ID A0A287AXJ7_PIG Unreviewed; 556 AA.
AC A0A287AXJ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Inositol-3-phosphate synthase 1 {ECO:0000256|ARBA:ARBA00017761};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
DE AltName: Full=Myo-inositol 1-phosphate synthase {ECO:0000256|ARBA:ARBA00032949};
GN Name=ISYNA1 {ECO:0000313|Ensembl:ENSSSCP00000048618.1,
GN ECO:0000313|VGNC:VGNC:99780};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000048618.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000048618.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000048618.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000048618.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A287AXJ7; -.
DR SMR; A0A287AXJ7; -.
DR STRING; 9823.ENSSSCP00000048618; -.
DR Ensembl; ENSSSCT00000059009.3; ENSSSCP00000048618.1; ENSSSCG00000040524.3.
DR VGNC; VGNC:99780; ISYNA1.
DR GeneTree; ENSGT00390000018395; -.
DR InParanoid; A0A287AXJ7; -.
DR Reactome; R-SSC-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000040524; Expressed in testis and 42 other cell types or tissues.
DR ExpressionAtlas; A0A287AXJ7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0006021; P:inositol biosynthetic process; IBA:GO_Central.
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:UP000008227}.
FT DOMAIN 307..420
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
SQ SEQUENCE 556 AA; 60784 MW; B56096C9AEC1876E CRC64;
MEAATEFVVE SPDVVYSPEA IEAKYEYRTT CVSREAGVLK VHPTSTRFTF RTARQVPRLG
VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR TGRKEANYYG SLTQAGTVSL GLDAEGQEVF
VPFSALLPMV APDDLVFDGW DISSLNLAEA MRRAQVLDWE LQEQLWPHME ALRPRPSVYI
PEFIAANQSA RADNLIPGTR AQQLEQIRRD IRDFRSNAGL DKVIVLWTAN TERFCEVVPG
LNDTADNLLR TIQLGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQRRVFVG
GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG QNLSAPPQFR SKEVSKSSVV
DDMVHSNPVL YKQGEEPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
LLAAPIMLDL ALLTELCQRV SFCTDADPEP QTFHPVLSLL SFLFKAPLAP PGSPVVNALF
RQRSCIENIL RACLGLPPQN HMLLEHKMER PGLKRVGLVT AACSLPCKKG PAPTTNGCTG
DANGHPQAEA PQMPTS
//
