ID   INO1_YEAST              Reviewed;         533 AA.
AC   P11986; D6VW34;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Inositol-3-phosphate synthase;
DE            Short=MIP synthase {ECO:0000303|PubMed:11779862};
DE            EC=5.5.1.4 {ECO:0000269|PubMed:14684747, ECO:0000269|PubMed:23902760, ECO:0000269|Ref.6, ECO:0000269|Ref.8};
DE   AltName: Full=Myo-inositol 1-phosphate synthase;
DE            Short=IPS;
DE            Short=MI-1-P synthase;
GN   Name=INO1; OrderedLocusNames=YJL153C; ORFNames=J0610;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 204510 / AB320;
RX   PubMed=2642902; DOI=10.1016/s0021-9258(19)85082-2;
RA   Dean-Johnson M., Henry S.A.;
RT   "Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-
RT   phosphate synthase (EC 5.5.1.4) and functional analysis of its structural
RT   gene, the INO1 locus.";
RL   J. Biol. Chem. 264:1274-1283(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AB322;
RX   PubMed=7975896; DOI=10.1002/yea.320100609;
RA   Klig L.S., Zobel P.A., Devry C.G., Losberger C.;
RT   "Comparison of INO1 gene sequences and products in Candida albicans and
RT   Saccharomyces cerevisiae.";
RL   Yeast 10:789-800(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8813765;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA   Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT   "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT   chromosome X reveals 14 known genes and 13 new open reading frames
RT   including homologues of genes clustered on the right arm of chromosome
RT   XI.";
RL   Yeast 12:787-797(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   DOI=10.1021/ja952570i;
RA   Migaud M.E., Frost J.W.;
RT   "Elaboration of a general strategy for inhibition of myo-Inositol 1-
RT   Phosphate Synthase: active site interactions of analogues possessing
RT   oxidized reaction centers.";
RL   J. Am. Chem. Soc. 118:495-501(1996).
RN   [7]
RP   INDUCTION.
RX   PubMed=9294443; DOI=10.1128/jb.179.18.5843-5848.1997;
RA   Griac P.;
RT   "Regulation of yeast phospholipid biosynthetic genes in phosphatidylserine
RT   decarboxylase mutants.";
RL   J. Bacteriol. 179:5843-5848(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   DOI=10.1021/ja9900196;
RA   Tian F., Migaud M.E., Frost J.W.;
RT   "myo-Inositol 1-phosphate synthase: does a single active-site amino acid
RT   catalyze multiple proton transfers?";
RL   J. Am. Chem. Soc. 121:5795-5796(1999).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [10]
RP   INDUCTION.
RX   PubMed=15576064; DOI=10.1016/j.biopsych.2004.08.027;
RA   Shaltiel G., Shamir A., Shapiro J., Ding D., Dalton E., Bialer M.,
RA   Harwood A.J., Belmaker R.H., Greenberg M.L., Agam G.;
RT   "Valproate decreases inositol biosynthesis.";
RL   Biol. Psychiatry 56:868-874(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY,
RP   DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-48; SER-177; SER-184; SER-296
RP   AND SER-374, AND MUTAGENESIS OF SER-184; SER-296 AND SER-374.
RX   PubMed=23902760; DOI=10.1074/jbc.m113.479121;
RA   Deranieh R.M., He Q., Caruso J.A., Greenberg M.L.;
RT   "Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel
RT   regulatory mechanism of inositol biosynthesis.";
RL   J. Biol. Chem. 288:26822-26833(2013).
RN   [13] {ECO:0007744|PDB:1LA2}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH NAD(+), COFACTOR,
RP   AND SUBUNIT.
RX   PubMed=12836703; DOI=10.1023/a:1021293408654;
RA   Kniewel R., Buglino J.A., Shen V., Chadha T., Beckwith A., Lima C.D.;
RT   "Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate
RT   synthase.";
RL   J. Struct. Funct. Genomics 2:129-134(2002).
RN   [14] {ECO:0007744|PDB:1JKF, ECO:0007744|PDB:1JKI}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADH AND INHIBITOR,
RP   COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=11779862; DOI=10.1074/jbc.m109371200;
RA   Stein A.J., Geiger J.H.;
RT   "The crystal structure and mechanism of 1-L-myo-inositol- 1-phosphate
RT   synthase.";
RL   J. Biol. Chem. 277:9484-9491(2002).
