ID Q7RHJ1_PLAYO Unreviewed; 603 AA.
AC Q7RHJ1;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN ORFNames=PY03995 {ECO:0000313|EMBL:EAA15800.1};
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA15800.1, ECO:0000313|Proteomes:UP000008553};
RN [1] {ECO:0000313|EMBL:EAA15800.1, ECO:0000313|Proteomes:UP000008553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL {ECO:0000313|EMBL:EAA15800.1,
RC ECO:0000313|Proteomes:UP000008553};
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
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:EAA15800.1}.
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DR EMBL; AABL01001197; EAA15800.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7RHJ1; -.
DR SMR; Q7RHJ1; -.
DR STRING; 73239.Q7RHJ1; -.
DR PaxDb; 73239-Q7RHJ1; -.
DR EnsemblProtists; EAA15800; EAA15800; EAA15800.
DR VEuPathDB; PlasmoDB:Py17XNL_001105532; -.
DR InParanoid; Q7RHJ1; -.
DR OMA; VPKVGMM; -.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000008553; 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:UP000008553}.
FT DOMAIN 332..486
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
SQ SEQUENCE 603 AA; 69171 MW; CF9D540C46E19E28 CRC64;
MENYKGLQFL GTKEVGSNFY KKDGNFLNIK YNKDEDSNFV YSNYEHSEIE VKKDVKNGTI
ECKEIKNNYK IMTEKIKTKK LGILIIGIGG NNSTTMLGGI CANAKKITYL DKYEKKKPNY
LGSIFLSSNI RLGYNKIDKE HYYCPIYNLI ELYNPENIVY GGWDINNLNL KDCLIRNKVF
DYNLVEQIKN DMNYVPLKSV YFKGNFIAAN QQKRVNNILV GNNKLEIMEK VRKQIQKFKK
ENKLTDIIVL WSGNTEKNIP HIPGINDTFQ NILLACQNNH ESISPSIIYA LASILENCPF
INSSPQNTLV NGVVELAEQK GIFIIGNDLK TGQTKIKNLL LDTYFGTGLK PKSIVSYNHL
GNNDGKNLSS DSQFYSKKIS KSNLICDYVK ANENLYIDDN FDDVYTNKDD DYCKGDSLIQ
TNVENEEMEN EYNYSDAIEK QKVNSEIVIK YIPYVGDDKK AMDEYISELF MNGKNTISLY
NVCQDSLLAS PILIDLILLV ELSQRIYFKS EKMNENKTNA SLTSTIKVGN YELKHDILSN
KYNGYRKMNS VLFLSSIFCK SPFNSNEYKT RHSFFSQIES LLNFVRVISG FPIDAHVDLS
YMV
//
