ID INO2_ARATH Reviewed; 510 AA.
AC Q38862; Q9SIE2;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Inositol-3-phosphate synthase isozyme 2;
DE Short=AtIPS2;
DE Short=MIP synthase 2;
DE EC=5.5.1.4;
DE AltName: Full=Myo-inositol 1-phosphate synthase 2;
DE Short=AtMIPS 2;
DE Short=MI-1-P synthase 2;
GN Name=IPS2; Synonyms=MIPS2; OrderedLocusNames=At2g22240; ORFNames=T26C19.10;
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].
RC STRAIN=cv. Columbia;
RA Johnson M.D., Burk D.H.;
RT "Isozyme of 1L-myo-inositol1-phosphate synthase from Arabidopsis.";
RL (er) Plant Gene Register PGR95-067(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18643983; DOI=10.1111/j.1365-313x.2008.03629.x;
RA Murphy A.M., Otto B., Brearley C.A., Carr J.P., Hanke D.E.;
RT "A role for inositol hexakisphosphate in the maintenance of basal
RT resistance to plant pathogens.";
RL Plant J. 56:638-652(2008).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, 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: Key enzyme in myo-inositol biosynthesis pathway that
CC catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-
CC phosphate in a NAD-dependent manner. {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=0.45 mM for D-glucose 6-phosphate {ECO:0000269|PubMed:20215587};
CC KM=0.30 uM for NAD(+) {ECO:0000269|PubMed:20215587};
CC Note=kcat is 4.0 min(-1) for D-glucose 6-phosphate. kcat is 3.6 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 -!- 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=Q38862-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in siliques, leaves, roots, seed
CC endosperm, but not in embryos. Highest expression in seeds. In leaves,
CC only expressed in hydathodes and vascular tissue.
CC {ECO:0000269|PubMed:18603618, ECO:0000269|PubMed:20215587}.
CC -!- DISRUPTION PHENOTYPE: No spontaneous lesion formation and no
CC significant alteration in the response to abscisic acid. Increased
CC susceptibility to bacterial and fungal pathogens.
CC {ECO:0000269|PubMed:18643983, ECO:0000269|PubMed:19812700,
CC ECO:0000269|PubMed:20215587}.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was called MIPS1 in PubMed:18603618. {ECO:0000305}.
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DR EMBL; U30250; AAC49172.1; -; mRNA.
DR EMBL; AC007168; AAD23618.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07280.1; -; Genomic_DNA.
DR EMBL; AY053415; AAK96645.1; -; mRNA.
DR EMBL; AY054202; AAL06863.1; -; mRNA.
DR EMBL; AY143904; AAN28843.1; -; mRNA.
DR PIR; D84610; D84610.
DR RefSeq; NP_179812.1; NM_127790.4. [Q38862-1]
DR AlphaFoldDB; Q38862; -.
DR SMR; Q38862; -.
DR BioGRID; 2110; 2.
DR IntAct; Q38862; 2.
DR STRING; 3702.Q38862; -.
DR PaxDb; 3702-AT2G22240-1; -.
DR EnsemblPlants; AT2G22240.1; AT2G22240.1; AT2G22240. [Q38862-1]
DR GeneID; 816757; -.
DR Gramene; AT2G22240.1; AT2G22240.1; AT2G22240. [Q38862-1]
DR KEGG; ath:AT2G22240; -.
DR Araport; AT2G22240; -.
DR TAIR; AT2G22240; MIPS2.
DR eggNOG; KOG0693; Eukaryota.
DR HOGENOM; CLU_021486_2_0_1; -.
DR InParanoid; Q38862; -.
DR OrthoDB; 1201882at2759; -.
DR PhylomeDB; Q38862; -.
DR BioCyc; ARA:AT2G22240-MONOMER; -.
DR BRENDA; 5.5.1.4; 399.
DR SABIO-RK; Q38862; -.
DR UniPathway; UPA00823; UER00787.
DR PRO; PR:Q38862; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38862; baseline and differential.
DR Genevisible; Q38862; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IGI:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; TAS:TAIR.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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:SF5; INOSITOL-3-PHOSPHATE SYNTHASE 1; 1.
DR PANTHER; PTHR11510; MYO-INOSITOL-1 PHOSPHATE SYNTHASE; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Inositol biosynthesis; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; NAD; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1..510
FT /note="Inositol-3-phosphate synthase isozyme 2"
FT /id="PRO_0000195187"
FT CONFLICT 135
FT /note="E -> D (in Ref. 1; AAC49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="F -> L (in Ref. 1; AAC49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="K -> N (in Ref. 1; AAC49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="L -> W (in Ref. 1; AAC49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="P -> A (in Ref. 1; AAC49172)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="A -> P (in Ref. 1; AAC49172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 56337 MW; BDD58C166E289CE5 CRC64;
MFIESFKVES PNVKYTENEI NSVYDYETTE VVHENRNGTY QWVVKPKTVK YDFKTDTRVP
KLGVMLVGWG GNNGSTLTAG VIANKEGISW ATKDKVQQAN YFGSLTQASS IRVGSYNGEE
IYAPFKSLLP MVNPEDVVFG GWDISDMNLA DAMARARVLD IDLQKQLRPY MENMIPLPGI
YDPDFIAANQ GSRANSVIKG TKKEQVDHII KDMREFKEKN KVDKLVVLWT ANTERYSNVI
VGLNDTTENL LASVEKDESE ISPSTLYAIA CVLEGIPFIN GSPQNTFVPG LIELAISKNC
LIGGDDFKSG QTKMKSVLVD FLVGAGIKPT SIVSYNHLGN NDGMNLSAPQ TFRSKEISKS
NVVDDMVASN GILFEPGEHP DHVVVIKYVP YVADSKRAMD EYTSEIFMGG RNTIVLHNTC
EDSLLAAPII LDLVLLAELS TRIQFKAEGE GKFHSFHPVA TILSYLTKAP LVPPGTPVVN
ALSKQRAMLE NILRACVGLA PENNMIMEYK
//
