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   27-MAR-2024, entry version 130.
DE   RecName: Full=Inositol oxygenase 1 {ECO:0000303|PubMed:15660207};
DE            EC=1.13.99.1 {ECO:0000250|UniProtKB:Q8H1S0, ECO:0000305|PubMed:15660207};
DE   AltName: Full=Myo-inositol oxygenase 1 {ECO:0000303|PubMed:15660207};
DE            Short=AtMIOX1 {ECO:0000303|PubMed:15660207};
DE            Short=MI oxygenase 1;
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., 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., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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].
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   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., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
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., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxygenative cleavage of myo-inositol to D-
CC       glucuronate. 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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23697;
CC         Evidence={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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q8L799-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, young leaves, stems, flowers
CC       and siliques. {ECO:0000269|PubMed:15660207}.
CC   -!- DISRUPTION PHENOTYPE: Incorporation of the inositol pathway-derived
CC       monosaccharides is strongly reduced in knockout AtMIOX1 seedling walls.
CC       {ECO:0000269|PubMed:15660207}.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF43953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF63180.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC010657; AAF63180.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC012188; AAF43953.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29174.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58508.1; -; 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; AK175818; BAD43581.1; -; mRNA.
DR   EMBL; AK175833; BAD43596.1; -; mRNA.
DR   EMBL; AK176690; BAD44453.1; -; mRNA.
DR   EMBL; AK221931; BAD94364.1; -; mRNA.
DR   RefSeq; NP_001320937.1; NM_001332123.1. [Q8L799-1]
DR   RefSeq; NP_172904.2; NM_101319.4. [Q8L799-1]
DR   AlphaFoldDB; Q8L799; -.
DR   SMR; Q8L799; -.
DR   STRING; 3702.Q8L799; -.
DR   PaxDb; 3702-AT1G14520-1; -.
DR   ProteomicsDB; 250705; -. [Q8L799-1]
DR   EnsemblPlants; AT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
DR   EnsemblPlants; AT1G14520.4; AT1G14520.4; AT1G14520. [Q8L799-1]
DR   GeneID; 838014; -.
DR   Gramene; AT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
DR   Gramene; AT1G14520.4; AT1G14520.4; AT1G14520. [Q8L799-1]
DR   KEGG; ath:AT1G14520; -.
DR   Araport; AT1G14520; -.
DR   TAIR; AT1G14520; MIOX1.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_2_0_1; -.
DR   InParanoid; Q8L799; -.
DR   OMA; HEVYSTK; -.
DR   PhylomeDB; Q8L799; -.
DR   BioCyc; MetaCyc:AT1G14520-MONOMER; -.
DR   BRENDA; 1.13.99.1; 399.
DR   UniPathway; UPA00111; UER00527.
DR   PRO; PR:Q8L799; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L799; 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:SF12; INOSITOL OXYGENASE 1; 1.
DR   PANTHER; PTHR12588; MYOINOSITOL OXYGENASE; 1.
DR   Pfam; PF05153; MIOX; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Ascorbate biosynthesis; Cytoplasm; Iron;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Inositol oxygenase 1"
FT                   /id="PRO_0000079154"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        111
FT                   /note="S -> G (in Ref. 5; BAC42925 and 6;
FT                   BAD43581/BAD43596/BAD94364)"
FT                   /evidence="ECO:0000305"
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
//