RN   [15] {ECO:0007744|PDB:1P1F, ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I, ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADH, AND COFACTOR.
RX   PubMed=12832758; DOI=10.1107/s0907444903008205;
RA   Jin X., Geiger J.H.;
RT   "Structures of NAD(+)- and NADH-bound 1-l-myo-inositol 1-phosphate
RT   synthase.";
RL   Acta Crystallogr. 59:1154-1164(2003).
RN   [16] {ECO:0007744|PDB:1RM0}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NADH AND INHIBITOR,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF LYS-369; LYS-412 AND LYS-489.
RX   PubMed=14684747; DOI=10.1074/jbc.m308986200;
RA   Jin X., Foley K.M., Geiger J.H.;
RT   "The structure of the 1L-myo-inositol-1-phosphate synthase-NAD+-2-deoxy-D-
RT   glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the
RT   enzyme mechanism.";
RL   J. Biol. Chem. 279:13889-13895(2004).
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 (Ref.6, Ref.8, PubMed:23902760,
CC       PubMed:14684747). Rate-limiting enzyme in the synthesis of all
CC       inositol-containing compounds (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NPH2, ECO:0000269|PubMed:14684747,
CC       ECO:0000269|PubMed:23902760, ECO:0000269|Ref.6, ECO:0000269|Ref.8}.
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:0000269|PubMed:14684747,
CC         ECO:0000269|PubMed:23902760, ECO:0000269|Ref.6, ECO:0000269|Ref.8};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12832758,
CC         ECO:0000269|PubMed:12836703, ECO:0000269|PubMed:14684747,
CC         ECO:0000269|Ref.6};
CC   -!- ACTIVITY REGULATION: Competitively inhibited by myo-2-inosose 1-
CC       phosphate, which is also an intermediate in the catalytic reaction
CC       (Ref.6). Competitively inhibited by 2-deoxy-myo-inositol 1-phosphate
CC       (dMIP), 1-deoxy-1-(phosphonomethyl)-myo-2-inosose (DPMI),
CC       dihydroxyacetone phosphate (DHAP), 6-deoxy-D-glucose 6-(E)-
CC       vinylhomophosphonate, 6-deoxy-D-glucitol 6-(E)-vinylhomophosphonate,
CC       2,6-dideoxy-D-glucose 6-(E)-vinylhomophosphonate and 2,6-dideoxy-D-
CC       glucitol 6-(E)-vinylhomophosphonate (Ref.6, Ref.8). Inhibited by 2-
CC       deoxyglucitol 6-phosphate (dgtolP) (Probable). {ECO:0000269|Ref.6,
CC       ECO:0000269|Ref.8, ECO:0000305|PubMed:11779862}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.2 mM for D-glucose 6-phosphate (at 37 degrees Celsius and pH
CC         7.2) {ECO:0000269|Ref.6};
CC         KM=17 uM for NAD (at 37 degrees Celsius and pH 7.2)
CC         {ECO:0000269|Ref.6};
CC       pH dependence:
CC         Optimum pH is 7.2-7.7. {ECO:0000269|PubMed:14684747};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11779862,
CC       ECO:0000269|PubMed:12836703}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Induced by valproate (PubMed:15576064). Repressed by
CC       inositol (PubMed:9294443, PubMed:15576064).
CC       {ECO:0000269|PubMed:15576064, ECO:0000269|PubMed:9294443}.
CC   -!- PTM: Phosphorylation at Ser-184 and Ser-374 is associated with a
CC       decrease in activity (PubMed:23902760). Increasingly phosphorylated in
CC       presence of valproate (PubMed:23902760). {ECO:0000269|PubMed:23902760}.
CC   -!- DISRUPTION PHENOTYPE: Inositol auxotrophy.
CC       {ECO:0000269|PubMed:23902760}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA60802.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA89448.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L23520; AAA34706.1; -; Genomic_DNA.
DR   EMBL; J04453; AAA66310.1; -; Genomic_DNA.
DR   EMBL; X87371; CAA60802.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z49428; CAA89448.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006943; DAA08650.1; -; Genomic_DNA.
DR   PIR; S55160; A30902.
DR   RefSeq; NP_012382.2; NM_001181586.1.
DR   PDB; 1JKF; X-ray; 2.40 A; A/B=1-533.
DR   PDB; 1JKI; X-ray; 2.20 A; A/B=1-533.
