ID A0A286A874_9SPHI Unreviewed; 437 AA.
AC A0A286A874;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN ORFNames=SAMN06297358_2835 {ECO:0000313|EMBL:SOD18116.1};
OS Pedobacter xixiisoli.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD18116.1, ECO:0000313|Proteomes:UP000219281};
RN [1] {ECO:0000313|EMBL:SOD18116.1, ECO:0000313|Proteomes:UP000219281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD18116.1,
RC ECO:0000313|Proteomes:UP000219281};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; OCMT01000003; SOD18116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286A874; -.
DR OrthoDB; 729130at2; -.
DR Proteomes; UP000219281; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
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 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..358
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
SQ SEQUENCE 437 AA; 48874 MW; C19E7EFAA5BE58DC CRC64;
MKKQVEGANG KLGIMMPGLG AVATTMIAGV VAARRGLSKP IGSLTQMGTI RVGKRTDNNE
PLIKDFVPLA KLEDLAFGGW DVYEDNVYDA AMKAKVIDGH LLYDIKDELE AIKPYKAAFD
KNYVKNLDGT YVKEAATKWE LAQQVIEDIK DFKAKNNCER IVLVWCGSTE IYLEPSAVHQ
TLAAFEQGLK DNDALIAPSM IYAYAALKLG YAYANGAPNL TVDIPAMLEL AKETQTPVAG
KDFKTGQTLM KTVLAPGLMA RSLGVRGWFS DNILGNRDGL VLDDPDNFKT KEVSKLGVLE
DIFKPEQNPD LYGDMYHKIR INYYPPHGDN KESWDNIDIF GWMGYKMQIK INFLCRDSIL
AAPIVLDLAL FSDLAKRAGM SGIQEWLSFY LKSPQTKEGL RPENDIFKQL EKLHNTLRYF
MGEELITHLG LDYYDEN
//
