ID   INO1B_XENLA             Reviewed;         563 AA.
AC   Q6DDT1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Inositol-3-phosphate synthase 1-B;
DE            Short=IPS 1-B;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol 1-phosphate synthase B;
DE            Short=MI-1-P synthase B;
DE            Short=MIP synthase B;
GN   Name=isyna1-b; Synonyms=ino1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that
CC       catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-
CC       phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC       synthesis of all inositol-containing compounds (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH77437.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC077437; AAH77437.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001086783.2; NM_001093314.1.
DR   RefSeq; XP_018101999.1; XM_018246510.1.
DR   RefSeq; XP_018102005.1; XM_018246516.1.
DR   AlphaFoldDB; Q6DDT1; -.
DR   SMR; Q6DDT1; -.
DR   MaxQB; Q6DDT1; -.
DR   DNASU; 446618; -.
DR   GeneID; 446618; -.
DR   KEGG; xla:446618; -.
DR   CTD; 446618; -.
DR   Xenbase; XB-GENE-6255674; isyna1.L.
DR   OMA; EHDLFIQ; -.
DR   OrthoDB; 451916at2759; -.
DR   UniPathway; UPA00823; UER00787.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446618; Expressed in kidney and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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; PTHR11510; 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; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..563
FT                   /note="Inositol-3-phosphate synthase 1-B"
FT                   /id="PRO_0000324633"
SQ   SEQUENCE   563 AA;  62383 MW;  CC7ADB09CAC3DAD0 CRC64;
     MAEMFKVESP HVRYLKDVIE ADYSYDTTQV YEEKGVTKVK PCSTKFTFHT ERKVPKLGVM
     LVGWGGNNGT TVTAAVLANR LGLSWMTKTG KKVANYYGSL FQSSTVCLGR GSSGEVFVPF
     RDLLPMVNPN DLVFDGWDIS SLNLADAMFR AEVLDWQLQE QLRPYMEKMK PRPSIYIPEF
     IAANQEDRAD HTIHGTKAEQ VQKIREDIQD FKRTSGVDKV IVLWTANTER FCDIIPGVND
     TADNLLKAIE NGLEVSPSTM FAVASILEGC AFINGSPQNT FVPGAIELAI RHNVFIGGDD
     FKSGQTKIKS VLMDFLVSAG LKPVSIVSYN HLGNNDGKNL SAPQQFRSKE ISKSNVVDDM
     VQSNPILYGP NEKPDHCVVI KYVPYVGDSK RAMDEYTSEI MMGGANTIVL HNTCEDSLLA
     SPIFLDLVLL TELCQRITFR TETDQEFQTF HSVLSILSFL CKAPLVPAGT PVVNAFFRQR
     NCIENILRAC LGLSPQNHMM LEHKMQRSFV SLKRPSVDCN AYPISSKKGN GVNGFHPPGI
     SNGLSHSNGL GKTVISSDIE IEN