DR   PDB; 1LA2; X-ray; 2.65 A; A/B/C/D=1-533.
DR   PDB; 1P1F; X-ray; 2.60 A; A/B=1-533.
DR   PDB; 1P1H; X-ray; 1.95 A; A/B/C/D=1-533.
DR   PDB; 1P1I; X-ray; 2.40 A; A/B=1-533.
DR   PDB; 1P1J; X-ray; 1.70 A; A/B=1-533.
DR   PDB; 1P1K; X-ray; 2.10 A; A/B=1-533.
DR   PDB; 1RM0; X-ray; 2.05 A; A/B=1-533.
DR   PDBsum; 1JKF; -.
DR   PDBsum; 1JKI; -.
DR   PDBsum; 1LA2; -.
DR   PDBsum; 1P1F; -.
DR   PDBsum; 1P1H; -.
DR   PDBsum; 1P1I; -.
DR   PDBsum; 1P1J; -.
DR   PDBsum; 1P1K; -.
DR   PDBsum; 1RM0; -.
DR   AlphaFoldDB; P11986; -.
DR   SMR; P11986; -.
DR   BioGRID; 33607; 103.
DR   DIP; DIP-5687N; -.
DR   IntAct; P11986; 28.
DR   MINT; P11986; -.
DR   STRING; 4932.YJL153C; -.
DR   iPTMnet; P11986; -.
DR   MaxQB; P11986; -.
DR   PaxDb; 4932-YJL153C; -.
DR   PeptideAtlas; P11986; -.
DR   EnsemblFungi; YJL153C_mRNA; YJL153C; YJL153C.
DR   GeneID; 853288; -.
DR   KEGG; sce:YJL153C; -.
DR   AGR; SGD:S000003689; -.
DR   SGD; S000003689; INO1.
DR   VEuPathDB; FungiDB:YJL153C; -.
DR   eggNOG; KOG0693; Eukaryota.
DR   GeneTree; ENSGT00390000018395; -.
DR   HOGENOM; CLU_021486_2_0_1; -.
DR   InParanoid; P11986; -.
DR   OMA; VPKVGMM; -.
DR   OrthoDB; 1201882at2759; -.
DR   BioCyc; YEAST:YJL153C-MONOMER; -.
DR   Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR   SABIO-RK; P11986; -.
DR   UniPathway; UPA00823; UER00787.
DR   BioGRID-ORCS; 853288; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P11986; -.
DR   PRO; PR:P11986; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P11986; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0006021; P:inositol biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Inositol biosynthesis;
KW   Isomerase; Lipid biosynthesis; Lipid metabolism; NAD;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..533
FT                   /note="Inositol-3-phosphate synthase"
FT                   /id="PRO_0000195185"
FT   BINDING         74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12836703, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1LA2"
FT   BINDING         75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1I, ECO:0007744|PDB:1P1J,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:14684747,
FT                   ECO:0007744|PDB:1JKF, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1I, ECO:0007744|PDB:1P1J,
FT                   ECO:0007744|PDB:1P1K, ECO:0007744|PDB:1RM0"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12832758,
FT                   ECO:0000269|PubMed:12836703, ECO:0000269|PubMed:14684747,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0007744|PDB:1JKF"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0007744|PDB:1JKF"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12832758,
FT                   ECO:0000269|PubMed:12836703, ECO:0000269|PubMed:14684747,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12836703,
FT                   ECO:0007744|PDB:1LA2"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:14684747,
FT                   ECO:0007744|PDB:1JKF, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1K, ECO:0007744|PDB:1RM0"
FT   BINDING         247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1I,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1P1H"
FT   BINDING         296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1I, ECO:0007744|PDB:1P1J,
FT                   ECO:0007744|PDB:1P1K, ECO:0007744|PDB:1RM0"
FT   BINDING         320
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1P1H"
FT   BINDING         321
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0007744|PDB:1JKF"
FT   BINDING         323
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKF,
FT                   ECO:0007744|PDB:1P1J"
FT   BINDING         354
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12832758,
FT                   ECO:0000269|PubMed:12836703, ECO:0007744|PDB:1LA2,
FT                   ECO:0007744|PDB:1P1H"
FT   BINDING         355
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1I, ECO:0007744|PDB:1P1J,
FT                   ECO:0007744|PDB:1P1K, ECO:0007744|PDB:1RM0"
FT   BINDING         356
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         369
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12832758,
FT                   ECO:0000269|PubMed:14684747, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         409
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0007744|PDB:1JKF"
FT   BINDING         410
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0007744|PDB:1JKI"
FT   BINDING         438
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:12832758,
FT                   ECO:0000269|PubMed:12836703, ECO:0000269|PubMed:14684747,
FT                   ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H,
FT                   ECO:0007744|PDB:1P1J, ECO:0007744|PDB:1P1K,
FT                   ECO:0007744|PDB:1RM0"
FT   BINDING         439
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:11779862,
FT                   ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKI,
FT                   ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1K"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:23902760"
FT   MUTAGEN         184
FT                   /note="S->D: Decreases activity. Inositol auxotrophy."
