ID   INO1_MAIZE              Reviewed;         510 AA.
AC   Q9FPK7; O65196;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Inositol-3-phosphate synthase;
DE            Short=MIP synthase;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol 1-phosphate synthase;
DE            Short=IPS;
DE            Short=MI-1-P synthase;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Early ACR; TISSUE=Leaf;
RA   Larson S.R., Raboy V.;
RT   "Linkage mapping maize and barley myo-inositol 1-phosphate synthase
RT   genes.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shukla S., VanToai T.T.;
RT   "Genomic sequence of maize myo-inositol 1-phosphate synthase gene.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF056326; AAC15756.1; -; mRNA.
DR   EMBL; AF323175; AAG40328.1; -; Genomic_DNA.
DR   PIR; T01647; T01647.
DR   RefSeq; NP_001105552.1; NM_001112082.1.
DR   AlphaFoldDB; Q9FPK7; -.
DR   SMR; Q9FPK7; -.
DR   STRING; 4577.GRMZM2G155242_P01; -.
DR   PaxDb; Q9FPK7; -.
DR   PRIDE; Q9FPK7; -.
DR   GeneID; 542540; -.
DR   KEGG; zma:542540; -.
DR   eggNOG; KOG0693; Eukaryota.
DR   OrthoDB; 451916at2759; -.
DR   BioCyc; MetaCyc:MON-10801; -.
DR   BRENDA; 5.5.1.4; 6752.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9FPK7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IBA:GO_Central.
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   2: Evidence at transcript 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="Inositol-3-phosphate synthase"
FT                   /id="PRO_0000195192"
FT   CONFLICT        18
FT                   /note="M -> T (in Ref. 2; AAG40328)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="A -> T (in Ref. 2; AAG40328)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  56245 MW;  D4B59EECF391CB6D CRC64;
     MFIESFRVES PHVRYGPMEI ESEYRYDTTE LVHEGKDGAS RWVVRPKSVK YNFRTRTAVP
     KLGVMLVGWG GNNGSTLTAG VIANREGISW ATKDKVQQAN YYGSLTQAST IRVGSYNGEE
     IYAPFKSLLP MVNPDDIVFG GWDISNMNLA DSMTRAKVLD IDLQKQLRPY MESMVPLPGI
     YDPDFIAANQ GSRANSVIKG TKKEQVEQII KDIREFKEKN KVDKIVVLWT ANTERYSNVC
     AGLNDTMENL LASVDKNEAE VSPSTLYAIA CVMEGVPFIN GSPQNTFVPG LIDLAIKNNC
     LIGGDDFKSG QTKMKSVLVD FLVGAGIKPT SIVSYNHLGN NDGMNLSAPQ AFRSKEISKS
     NVVDDMVSSN AILYEPGEHP DHVVVIKYVP YVGDSKRAMD EYTSEIFMGG KNTIVLHNTC
     EDSLLAAPII LDLVLLAELS TRIQLKAEGE DKFHSFHPVA TILSYLTKAP LVPPGTPVVN
     ALAKQRAMLE NIMRACVGLA PENNMILEYK