MIOX4_ARATH
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 03-AUG-2022, entry version 121.
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}.
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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.AT4G26260.2; -.
DR PaxDb; Q8H1S0; -.
DR PRIDE; Q8H1S0; -.
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; locus:2136839; AT4G26260.
DR eggNOG; KOG1573; Eukaryota.
DR HOGENOM; CLU_050259_2_0_1; -.
DR InParanoid; Q8H1S0; -.
DR OMA; GHEIYGT; -.
DR PhylomeDB; Q8H1S0; -.
DR BioCyc; MetaCyc:AT4G26260-MON; -.
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 Genevisible; Q8H1S0; AT.
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; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
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..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
