MIOX2_ARATH
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 03-AUG-2022, entry version 126.
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.AT2G19800.1; -.
DR PaxDb; O82200; -.
DR PRIDE; O82200; -.
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; locus:2052015; AT2G19800.
DR eggNOG; KOG1573; Eukaryota.
DR HOGENOM; CLU_050259_2_0_1; -.
DR InParanoid; O82200; -.
DR OMA; MINCSNA; -.
DR OrthoDB; 1436589at2759; -.
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 Genevisible; O82200; AT.
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; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR007828; Inositol_oxygenase.
DR PANTHER; PTHR12588; PTHR12588; 1.
DR Pfam; PF05153; MIOX; 1.
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
