ID C4YCE8_CLAL4 Unreviewed; 517 AA.
AC C4YCE8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN ORFNames=CLUG_05787 {ECO:0000313|EMBL:EEQ41659.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ41659.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ41659.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ41659.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408083; EEQ41659.1; -; Genomic_DNA.
DR RefSeq; XP_002614301.1; XM_002614255.1.
DR AlphaFoldDB; C4YCE8; -.
DR STRING; 306902.C4YCE8; -.
DR GeneID; 8494829; -.
DR KEGG; clu:CLUG_05787; -.
DR VEuPathDB; FungiDB:CLUG_05787; -.
DR HOGENOM; CLU_021486_2_0_1; -.
DR InParanoid; C4YCE8; -.
DR OMA; VPKVGMM; -.
DR OrthoDB; 1201882at2759; -.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000007703; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT DOMAIN 313..428
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
SQ SEQUENCE 517 AA; 57513 MW; C9FEA0C543BC9E90 CRC64;
MSVDFNTNAV SKDGALYTKF TYESATVEKQ ANGKLSVTPT ATEYEFKVDL SVPKTGLMLV
GLGGNNGTTM VAATLANKHN ISFENKECVV KPNYYGSVTQ SSTIKLGVDK EGNDVYAPFN
SILPFVHPND LVIGGWDISK LPLDKAMKRA KVLDHDLQRQ LVQHMDKIVP LPSVYYPDFI
AMNQKERADN VFNVDKEGNV TTGDKWKDVE RIRSDIQKFK KENGLDKVIV LWTANTERYS
DILSGVNDTA DNLLKAIKDN HDEVSPSTVF AVACILEQVP YINGSPQNTF VPGAIELAEK
HQSFIGGDDF KSGQTKVKSV LAQFLVDAGI KPLSIASYNH LGNNDGFNLS APKQFRSKEI
SKQSVVDDMI ESNEILYNEE TGNKVDHCIV IKYLPAVGDS KVAMDEYYSE LMLGGHNKIS
IHNVCEDSLL ATPLIIDLVV MTEFFQRVTY KKVGSDKYES FYSVLTLLSY WLKAPLAKPG
FKAINGLNKQ RLAVENLLRL LVGMPINNEL RFEERLV
//
