ID   MIOX4_ARATH             Reviewed;         317 AA.
AC   Q8H1S0; Q6XGZ9; Q9STQ8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Inositol oxygenase 4;
DE            EC=1.13.99.1 {ECO:0000305|PubMed:14976233};
DE   AltName: Full=Myo-inositol oxygenase 4 {ECO:0000303|PubMed:14976233};
DE            Short=AtMIOX4 {ECO:0000303|PubMed:14976233};
DE            Short=MI oxygenase 4;
GN   Name=MIOX4; OrderedLocusNames=At4g26260; ORFNames=T25K17.70;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=14976233; DOI=10.1104/pp.103.033936;
RA   Lorence A., Chevone B.I., Mendes P., Nessler C.L.;
RT   "Myo-inositol oxygenase offers a possible entry point into plant ascorbate
RT   biosynthesis.";
RL   Plant Physiol. 134:1200-1205(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND FUNCTION.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
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. {ECO:0000269|PubMed:14976233,
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:0000305|PubMed:14976233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23697;
CC         Evidence={ECO:0000305|PubMed:14976233};
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=2;
CC       Name=1;
CC         IsoId=Q8H1S0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8H1S0-2; Sequence=VSP_041591;
CC   -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, siliques, and to a
CC       lesser extent in roots. {ECO:0000269|PubMed:14976233,
CC       ECO:0000269|PubMed:15660207}.
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; AY232552; AAP59548.1; -; mRNA.
DR   EMBL; AL049171; CAB38955.1; -; Genomic_DNA.
DR   EMBL; AL161564; CAB79481.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85176.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85177.1; -; Genomic_DNA.
DR   EMBL; AY142501; AAN13052.1; -; mRNA.
DR   PIR; T06010; T06010.
DR   RefSeq; NP_001190844.1; NM_001203915.2. [Q8H1S0-2]
DR   RefSeq; NP_194356.2; NM_118759.5. [Q8H1S0-1]
DR   AlphaFoldDB; Q8H1S0; -.
DR   SMR; Q8H1S0; -.
DR   BioGRID; 14019; 1.
DR   STRING; 3702.Q8H1S0; -.
DR   PaxDb; 3702-AT4G26260-2; -.
DR   ProteomicsDB; 250706; -. [Q8H1S0-1]
DR   EnsemblPlants; AT4G26260.1; AT4G26260.1; AT4G26260. [Q8H1S0-1]
DR   EnsemblPlants; AT4G26260.2; AT4G26260.2; AT4G26260. [Q8H1S0-2]
DR   GeneID; 828732; -.
DR   Gramene; AT4G26260.1; AT4G26260.1; AT4G26260. [Q8H1S0-1]
DR   Gramene; AT4G26260.2; AT4G26260.2; AT4G26260. [Q8H1S0-2]
DR   KEGG; ath:AT4G26260; -.
DR   Araport; AT4G26260; -.
DR   TAIR; AT4G26260; MIOX4.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_2_0_1; -.
DR   InParanoid; Q8H1S0; -.
DR   OMA; MTIQLEG; -.
DR   OrthoDB; 66304at2759; -.
DR   PhylomeDB; Q8H1S0; -.
DR   BioCyc; MetaCyc:AT4G26260-MONOMER; -.
DR   BRENDA; 1.13.99.1; 399.
DR   UniPathway; UPA00111; UER00527.
DR   PRO; PR:Q8H1S0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8H1S0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050113; F:inositol oxygenase activity; IDA:TAIR.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR   InterPro; IPR007828; Inositol_oxygenase.
DR   PANTHER; PTHR12588:SF4; INOSITOL OXYGENASE 4; 1.
DR   PANTHER; PTHR12588; MYOINOSITOL OXYGENASE; 1.
DR   Pfam; PF05153; MIOX; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   Genevisible; Q8H1S0; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Ascorbate biosynthesis; Cytoplasm; Iron;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..317
FT                   /note="Inositol oxygenase 4"
FT                   /id="PRO_0000079156"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         10
FT                   /note="F -> FE (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041591"
FT   CONFLICT        77
FT                   /note="Q -> R (in Ref. 1; AAP59548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="K -> E (in Ref. 1; AAP59548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  36904 MW;  59485B8A05BD2497 CRC64;
     MTISVEKPIF EEVSAFEKSG DNIGELKLDG GFSMPKMDTN DDEAFLAPEM NAFGRQFRDY
     DVESERQKGV EEFYRLQHIN QTVDFVKKMR AEYGKLDKMV MSIWECCELL NEVVDESDPD
     LDEPQIQHLL QSAEAIRKDY PNEDWLHLTA LIHDLGKVIT LPQFGGLPQW AVVGDTFPVG
     CAFDESNVHH KYFVENPDFH NETYNTKNGI YSEGCGLNNV MMSWGHDDYM YLVAKENGST
     LPSAGQFIIR YHSFYPLHTA GEYTHLMNEE DKENLKWLHV FNKYDLYSKS KVHVDVEKVK
     PYYMSLIKKY FPENLRW
//