ID   A0A2B4SQ58_STYPI        Unreviewed;       562 AA.
AC   A0A2B4SQ58;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE            EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN   Name=isyna1-a {ECO:0000313|EMBL:PFX30738.1};
GN   ORFNames=AWC38_SpisGene4483 {ECO:0000313|EMBL:PFX30738.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX30738.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
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   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000256|ARBA:ARBA00010813}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFX30738.1}.
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DR   EMBL; LSMT01000046; PFX30738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4SQ58; -.
DR   STRING; 50429.A0A2B4SQ58; -.
DR   EnsemblMetazoa; XM_022926521.1; XP_022782256.1; LOC111323209.
DR   OrthoDB; 1201882at2759; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706}.
FT   DOMAIN          308..421
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   562 AA;  62679 MW;  B2A3F6DDC304F543 CRC64;
     MSNMETFRVQ SPNVQYTTDY IESKYTYETT QVDCSSKGSY VVRPVETQYT FRTDRRVPKV
     GCMLVGWGGN NGSTITAAVL ANKLGLSWDT KHGVKKANYV GSLTQSSTIC LGTGPNGDVY
     IPLKDILPMV HPDDIIFDGW DISSLNIADA AERAQVLDCG LQRQLRPYLE KMRPRRSIYC
     PDFIAANQVD RADNVLSGSK QGMMEQIRTD IRDFKQKKNL DKVIVLWTAN TERFCDVSEG
     LNDTAENLLM SIAKNEEEVS PSTIFAVASI LEKCSYINGS PQNTNVPGVV ELAKQHGTFI
     GGDDFKSGQT KMKSVLVDFL VSAGLKPVSI VSYNHLGNND GKNLSAPKQF RSKEISKSNV
     VDDMVESNRI LYEKGEKPDH CVVIKYVPYV GDSKRAMDEY TSEIFMHGHN TIVLHNTCED
     SLLAAPIILD LVILCEVCER IKFKVGDDPE FQSFNPVLSL LSYLLKAPLV PSGTPVVNAL
     FKQRSCIENI FRACVGLKPQ NHMTLEHKLS REVHQPLEQN GVADIHNHLE NGIKKNGYVN
     GETKDLKHFH MNGDITQVKE IM
//