ID D7FUT9_ECTSI Unreviewed; 759 AA.
AC D7FUT9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN Name=IPS {ECO:0000313|EMBL:CBJ31745.1};
GN ORFNames=Esi_0279_0022 {ECO:0000313|EMBL:CBJ31745.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ31745.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ31745.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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 EMBL; FN648463; CBJ31745.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FUT9; -.
DR SMR; D7FUT9; -.
DR STRING; 2880.D7FUT9; -.
DR EnsemblProtists; CBJ31745; CBJ31745; Esi_0279_0022.
DR eggNOG; KOG0693; Eukaryota.
DR InParanoid; D7FUT9; -.
DR OrthoDB; 35034at2759; -.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000002630; Chromosome LG16.
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; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
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 Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Inositol biosynthesis {ECO:0000256|ARBA:ARBA00022550};
KW Isomerase {ECO:0000313|EMBL:CBJ31745.1};
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:UP000002630}.
FT DOMAIN 202..305
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
FT DOMAIN 394..726
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 759 AA; 80135 MW; 15DD0D9DB7D393C5 CRC64;
MVSPWPPLPS KGGSGGYRER YALADANNAA IGGWDIRPTP LGEALYNARI LDFDLVRQVR
EEMDTLRLLP GVWDPDFIGE SQHESATNVV GDGESQQSRL ERLRIDIREF REAEGVTGHV
TVIWSASVER PSEREFQEPS QLLEAIAADD KEVSPSILYA AAAVLEGCSF VNGGSQNTMC
GALLKLAEDN ACYMLGTDFK AGQTKFKTAA VEYIRSLGMC PKVIASSNHL GNNDMLNLTT
KKTLGAKMRV KSNIFAPWEE DINHEVRVMY TPLMGDEKRD IVEYTSFGFM NCAHTMLTYT
RAMDSALCVP LMIDAAVWCD YFARAGAHQG SVARALAYLF KVPEGGAQGV DPGFFKQMRA
LEEELEATRL GSVEAAAASP GGASAVGGML VGRVLCAGIS CLDLQLCGSG GGGEGGVETI
RKFKETKYCP GGSCPQASTA LARLGVPGVV AVTKMGADAH GDEMVRQMLA AGVDCSRVIR
DASVQTALAV LPIFSSGERG CFVNLAANDD LLGDEVAAVL KEVAAEDGPP LAAFHYGYPH
FTKQIQGQAL ADVLRLPRSL PGSPLVSLDL NGVDPGNDAP TRHAAVLEKA YPFVDILHAN
LEEAEAIVGP LETGDGDARL RALAEWFLSK GVAVVAITAG AKGSFTAVTS DAERLAASPG
LARQVSAWAG REVRAAAFAA GEGAAVNANG AGDAFVGGLV LAAAAWRESL SLEEAVRFAA
LAALQRVDES LRQAEDATNA AELMTVARAG SLPPTLPLS
//
