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Database: UniProt
Entry: R5CTM2_9BACT
LinkDB: R5CTM2_9BACT
Original site: R5CTM2_9BACT 
ID   R5CTM2_9BACT            Unreviewed;       434 AA.
AC   R5CTM2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE            EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN   ORFNames=BN458_00424 {ECO:0000313|EMBL:CCX67001.1};
OS   Prevotella sp. CAG:1058.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262918 {ECO:0000313|EMBL:CCX67001.1, ECO:0000313|Proteomes:UP000018314};
RN   [1] {ECO:0000313|EMBL:CCX67001.1, ECO:0000313|Proteomes:UP000018314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1058 {ECO:0000313|Proteomes:UP000018314};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CCX67001.1}.
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DR   EMBL; CAWU010000171; CCX67001.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CTM2; -.
DR   STRING; 1262918.BN458_00424; -.
DR   Proteomes; UP000018314; 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   Reference proteome {ECO:0000313|Proteomes:UP000018314};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          250..362
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   434 AA;  48898 MW;  F5A7D0964CA51B1B CRC64;
     MDKNSVKPSE GKLGILCVGL GAVSSTFITG VLMIRKGMGK PIGSITQMAK IRVGRGDKAE
     YKHVSEIVPM PTLDDIVFGA WDILPDNAFE SAMHAEVLKD RDIYPVKEEL EKIVPMRGIY
     DQDYVKAIDG TWTKDTTLTR WQLMEQARED IRNFKEKNGC SRIVVIWAAS TEIYIPRDKN
     VHDDLTAFEA AMKADDRQHI SPSMCYAYAA MSEGAPFIMG APNTCLDIPA MWQYAEKTGT
     PIAGKDFKTG QTMMKTVLST AFRTRMLGVS GWFSTNILGN RDGLVLDVPE NFKTKEVSKL
     GVIDTILKKD EYPDLYGDIF HKVRINYYPP RNDDKEGWDN IDIFGWMGYP MQIKVDFLCK
     DSILAAPLLL DLALLGDLAL RAGKSGIQTW LSFYLKSPMH DDEHEPVHDL FQQYTMLKNA
     IREMGGYEAD EEID
//
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