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   27-MAR-2024, entry version 134.
DE   RecName: Full=Inositol oxygenase 2 {ECO:0000303|PubMed:15660207};
DE            EC=1.13.99.1 {ECO:0000250|UniProtKB:Q8H1S0, ECO:0000305|PubMed:15660207};
DE   AltName: Full=Myo-inositol oxygenase 2;
DE            Short=AtMIOX2;
DE            Short=MI oxygenase 2;
GN   Name=MIOX2; OrderedLocusNames=At2g19800; ORFNames=F6F22.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND CATALYTIC ACTIVITY.
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   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., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-317.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Involved in the biosynthesis of UDP-glucuronic acid (UDP-
CC       GlcA), providing nucleotide sugars for cell-wall polymers. May be also
CC       involved in plant ascorbate biosynthesis.
CC       {ECO:0000305|PubMed:15660207}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + O2 = D-glucuronate + H(+) + H2O;
CC         Xref=Rhea:RHEA:23696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17268, ChEBI:CHEBI:58720;
CC         EC=1.13.99.1; Evidence={ECO:0000250|UniProtKB:Q8H1S0,
CC         ECO:0000305|PubMed:15660207};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC       glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in roots, stems, flowers and
CC       siliques. Low expression in leaves. {ECO:0000269|PubMed:15660207}.
CC   -!- DISRUPTION PHENOTYPE: Incorporation of the inositol pathway-derived
CC       monosaccharides is strongly reduced in knockout AtMIOX2 seedling walls.
CC       {ECO:0000269|PubMed:15660207}.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AC005169; AAC62136.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06927.1; -; Genomic_DNA.
DR   EMBL; AY086497; AAM63498.1; -; mRNA.
DR   EMBL; AF370587; AAK43906.1; -; mRNA.
DR   PIR; C84581; C84581.
DR   RefSeq; NP_565459.1; NM_127538.4.
DR   AlphaFoldDB; O82200; -.
DR   SMR; O82200; -.
DR   STRING; 3702.O82200; -.
DR   PaxDb; 3702-AT2G19800-1; -.
DR   ProteomicsDB; 250711; -.
DR   EnsemblPlants; AT2G19800.1; AT2G19800.1; AT2G19800.
DR   GeneID; 816499; -.
DR   Gramene; AT2G19800.1; AT2G19800.1; AT2G19800.
DR   KEGG; ath:AT2G19800; -.
DR   Araport; AT2G19800; -.
DR   TAIR; AT2G19800; MIOX2.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_2_0_1; -.
DR   InParanoid; O82200; -.
DR   OMA; HHKYFEG; -.
DR   OrthoDB; 66304at2759; -.
DR   PhylomeDB; O82200; -.
DR   BRENDA; 1.13.99.1; 399.
DR   UniPathway; UPA00111; UER00527.
DR   PRO; PR:O82200; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82200; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050113; F:inositol oxygenase activity; IMP:TAIR.
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   InterPro; IPR007828; Inositol_oxygenase.
DR   PANTHER; PTHR12588:SF10; INOSITOL OXYGENASE 2; 1.
DR   PANTHER; PTHR12588; MYOINOSITOL OXYGENASE; 1.
DR   Pfam; PF05153; MIOX; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   Genevisible; O82200; AT.
PE   1: Evidence at protein level;
KW   Ascorbate biosynthesis; Cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..317
FT                   /note="Inositol oxygenase 2"
FT                   /id="PRO_0000079155"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        62
FT                   /note="G -> D (in Ref. 4; AAM63498)"
FT                   /evidence="ECO:0000305"
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
//