ID A0A0G2IYT6_9EURO Unreviewed; 532 AA.
AC A0A0G2IYT6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN ORFNames=EMCG_04445 {ECO:0000313|EMBL:KKZ60854.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ60854.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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:KKZ60854.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCZI01001406; KKZ60854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2IYT6; -.
DR VEuPathDB; FungiDB:EMCG_04445; -.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000034164; Unassembled WGS sequence.
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; 3.40.50.720; 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}.
FT DOMAIN 330..443
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 58041 MW; E10031AC5B158A48 CRC64;
MAPHAEENAK GSLNGSVSTS TPSLFTVDSP NVVYTDEEIK TRYVYHTTAV TRAADGKYIA
APKESAYDFK VGRKVGKVGM MLVGWGGNNG TTVTAGIIAN RRGLVWNTRE GKRAANYYGS
VVMGSTVKLG TDPETAEEVN VPFYDMLPMV HPNDLAIGGW DISGMNIAEA MDRAQVLEPS
LKEMVRKEMA EMKPLPSIYY PDFIAANQED RADNVIEGSK ASWAHVERIQ QDIREFKAAN
GLDKVVVMWT ANTERYADII PGVNDTADNL LKAIKDGHEE VSPSTVFAVA SILENAPFIN
GSPQNTFVPG AIKFAEQHGA FIGGDDFKSG QTKMKSALVD FLINAGIKLT SIASYNHLGN
NDGKNLSSHK QFRSKEISKS NVVDDMVAAN SVLYKKGEHP DHTVVIKYMP AVGDNKRALD
EYYAEIFMGG HQTISMFNVC EDSLLASPLI IDLVLIAELM TRVSWKTASS DEYKGFHSVL
SVLSYMLKAP LTPPGTPVVN ALGKQRAAVT NIFRACVGLQ PESDMTLEHK LF
//