ID   INO1_CANGA              Reviewed;         538 AA.
AC   Q6FQI1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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;
GN   Name=INO1; OrderedLocusNames=CAGL0I06050g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380955; CAG60450.1; -; Genomic_DNA.
DR   RefSeq; XP_447513.1; XM_447513.1.
DR   AlphaFoldDB; Q6FQI1; -.
DR   SMR; Q6FQI1; -.
DR   STRING; 5478.XP_447513.1; -.
DR   EnsemblFungi; CAG60450; CAG60450; CAGL0I06050g.
DR   GeneID; 2889369; -.
DR   KEGG; cgr:CAGL0I06050g; -.
DR   CGD; CAL0129696; INO1.
DR   VEuPathDB; FungiDB:CAGL0I06050g; -.
DR   eggNOG; KOG0693; Eukaryota.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   InParanoid; Q6FQI1; -.
DR   OMA; EHDLFIQ; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; 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: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   3: Inferred from homology;
KW   Cytoplasm; Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..538
FT                   /note="Inositol-3-phosphate synthase"
FT                   /id="PRO_0000195184"
SQ   SEQUENCE   538 AA;  60271 MW;  FC79F4574C70A328 CRC64;
     MTVNKGISIR VNNVGDKVSY KENELLTNYT YHTNVVHTNS DKTQFEVTPL DKNYQFKVDL
     NKPERLGVML VGLGGNNGST MMAAVLANKH NVCFRTRDKE GLTEPNYYGS LTQSSTIKLG
     VDSKGKDVYV PFNSLVPMVN PNDFVVSGWD INGATMDQAM ERASVLEVDL RNKLAPMMKD
     HKPLKSVYYP DFIAANQDER ADNCLNVDPQ TGKVTTTGKW EHLNHIRNDI RTFKQQNDLD
     KVIILWTANT ERYVEILPGV NDTMENLLEA IKNDHTEIAP STIFAAASIL EHCPYINGSP
     QNTFVPGLIE LAEKNDSLIA GDDFKSGQTK MKSVLAQFLV DAGIRPVSIA SYNHLGNNDG
     YNLSSPQQFR SKEISKASVV DDIIESNPIL YNDKLGNKID HCIVIKYMHA VGDSKVAMDE
     YYSELMLGGH NRISIHNVCE DSLLATPLII DLIVMTEFCS RVTYRNVDGQ DGAEAKGDFE
     NFYPVLSFLS YWLKAPLTKP GYQPINGLNK QRTALENFLR LLIGLPAIDE LRFEERLK