ID   MIOX5_ARATH             Reviewed;         314 AA.
AC   Q9FJU4; Q8LFV4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   RecName: Full=Inositol oxygenase 5;
DE            EC=1.13.99.1 {ECO:0000250|UniProtKB:Q8H1S0};
DE   AltName: Full=Myo-inositol oxygenase 5;
DE            Short=AtMIOX5;
DE            Short=MI oxygenase 5;
GN   Name=MIOX5; OrderedLocusNames=At5g56640; ORFNames=MIK19.9;
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], AND TISSUE SPECIFICITY.
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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.
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:0000250|UniProtKB:Q8H1S0}.
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   -!- 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 in flowers and siliques.
CC       {ECO:0000269|PubMed:15660207}.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB013392; BAB09882.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96791.1; -; Genomic_DNA.
DR   EMBL; AY084627; AAM61190.1; -; mRNA.
DR   RefSeq; NP_200475.1; NM_125047.3.
DR   AlphaFoldDB; Q9FJU4; -.
DR   SMR; Q9FJU4; -.
DR   STRING; 3702.Q9FJU4; -.
DR   PaxDb; 3702-AT5G56640-1; -.
DR   ProteomicsDB; 237030; -.
DR   EnsemblPlants; AT5G56640.1; AT5G56640.1; AT5G56640.
DR   GeneID; 835765; -.
DR   Gramene; AT5G56640.1; AT5G56640.1; AT5G56640.
DR   KEGG; ath:AT5G56640; -.
DR   Araport; AT5G56640; -.
DR   TAIR; AT5G56640; MIOX5.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_2_0_1; -.
DR   InParanoid; Q9FJU4; -.
DR   OrthoDB; 66304at2759; -.
DR   PhylomeDB; Q9FJU4; -.
DR   BioCyc; ARA:AT5G56640-MONOMER; -.
DR   BRENDA; 1.13.99.1; 399.
DR   UniPathway; UPA00111; UER00527.
DR   PRO; PR:Q9FJU4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJU4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050113; F:inositol oxygenase activity; IEA:UniProtKB-EC.
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:SF14; INOSITOL OXYGENASE 5; 1.
DR   PANTHER; PTHR12588; MYOINOSITOL OXYGENASE; 1.
DR   Pfam; PF05153; MIOX; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   Genevisible; Q9FJU4; AT.
PE   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; Cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..314
FT                   /note="Inositol oxygenase 5"
FT                   /id="PRO_0000079157"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         249..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        107
FT                   /note="S -> L (in Ref. 4; AAM61190)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  36544 MW;  ABCF484CC1CDA23C CRC64;
     MNISVENPVF VHEDSTTQKT GELRLDSDIP MSKISSDDEV FLAPEMNAFG RQFRDYTDTN
     SERQKSVEHF YATQHTNQTL DFVQKMRSEY GKLDKMVMNI WECCELSKEV VDESDPDLDE
     PQIQHLLQSA EAIRKDYPNE DWLHLTALIH DLGKVLTLPQ FGGLPQWAVV GDTFPVGCAF
     DESNVHHKYF MENPDFNNPK YNTKAGIYSE GCGLENVLMS WGHDDYMYLV AKENGSTLPS
     PGLFIIRYHS FYPLHKAGAY THLMNEEDKE NLKWLHVFNK YDLYSKSKVH VNVEKVKPYY
     MSLIKKYFPE NLRW
//