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Database: UniProt
Entry: A0A0D2I3A6_9EURO
LinkDB: A0A0D2I3A6_9EURO
Original site: A0A0D2I3A6_9EURO 
ID   A0A0D2I3A6_9EURO        Unreviewed;       535 AA.
AC   A0A0D2I3A6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE            EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN   ORFNames=Z518_10398 {ECO:0000313|EMBL:KIX00259.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX00259.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX00259.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX00259.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) 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; 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}.
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DR   EMBL; KN847483; KIX00259.1; -; Genomic_DNA.
DR   RefSeq; XP_013267395.1; XM_013411941.1.
DR   AlphaFoldDB; A0A0D2I3A6; -.
DR   STRING; 1442369.A0A0D2I3A6; -.
DR   GeneID; 25298469; -.
DR   VEuPathDB; FungiDB:Z518_10398; -.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   OrthoDB; 1201882at2759; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000053617; 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:UP000053617}.
FT   DOMAIN          333..446
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   535 AA;  58528 MW;  DBFD135DABD238EC CRC64;
     MAPHAEVGVG TVNGYSAHEA QPSTKGLFTV NSPNVTYTDD HIKSKYVYRT TAVTKTADGK
     YTASPQETTY DFQVDRKIPK VGMMLVGWGG NNGSTVTAGI IANRRGLVWD TREGPRAANY
     YGSVVMGSTI KLGTDTESGE EINIPFHDVL PMVHPNDLVI GGWDISSMNI AAAMDRAQVL
     EPTLKAMVYK EMALMKPLPS IYYPDFIAAN QEDRADNVLP GNKACMAHVE QIRTDIRNFK
     AQNHLDKVIV LWTANTERYA DIIPGVNDTA ENLLKAIEEG HEEVSPSTVF SVACILENAP
     FINGSPQNTF VPGAIKLAEK HHAFIGGDDF KSGQTKMKSA LVDFLINAGI KLTSIASYNH
     LGNNDGKNLS SQKQFRSKEI SKSNVVDDMV AANTVLYKKG EHPDHTVVIK YMPAVGDNKR
     ALDEYYAEIF MGGHQTISIF NVCEDSLLAS PLIIDLVLVA EMMTRIQWKA EAAGEYKGFH
     SVLSILSYML KAPLTPPGTP VVNALAKQRG ALTNIFRACV GLQPESDMTL EHKLF
//
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