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Database: UniProt
Entry: A0A067T6U7_GALM3
LinkDB: A0A067T6U7_GALM3
Original site: A0A067T6U7_GALM3 
ID   A0A067T6U7_GALM3        Unreviewed;       555 AA.
AC   A0A067T6U7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, 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=GALMADRAFT_154800 {ECO:0000313|EMBL:KDR78900.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR78900.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL142374; KDR78900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067T6U7; -.
DR   STRING; 685588.A0A067T6U7; -.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   OrthoDB; 1201882at2759; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000027222; 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:UP000027222}.
FT   DOMAIN          340..465
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   555 AA;  60971 MW;  5B2B0B6928B8B32A CRC64;
     MAPVLSTNTS GYNTPESELE SMLPVHPTAA RRPHAITVQS ENTLYSDEHI TAKFFNRGSE
     VTVTDGHVNV KPTVQEYEFQ TKRAVSKTGL MMIGVGGNNG STLCATILAN RHNILWHTKE
     GIRQPNYIGS VLRASTVRIG TESSSGKEVH VPVSDVLPMV HPNDLVLGGW DISGLPMDKA
     MQRAQVLDYD LQRQVTPHMA LLGKPLPSIY YPDFIAANQE ARADNLIPGN DKQAHLDHIR
     GDIRKFKQEN GLDRIVVFWT ANTERYSDII PGVNDNADNL LNAIKTSHAE ISPSSLFAVA
     AILEGEPFIN GAPQNTFVPG VIQLAERHHS FIGGDDLKSG QTKLKSVLAE FLVNAGIKPL
     SIASYNHLGN NDGHNLSAER QFKSKEISKS SVVDDMVDAN RLLYKAPKVG AKGVPVGKGE
     HPDHIVVIKY VPAVGDSKRA IDEYYSEIFC GGRSTINIFN ECEDSLLATP LILDLTILTE
     LLTRVQYRKV AEQKDFAPLY SVLSLLSYML KAPLVKPGTE VVNSLNRQRN ALESFLKACI
     GLEGNTDLLL ETRIW
//
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