ID   INO1_BOVIN              Reviewed;         557 AA.
AC   Q2NL29;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Inositol-3-phosphate synthase 1;
DE            Short=IPS 1;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol 1-phosphate synthase;
DE            Short=MI-1-P synthase;
DE            Short=MIP synthase;
GN   Name=ISYNA1; Synonyms=INO1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that
CC       catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-
CC       phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC       synthesis of all inositol-containing compounds (By similarity).
CC       {ECO:0000250}.
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; BC111160; AAI11161.1; -; mRNA.
DR   RefSeq; NP_001039497.1; NM_001046032.2.
DR   AlphaFoldDB; Q2NL29; -.
DR   SMR; Q2NL29; -.
DR   STRING; 9913.ENSBTAP00000023241; -.
DR   PaxDb; Q2NL29; -.
DR   PRIDE; Q2NL29; -.
DR   Ensembl; ENSBTAT00000023241; ENSBTAP00000023241; ENSBTAG00000017482.
DR   GeneID; 509394; -.
DR   KEGG; bta:509394; -.
DR   CTD; 51477; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017482; -.
DR   VGNC; VGNC:30306; ISYNA1.
DR   eggNOG; KOG0693; Eukaryota.
DR   GeneTree; ENSGT00390000018395; -.
DR   HOGENOM; CLU_021486_2_1_1; -.
DR   InParanoid; Q2NL29; -.
DR   OMA; EHDLFIQ; -.
DR   OrthoDB; 451916at2759; -.
DR   TreeFam; TF300382; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000017482; Expressed in spermatocyte and 108 other tissues.
DR   ExpressionAtlas; Q2NL29; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0006021; P:inositol biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..557
FT                   /note="Inositol-3-phosphate synthase 1"
FT                   /id="PRO_0000324627"
FT   REGION          527..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  60761 MW;  ED36D9C5754C1FDA CRC64;
     MEAATEFVVE SPDVVYSPET IEAQYEYRTT SVSREGGVLK VHPTSTRFTF RTARQVPRLG
     VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR TGRKEANYYG SLTQAGTVSL GLDAEGKEVF
     VPFSSLLPMV APDDLVFDGW DISSLNLAEA MRRAQVLDWG LQEQLWPHME AMRPRPSVYI
     PEFIAANQSA RADNVIPGTR AQQLEQIRRD IRDFRFSAGL DKVIVLWTAN TERFCEVIPG
     LNDTAENLLR TIQLGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQRRVFVG
     GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG QNLSAPPQFR SKEVSKSSVV
     DDMVHSNPVL YSPGEQPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
     LLAAPIMLDL ALLTELCQRV SFCTDVDPDP QSFHPVLSLL GFLFKAPLAP PGSPVVNALF
     RQRSCIENIL RACVGLPPQN HMLLEHKMER PGLKRVGPLA TTSPVLCKKG SAPTAPNGCT
     GDANGHSQAE APQMPTT