ID MIOX1_ARATH Reviewed; 311 AA. AC Q8L799; Q8GXC4; Q9M9R1; Q9MA30; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-DEC-2008, entry version 38. DE RecName: Full=Inositol oxygenase 1; DE EC=1.13.99.1; DE AltName: Full=Myo-inositol oxygenase 1; DE Short=MI oxygenase 1; DE Short=AtMIOX1; GN Name=MIOX1; OrderedLocusNames=At1g14520; GN ORFNames=F14L17.30, T5E21.2, T5E21_19; 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=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21932900; PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [6] 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 in roots, young leaves, stems, CC flowers and siliques. CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAF43953.1; Type=Erroneous gene model prediction; CC Sequence=AAF63180.1; Type=Erroneous gene model prediction; 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; AC012188; AAF43953.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC010657; AAF63180.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY136388; AAM97054.1; -; mRNA. DR EMBL; BT000187; AAN15506.1; -; mRNA. DR EMBL; AK118307; BAC42925.1; -; mRNA. DR EMBL; AK175115; BAD42878.1; -; mRNA. DR EMBL; AK176690; BAD44453.1; -; mRNA. DR EMBL; AK175818; BAD43581.1; -; mRNA. DR EMBL; AK175833; BAD43596.1; -; mRNA. DR EMBL; AK221931; BAD94364.1; -; mRNA. DR RefSeq; NP_172904.2; -. DR UniGene; At.23143; -. DR PRIDE; Q8L799; -. DR GeneID; 838014; -. DR GenomeReviews; CT485782_GR; AT1G14520. DR KEGG; ath:AT1G14520; -. DR NMPDR; fig|3702.1.peg.1736; -. DR TAIR; At1g14520; -. DR BioCyc; MetaCyc:AT1G14520-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0050113; F:inositol oxygenase activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; 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 1 311 Inositol oxygenase 1. FT /FTId=PRO_0000079154. FT METAL 122 122 Iron 1 (By similarity). FT METAL 147 147 Iron 1 (By similarity). FT METAL 148 148 Iron 1 (By similarity). FT METAL 148 148 Iron 2 (By similarity). FT METAL 220 220 Iron 2 (By similarity). FT METAL 246 246 Iron 2 (By similarity). FT METAL 279 279 Iron 1 (By similarity). FT CONFLICT 111 111 S -> G (in Ref. 4; BAC42925 and 5; FT BAD43581/BAD43596/BAD94364). SQ SEQUENCE 311 AA; 36574 MW; 0BCBDE175D505F59 CRC64; MTILIDRHSD QNDAGDEIVE KNQGNGKEEE TELVLDAGFE APHTNSFGRT FRDYDAESER RRGVEEFYRV NHIGQTVDFV RKMREEYEKL NRTEMSIWEC CELLNEFIDE SDPDLDEPQI EHLLQTAEAI RKDYPDEDWL HLTGLIHDLG KVLLHSSFGE LPQWAVVGDT FPVGCAFDES IVHHKYFKEN PDYDNPSYNS KYGIYTEGCG LDNVLMSWGH DDYMYLVAKE NQTTLPSAGL FIIRYHSFYA LHKSEAYKHL MNNEDRENMK WLKVFNKYDL YSKSKVRVNV EEVKPYYLSL TNKYFPSKLK W //