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MUTAGEN         296
FT                   /note="S->A,D: Decreases activity. Inositol auxotrophy."
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MUTAGEN         369
FT                   /note="K->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:14684747"
FT   MUTAGEN         374
FT                   /note="S->D: Decreases activity. Inositol auxotrophy."
FT                   /evidence="ECO:0000269|PubMed:23902760"
FT   MUTAGEN         412
FT                   /note="K->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:14684747"
FT   MUTAGEN         489
FT                   /note="K->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:14684747"
FT   CONFLICT        14
FT                   /note="V -> RL (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="L -> FE (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66..93
FT                   /note="LGIMLIGLGGNNGSTLVASVLANKHNVE -> TRNYAHWVRWLQQWLTLWPR
FT                   YWRISTMWS (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="E -> AK (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140..141
FT                   /note="ND -> KH (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="N -> Q (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444
FT                   /note="P -> A (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476..497
FT                   /note="NFYPVLTFLSYWLKAPLTRPGF -> ELLSSFNLLELLVKSSINKNQDL
FT                   (in Ref. 1; AAA66310)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        524..533
FT                   /note="NELRFEERLL -> KRTKIRREIVVISFQRLSFSFSAYL (in Ref. 1;
FT                   AAA34706)"
FT                   /evidence="ECO:0000305"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          25..39
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          43..59
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           76..89
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          114..119
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:1P1H"
FT   STRAND          125..129
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          142..147
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           154..161
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           166..176
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           193..198
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:1JKI"
FT   HELIX           216..233
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          258..260
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           261..269
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           277..287
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:1P1H"
FT   HELIX           303..312
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          316..321
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           325..338
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          342..352
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           355..360
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           363..375
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           378..382
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   TURN            385..387
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   TURN            390..392
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          397..404
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           406..408
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          411..421
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           423..425
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          427..437
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           438..457
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          459..463
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          466..468
FT                   /evidence="ECO:0007829|PDB:1P1H"
FT   HELIX           482..487
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   STRAND          488..490
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           503..517
FT                   /evidence="ECO:0007829|PDB:1P1J"
FT   HELIX           528..531
FT                   /evidence="ECO:0007829|PDB:1P1J"
SQ   SEQUENCE   533 AA;  59642 MW;  282E2AE5D156289D CRC64;
     MTEDNIAPIT SVKVVTDKCT YKDNELLTKY SYENAVVTKT ASGRFDVTPT VQDYVFKLDL
     KKPEKLGIML IGLGGNNGST LVASVLANKH NVEFQTKEGV KQPNYFGSMT QCSTLKLGID
     AEGNDVYAPF NSLLPMVSPN DFVVSGWDIN NADLYEAMQR SQVLEYDLQQ RLKAKMSLVK
     PLPSIYYPDF IAANQDERAN NCINLDEKGN VTTRGKWTHL QRIRRDIQNF KEENALDKVI
     VLWTANTERY VEVSPGVNDT MENLLQSIKN DHEEIAPSTI FAAASILEGV PYINGSPQNT
     FVPGLVQLAE HEGTFIAGDD LKSGQTKLKS VLAQFLVDAG IKPVSIASYN HLGNNDGYNL
     SAPKQFRSKE ISKSSVIDDI IASNDILYND KLGKKVDHCI VIKYMKPVGD SKVAMDEYYS
     ELMLGGHNRI SIHNVCEDSL LATPLIIDLL VMTEFCTRVS YKKVDPVKED AGKFENFYPV
     LTFLSYWLKA PLTRPGFHPV NGLNKQRTAL ENFLRLLIGL PSQNELRFEE RLL
//