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INO3_ARATH
ID   INO3_ARATH              Reviewed;         510 AA.
AC   Q9LX12;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Probable inositol 3-phosphate synthase isozyme 3;
DE            Short=AtIPS3;
DE            Short=MIP synthase 3;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol 1-phosphate synthase 3;
DE            Short=AtMIPS 3;
DE            Short=MI-1-P synthase 3;
GN   Name=IPS3; Synonyms=MIPS3; OrderedLocusNames=At5g10170;
GN   ORFNames=T31P16_160;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
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   [3]
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   [4]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=18603618; DOI=10.1093/jxb/ern161;
RA   Mitsuhashi N., Kondo M., Nakaune S., Ohnishi M., Hayashi M.,
RA   Hara-Nishimura I., Richardson A., Fukaki H., Nishimura M., Mimura T.;
RT   "Localization of myo-inositol-1-phosphate synthase to the endosperm in
RT   developing seeds of Arabidopsis.";
RL   J. Exp. Bot. 59:3069-3076(2008).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19812700; DOI=10.1371/journal.pone.0007364;
RA   Meng P.H., Raynaud C., Tcherkez G., Blanchet S., Massoud K.,
RA   Domenichini S., Henry Y., Soubigou-Taconnat L., Lelarge-Trouverie C.,
RA   Saindrenan P., Renou J.P., Bergounioux C.;
RT   "Crosstalks between myo-inositol metabolism, programmed cell death and
RT   basal immunity in Arabidopsis.";
RL   PLoS ONE 4:E7364-E7364(2009).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=20215587; DOI=10.1105/tpc.109.071779;
RA   Donahue J.L., Alford S.R., Torabinejad J., Kerwin R.E., Nourbakhsh A.,
RA   Ray W.K., Hernick M., Huang X., Lyons B.M., Hein P.P., Gillaspy G.E.;
RT   "The Arabidopsis thaliana Myo-inositol 1-phosphate synthase1 gene is
RT   required for Myo-inositol synthesis and suppression of cell death.";
RL   Plant Cell 22:888-903(2010).
CC   -!- FUNCTION: Involved in myo-inositol synthesis.
CC       {ECO:0000269|PubMed:20215587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate;
CC         Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548;
CC         EC=5.5.1.4; Evidence={ECO:0000269|PubMed:20215587};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.31 mM for D-glucose 6-phosphate {ECO:0000269|PubMed:20215587};
CC         KM=0.13 uM for NAD(+) {ECO:0000269|PubMed:20215587};
CC         Note=kcat is 5.2 min(-1) for D-glucose 6-phosphate. kcat is 4.8 min(-
CC         1) for NAD(+).;
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18603618,
CC       ECO:0000269|PubMed:20215587}.
CC   -!- TISSUE SPECIFICITY: Expressed in siliques, leaves, roots, seed
CC       endosperm, but not in embryos. Highest expression in roots. Confined to
CC       vascular tissue and hydathodes of leaves. {ECO:0000269|PubMed:18603618,
CC       ECO:0000269|PubMed:20215587}.
CC   -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC       {ECO:0000269|PubMed:19812700}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AL356332; CAB92058.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91504.1; -; Genomic_DNA.
DR   EMBL; AY065415; AAL38856.1; -; mRNA.
DR   EMBL; AY096554; AAM20204.1; -; mRNA.
DR   PIR; T50021; T50021.
DR   RefSeq; NP_196579.1; NM_121055.4.
DR   AlphaFoldDB; Q9LX12; -.
DR   SMR; Q9LX12; -.
DR   BioGRID; 16159; 2.
DR   STRING; 3702.AT5G10170.1; -.
DR   PaxDb; Q9LX12; -.
DR   PRIDE; Q9LX12; -.
DR   ProteomicsDB; 248459; -.
DR   EnsemblPlants; AT5G10170.1; AT5G10170.1; AT5G10170.
DR   GeneID; 830881; -.
DR   Gramene; AT5G10170.1; AT5G10170.1; AT5G10170.
DR   KEGG; ath:AT5G10170; -.
DR   Araport; AT5G10170; -.
DR   TAIR; locus:2184153; AT5G10170.
DR   eggNOG; KOG0693; Eukaryota.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   InParanoid; Q9LX12; -.
DR   OMA; WDHIAFD; -.
DR   OrthoDB; 451916at2759; -.
DR   PhylomeDB; Q9LX12; -.
DR   BioCyc; ARA:AT5G10170-MON; -.
DR   BRENDA; 5.5.1.4; 399.
DR   SABIO-RK; Q9LX12; -.
DR   UniPathway; UPA00823; UER00787.
DR   PRO; PR:Q9LX12; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LX12; baseline and differential.
DR   Genevisible; Q9LX12; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IGI:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR   GO; GO:0006021; P:inositol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR   InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11510; PTHR11510; 1.
DR   Pfam; PF01658; Inos-1-P_synth; 1.
DR   Pfam; PF07994; NAD_binding_5; 1.
DR   PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..510
FT                   /note="Probable inositol 3-phosphate synthase isozyme 3"
FT                   /id="PRO_0000195188"
SQ   SEQUENCE   510 AA;  56418 MW;  5CB8108082162473 CRC64;
     MFIESFKVES PNVKYTENEI HSVYDYQTTE LVHENKNGAF QWTVKPKTVK YEFKTDTHVP
     KLGVMLVGWG GNNGSTLTAG VIANREGISW ATKEKVQQAN YFGSLTQASS IRVGSFNGEE
     IYAPFKSLLP MVNPEEIVFG GWDISDMNLA DAMARAKVLD IDLQKQMRPF MEHMVPLPGI
     FDPDFIAANQ GSRANHVIKG TKKQQLEQVI KDIREFKEKN KVDKVVVLWT ANTERYSNVV
     VGLNDTTENL MSSLDKDEAE ISPSTLYAIA CVLENVPFIN GSPQNTFVPG LIELAIKRNC
     LIGGDDFKSG QTKMKSVLVD FLVGAGIKPT SIVSYNHLGN NDGMNLSAPQ TFRSKEISKS
     NVVDDMVGSN GILYEPGEHP DHVVVIKYVP CVGDSKRAMD EYTSEIFMGG KNTIVMHNTC
     EDSLLAAPII LDLVLLAELT TRIQFMSENE GKFHSFHPVA TLLSYLSKAP LVPPGTPVVN
     ALSKQRAMLE NVLRACVGLA PENNMILEYK
 
 
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