ID Q5KJI4_CRYNJ Unreviewed; 558 AA.
AC Q5KJI4; Q55WR3;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN OrderedLocusNames=CNC06440 {ECO:0000313|EMBL:AAW42593.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW42593.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW42593.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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 EMBL; AE017343; AAW42593.1; -; Genomic_DNA.
DR RefSeq; XP_569900.1; XM_569900.1.
DR AlphaFoldDB; Q5KJI4; -.
DR STRING; 214684.Q5KJI4; -.
DR PaxDb; 214684-Q5KJI4; -.
DR EnsemblFungi; AAW42593; AAW42593; CNC06440.
DR GeneID; 3256678; -.
DR KEGG; cne:CNC06440; -.
DR VEuPathDB; FungiDB:CNC06440; -.
DR eggNOG; KOG0693; Eukaryota.
DR HOGENOM; CLU_021486_2_0_1; -.
DR InParanoid; Q5KJI4; -.
DR OMA; VPKVGMM; -.
DR OrthoDB; 1201882at2759; -.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000002149; Chromosome 3.
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:UP000002149}.
FT DOMAIN 342..469
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 61231 MW; AFD236EEB5F1D253 CRC64;
MSPTALDARG HNDSFSLPAQ DQSEVHPSAR RTPEGGLIKV ESDSTVYEAD GIKAKFTDRG
ASVIKGPDGK LSVKKTEKNF EFFTKSKVGR VGLMLVGLGG NNGTTVLATN LANKHNISWH
TKNGIQQPNY IGSVVRASTV RLGTDPATGK DVFVPISDML PMVHPNDFVI GGWDISSLSM
DKAMLRAKVL EWDLQRQLIP LMEDVKPLPS IYYPDFIAAN QADRADNLIP GGDKKAHLEH
IRADIRRFKA DNHLDSVVVL WTANTERYAD IIPGVNDTAN NLLKAVETSH EEVSPSTIFA
IASILEGVPF INGSPQNTFV PGCIELAEKH KAFIGGDDFK SGQTKVKSVL AEFLVNAGIK
PLSISSYNHL GNNDGKNLSS QRQFRSKEIS KSSVVDDMVA ANHILYKTAE DLSKATGEVV
KKGEHPDHIV VIKHVPAVGD SKRAIDEYYS ELLMGGRNVM NIFNECEDSL LATPLIFDLA
ILAELLTRVT YRENATGEWQ PLYSVLSLLS YMLKAPLVKP GEDVVNSLNR QRNALEQFLK
ACLGLEHSND LLLNTRVW
//
