MIOX1_ARATH
ID MIOX1_ARATH Reviewed; 311 AA.
AC Q8L799; Q8GXC4; Q9M9R1; Q9MA30;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Inositol oxygenase 1 {ECO:0000303|PubMed:15660207};
DE EC=1.13.99.1 {ECO:0000250|UniProtKB:Q8H1S0, ECO:0000305|PubMed:15660207};
DE AltName: Full=Myo-inositol oxygenase 1 {ECO:0000303|PubMed:15660207};
DE Short=AtMIOX1 {ECO:0000303|PubMed:15660207};
DE Short=MI oxygenase 1;
GN Name=MIOX1; OrderedLocusNames=At1g14520;
GN ORFNames=F14L17.30, T5E21.2, T5E21_19;
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxygenative cleavage of myo-inositol to D-
CC glucuronate. 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:0000305|PubMed:15660207}.
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 ECO:0000305|PubMed:15660207};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23697;
CC Evidence={ECO:0000305|PubMed:15660207};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8L799-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, young leaves, stems, flowers
CC and siliques. {ECO:0000269|PubMed:15660207}.
CC -!- DISRUPTION PHENOTYPE: Incorporation of the inositol pathway-derived
CC monosaccharides is strongly reduced in knockout AtMIOX1 seedling walls.
CC {ECO:0000269|PubMed:15660207}.
CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF63180.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010657; AAF63180.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC012188; AAF43953.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29174.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58508.1; -; Genomic_DNA.
DR EMBL; AY136388; AAM97054.1; -; mRNA.
DR EMBL; BT000187; AAN15506.1; -; mRNA.
DR EMBL; AK118307; BAC42925.1; -; mRNA.
DR EMBL; AK175115; BAD42878.1; -; mRNA.
DR EMBL; AK175818; BAD43581.1; -; mRNA.
DR EMBL; AK175833; BAD43596.1; -; mRNA.
DR EMBL; AK176690; BAD44453.1; -; mRNA.
DR EMBL; AK221931; BAD94364.1; -; mRNA.
DR RefSeq; NP_001320937.1; NM_001332123.1. [Q8L799-1]
DR RefSeq; NP_172904.2; NM_101319.4. [Q8L799-1]
DR AlphaFoldDB; Q8L799; -.
DR SMR; Q8L799; -.
DR STRING; 3702.AT1G14520.1; -.
DR PaxDb; Q8L799; -.
DR ProteomicsDB; 250705; -. [Q8L799-1]
DR EnsemblPlants; AT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
DR EnsemblPlants; AT1G14520.4; AT1G14520.4; AT1G14520. [Q8L799-1]
DR GeneID; 838014; -.
DR Gramene; AT1G14520.1; AT1G14520.1; AT1G14520. [Q8L799-1]
DR Gramene; AT1G14520.4; AT1G14520.4; AT1G14520. [Q8L799-1]
DR KEGG; ath:AT1G14520; -.
DR Araport; AT1G14520; -.
DR TAIR; locus:2012572; AT1G14520.
DR eggNOG; KOG1573; Eukaryota.
DR HOGENOM; CLU_050259_2_0_1; -.
DR InParanoid; Q8L799; -.
DR OMA; HTNSFGQ; -.
DR PhylomeDB; Q8L799; -.
DR BioCyc; MetaCyc:AT1G14520-MON; -.
DR BRENDA; 1.13.99.1; 399.
DR UniPathway; UPA00111; UER00527.
DR PRO; PR:Q8L799; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L799; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050113; F:inositol oxygenase activity; IMP:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Ascorbate biosynthesis; Cytoplasm; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..311
FT /note="Inositol oxygenase 1"
FT /id="PRO_0000079154"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246..247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="S -> G (in Ref. 5; BAC42925 and 6; BAD43581/
FT BAD43596/BAD94364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 36574 MW; 0BCBDE175D505F59 CRC64;
MTILIDRHSD QNDAGDEIVE KNQGNGKEEE TELVLDAGFE APHTNSFGRT FRDYDAESER
RRGVEEFYRV NHIGQTVDFV RKMREEYEKL NRTEMSIWEC CELLNEFIDE SDPDLDEPQI
EHLLQTAEAI RKDYPDEDWL HLTGLIHDLG KVLLHSSFGE LPQWAVVGDT FPVGCAFDES
IVHHKYFKEN PDYDNPSYNS KYGIYTEGCG LDNVLMSWGH DDYMYLVAKE NQTTLPSAGL
FIIRYHSFYA LHKSEAYKHL MNNEDRENMK WLKVFNKYDL YSKSKVRVNV EEVKPYYLSL
TNKYFPSKLK W
