ID   INO1_RAT                Reviewed;         557 AA.
AC   Q6AYK3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 115.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
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; AABR03100304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001013902.2; NM_001013880.2.
DR   AlphaFoldDB; Q6AYK3; -.
DR   SMR; Q6AYK3; -.
DR   BioGRID; 253271; 1.
DR   STRING; 10116.ENSRNOP00000026821; -.
DR   iPTMnet; Q6AYK3; -.
DR   PhosphoSitePlus; Q6AYK3; -.
DR   SwissPalm; Q6AYK3; -.
DR   PaxDb; Q6AYK3; -.
DR   PRIDE; Q6AYK3; -.
DR   Ensembl; ENSRNOT00000026821; ENSRNOP00000026821; ENSRNOG00000019741.
DR   GeneID; 290651; -.
DR   KEGG; rno:290651; -.
DR   UCSC; RGD:1359423; rat.
DR   CTD; 51477; -.
DR   RGD; 1359423; Isyna1.
DR   eggNOG; KOG0693; Eukaryota.
DR   GeneTree; ENSGT00390000018395; -.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   InParanoid; Q6AYK3; -.
DR   OMA; EHDLFIQ; -.
DR   OrthoDB; 451916at2759; -.
DR   PhylomeDB; Q6AYK3; -.
DR   TreeFam; TF300382; -.
DR   BRENDA; 5.5.1.4; 5301.
DR   Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR   SABIO-RK; Q6AYK3; -.
DR   UniPathway; UPA00823; UER00787.
DR   PRO; PR:Q6AYK3; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000019741; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q6AYK3; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; ISO:RGD.
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   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..557
FT                   /note="Inositol-3-phosphate synthase 1"
FT                   /id="PRO_0000324631"
FT   REGION          514..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  60884 MW;  F351B16D74E94281 CRC64;
     MEPAAEILVD SPDVIFGPEA IEARYEYRTT RVSREGGVLR VRPTATRFTF RTARQVPRLG
     VMLVGWGGNN GSTLTAAVLA NRLRLTWPTR TGRKEANYYG SLTQAGTVNL GLDGDGREVF
     VPFSALLPMV APNDLVFDGW DISSLNLAEA MRRAQVLDCG LQEQLWPHME SLRPRPSVYI
     PEFIAANQTA RADNLIPGTR AQQLEQIRKD IRDFRSSAGL DKVIVLWTAN TERFCEVVPG
     RNDTAENLLR TIQLGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LASQRHVFVG
     GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG QNLSAPLQFR SKEVTKSSVV
     DDMVQSNRVL YAPGEEPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
     LLAAPIMLDL VLLTELCQRV SFCTDSDPEP QGFHPVLSVL SFLFKAPLVP PGSPVVNALF
     RQRSCIENIF RACVGLPPQN HMLLEHKMER PFPGIKPEEV KATSPLPCKK ESTPATNGCT
     GDANGHTQAP TPELSTA