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 27-MAR-2024, entry version 102. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 39947.Q5Z8T3; -. DR PaxDb; 39947-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; HTSGAYM; -. DR OrthoDB; 66304at2759; -. 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 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 Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1. 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. DR Genevisible; Q5Z8T3; OS. 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 //