ID A0A0D3DW25_BRAOL Unreviewed; 510 AA.
AC A0A0D3DW25;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN Name=106311363 {ECO:0000313|EnsemblPlants:Bo8g101260.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g101260.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g101260.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo8g101260.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013604011.1; XM_013748557.1.
DR AlphaFoldDB; A0A0D3DW25; -.
DR SMR; A0A0D3DW25; -.
DR STRING; 109376.A0A0D3DW25; -.
DR EnsemblPlants; Bo8g101260.1; Bo8g101260.1; Bo8g101260.
DR GeneID; 106311363; -.
DR Gramene; Bo8g101260.1; Bo8g101260.1; Bo8g101260.
DR KEGG; boe:106311363; -.
DR eggNOG; KOG0693; Eukaryota.
DR HOGENOM; CLU_021486_2_0_1; -.
DR OMA; VPKVGMM; -.
DR OrthoDB; 1201882at2759; -.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000032141; Chromosome C8.
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:UP000032141}.
FT DOMAIN 310..423
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
SQ SEQUENCE 510 AA; 56294 MW; 4977D959C4456C37 CRC64;
MFIESFKVES PNVKYTENEI HSVYDYETTE VVHENRNGTY QWVVKPKTVK YDFKTDTRVP
KLGVMLVGWG GNNGSTLTAG VIANKEGISW ATKDKVQQAN YFGSLTQASS IRVGSYNGEE
IYAPFKSLLP MVNPDDVVFG GWDISDMNLA DAMARARVLD IDLQKQLRPY MEHMVPLPGI
YDPDFIAANQ GSRANSVIKG TKKEQVDQII KDMREFKEKN KVDKLVVLWT ANTERYSDVV
VGLNDTMENL LASVEKNESE ISPSTLYAIA CVLEGIPFIN GSPQNTFVPG LIELAISKNC
LIGGDDFKSG QTKMKSVLVD FLVGAGIKPT SIVSYNHLGN NDGMNLSAPQ TFRSKEISKS
NVVDDMVASN GILFEPGEHP DHVVVIKYVP YVGDSKRAMD EYTSEIFMGG KNTIVMHNTC
EDSLLAAPII LDLVLLAELS TRIQFKAEGE GKFHSFHPVA TILSYLTKAP LVPAGTPVVN
ALSKQRAMLE NILRACVGLA PENNMILEYK
//
