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MIOX_ORYSJ
ID   MIOX_ORYSJ              Reviewed;         308 AA.
AC   Q5Z8T3;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable inositol oxygenase;
DE            EC=1.13.99.1;
DE   AltName: Full=Myo-inositol oxygenase;
DE            Short=MI oxygenase;
GN   OrderedLocusNames=Os06g0561000, LOC_Os06g36560;
GN   ORFNames=P0456F09.5, P0528E12.30;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(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 (By similarity).
CC       {ECO:0000250}.
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;
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:0000250}.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AP003713; BAD53740.1; -; Genomic_DNA.
DR   EMBL; AP003762; BAD53821.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS98249.1; -; Genomic_DNA.
DR   EMBL; AK068862; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015643978.1; XM_015788492.1.
DR   AlphaFoldDB; Q5Z8T3; -.
DR   SMR; Q5Z8T3; -.
DR   STRING; 4530.OS06T0561000-01; -.
DR   PaxDb; Q5Z8T3; -.
DR   PRIDE; Q5Z8T3; -.
DR   EnsemblPlants; Os06t0561000-01; Os06t0561000-01; Os06g0561000.
DR   GeneID; 4341305; -.
DR   Gramene; Os06t0561000-01; Os06t0561000-01; Os06g0561000.
DR   KEGG; osa:4341305; -.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_1_0_1; -.
DR   InParanoid; Q5Z8T3; -.
DR   OMA; RYNTKYG; -.
DR   OrthoDB; 1436589at2759; -.
DR   BRENDA; 1.13.99.1; 4460.
DR   PlantReactome; R-OSA-1119431; UDP-D-glucuronate biosynthesis (from myo-inositol).
DR   UniPathway; UPA00111; UER00527.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   ExpressionAtlas; Q5Z8T3; baseline and differential.
DR   Genevisible; Q5Z8T3; OS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050113; F:inositol oxygenase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; Cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..308
FT                   /note="Probable inositol oxygenase"
FT                   /id="PRO_0000079158"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  35805 MW;  7612DA5BFA7DE5FF CRC64;
     MTITIEQPHL DAIADRKVAG GGGGDNAAEL VLDGGFVVPD SNAFGNAFRN YEAESERKET
     VEEFYRVNHI NQTYDFVRRM REEYGRVDKT EMGIWECIEL LNEFIDDSDP DLDMPQIEHL
     LQTAEAIRKD FPDEDWLHLT GLIHDLGKVL LHPSFGELPQ WSVVGDTFPV GCAFDECNVH
     FKYFKENPDY LNPKLNTKFG AYSEGCGLDN VLMSWGHDDY MYLVAKENKT TLPSAGLFII
     RYHSFYPLHK HGAYMHLMND EDKENLKWLR VFNKYDLYSK SNERIDVEKV KPYYMSLIEK
     YFPAKLRW
 
 
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