MIOX5_ARATH
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 03-AUG-2022, entry version 117.
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.AT5G56640.1; -.
DR PaxDb; Q9FJU4; -.
DR PRIDE; Q9FJU4; -.
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; locus:2165061; AT5G56640.
DR eggNOG; KOG1573; Eukaryota.
DR HOGENOM; CLU_050259_2_0_1; -.
DR InParanoid; Q9FJU4; -.
DR OrthoDB; 1436589at2759; -.
DR PhylomeDB; Q9FJU4; -.
DR BioCyc; ARA:AT5G56640-MON; -.
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 Genevisible; Q9FJU4; AT.
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..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
