ID   I1P8F7_ORYGL            Unreviewed;       510 AA.
AC   I1P8F7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE            EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
DE   AltName: Full=Myo-inositol 1-phosphate synthase {ECO:0000256|ARBA:ARBA00032949};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA03G0065300.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA03G0065300.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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:0000256|ARBA:ARBA00000113};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005117}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000256|ARBA:ARBA00010813}.
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DR   AlphaFoldDB; I1P8F7; -.
DR   STRING; 4538.I1P8F7; -.
DR   EnsemblPlants; ORGLA03G0065300.1; ORGLA03G0065300.1; ORGLA03G0065300.
DR   Gramene; ORGLA03G0065300.1; ORGLA03G0065300.1; ORGLA03G0065300.
DR   eggNOG; KOG0693; Eukaryota.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   OMA; VPKVGMM; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000007306; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Inositol biosynthesis {ECO:0000256|ARBA:ARBA00022550};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          310..423
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   510 AA;  56262 MW;  2AB9739D7A4330EE CRC64;
     MFIESFRVES PHVRYGAAEI ESDYRYDTTE LVHESHDGAS RWVVRPKSVR YNFRTTTTVP
     KLGVMLVGWG GNNGSTLTAG VIANREGISW ATKDKVQQAN YYGSLTQAST IRVGSYNGEE
     IYAPFKSLLP MVNPDDLVFG GWDISNMNLA DAMTRAKVLD IDLQKQLRPY MESMVPLPGI
     YDPDFIAANQ GSRANNVIKG TKKEQMEQII KDIREFKEKS KVDKVVVLWT ANTERYSNVC
     VGLNDTMENL LASVDKNEAE ISPSTLYAIA CVMEGIPFIN GSPQNTFVPG LIDLAIKNNC
     LIGGDDFKSG QTKMKSVLVD FLVGAGIKPT SIVSYNHLGN NDGMNLSAPQ TFRSKEISKS
     NVVDDMVSSN AILYEPGEHP DHVVVIKYVP YVGDSKRAMD EYTSEIFMGG KSTIVLHNTC
     EDSLLAAPII LDLVLLAELS TRIQLKAEGE EKFHSFHPVA TILSYLTKAP LVPPGTPVVN
     ALAKQRAMLE NIMRACVGLA PENNMILEYK
//