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   16-JUN-2009, entry version 41.
DE   RecName: Full=Inositol oxygenase 4;
DE            EC=1.13.99.1;
DE   AltName: Full=Myo-inositol oxygenase 4;
DE            Short=MI oxygenase 4;
DE            Short=AtMIOX4;
GN   Name=MIOX4; OrderedLocusNames=At4g26260; ORFNames=T25K17.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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
RT   ascorbate biosynthesis.";
RL   Plant Physiol. 134:1200-1205(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Involved in the biosynthesis of UDP-glucuronic acid
CC       (UDP-GlcA), providing nucleotide sugars for cell-wall polymers.
CC       May be also involved in plant ascorbate biosynthesis.
CC   -!- CATALYTIC ACTIVITY: Myo-inositol + O(2) = D-glucuronate + H(2)O.
CC   -!- COFACTOR: Binds 2 iron ions per subunit (By similarity).
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC       glucuronic acid; D-glucuronic acid from myo-inositol: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
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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; AY142501; AAN13052.1; -; mRNA.
DR   IPI; IPI00533093; -.
DR   PIR; T06010; T06010.
DR   RefSeq; NP_194356.2; -.
DR   UniGene; At.32196; -.
DR   GeneID; 828732; -.
DR   GenomeReviews; CT486007_GR; AT4G26260.
DR   KEGG; ath:AT4G26260; -.
DR   NMPDR; fig|3702.1.peg.20548; -.
DR   TAIR; At4g26260; -.
DR   OMA; Q8H1S0; DTFPLGC.
DR   BRENDA; 1.13.99.1; 302.
DR   GermOnline; AT4G26260; Arabidopsis thaliana.
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:UniProtKB-KW.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007828; DUF706.
DR   PANTHER; PTHR12588; DUF706; 1.
DR   Pfam; PF05153; DUF706; 1.
PE   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; Complete proteome; Cytoplasm; Iron;
KW   Metal-binding; Oxidoreductase.
FT   CHAIN         1    317       Inositol oxygenase 4.
FT                                /FTId=PRO_0000079156.
FT   METAL       128    128       Iron 1 (By similarity).
FT   METAL       153    153       Iron 1 (By similarity).
FT   METAL       154    154       Iron 1 (By similarity).
FT   METAL       154    154       Iron 2 (By similarity).
FT   METAL       226    226       Iron 2 (By similarity).
FT   METAL       252    252       Iron 2 (By similarity).
FT   METAL       285    285       Iron 1 (By similarity).
FT   CONFLICT     10     10       F -> FE (in Ref. 3; CAB38955/CAB79481).
FT   CONFLICT     77     77       Q -> R (in Ref. 1; AAP59548).
FT   CONFLICT    300    300       K -> E (in Ref. 1; AAP59548).
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
//