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 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 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.
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
//
