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Database: UniProt
Entry: A0A0N1NYH3_9EURO
LinkDB: A0A0N1NYH3_9EURO
Original site: A0A0N1NYH3_9EURO 
ID   A0A0N1NYH3_9EURO        Unreviewed;       551 AA.
AC   A0A0N1NYH3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-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=AB675_3311 {ECO:0000313|EMBL:KPI39802.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI39802.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI39802.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI39802.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-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}.
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:KPI39802.1}.
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DR   EMBL; LFJN01000014; KPI39802.1; -; Genomic_DNA.
DR   RefSeq; XP_017999765.1; XM_018143351.1.
DR   AlphaFoldDB; A0A0N1NYH3; -.
DR   STRING; 1664694.A0A0N1NYH3; -.
DR   GeneID; 28735231; -.
DR   OrthoDB; 1201882at2759; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000038010; 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:UP000038010}.
FT   DOMAIN          339..452
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   551 AA;  60905 MW;  C68499B5C8EE0877 CRC64;
     MAPHADVGAG TMNGFSITNG TLTPPEFIHN QKETFIVNSP DVQYSADQIR SKYVYRTTTV
     TKSGDYYVAA PKETTYDFKV DRKVGKTGLM LVGLGGNNGT TVTGGILANR RNLTFETKEG
     PRPSNYYGSL VMSSTMKLGT DAISNEEVNI PFHDVLPMVH PNDLVIGGWD ISSMNLADAM
     DRASVLEPDL KRQLRKEMAL MTPLKSIYYP DFIAANQEDR ADHILEGSKA CMAHVEQLRT
     DIRDFKRNNN LDKVIVLWSA NTERFAEIIP GVNDTADNLL KAIEQGHEEV SPSTVFAVAC
     ILEKTPFING SPQNTFVPGA VQLAEQHNAF IGGDDFKSGQ TKMKSALVEF LINAGIKLTS
     IASYNHLGNN DGKNLSSQKQ FRSKEISKSN VVDDMVAANS VLYKKGEHPD HTVVIKYMPA
     VGDNKRALDE YYAEIFMGGH QTISLFNVCE DSLLASPLII DLVILAEMFT RIQWKNNTEP
     EYKNFHSVLS VLSYMLKAPM TPPGTPVVNA LAKQRNALTN IFRACVGLQP ESDMTLEHKL
     FPEAKSKKLV Q
//
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