METAL 285 285 Iron 1 (By similarity). FT CONFLICT 62 62 G -> D (in Ref. 3; AAM63498). SQ SEQUENCE 317 AA; 37048 MW; 857EF7C180F00662 CRC64; MTILVEHFVP DSRVDEKKVI EERDNELVLD GGFVVPKSKE TDAFDAPDMN FLGHSFRDYE NGESERQQGV EEFYRMQHIH QTYDFVKKMR KEYGKLNKME MSIWECCELL NNVVDESDPD LDEPQIQHLL QTAEAIRRDY PDEDWLHLTA LIHDLGKVLL LPEFGGLPQW AVVGDTFPVG CTFDSANIHH KYFKGNHDIN NPKYNTKNGV YTEGCGLDNV LMSWGHDDYM YLVAKKNGTT LPHAGLFIIR YHSFYPLHKA GAYTHLMNDE DRDDLKWLHV FNKYDLYSKS KVLVDVEQVK PYYISLINKY FPAKLKW //