INO1_YEAST
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 03-AUG-2022, entry version 191.
DE RecName: Full=Inositol-3-phosphate synthase;
DE Short=MIP synthase;
DE EC=5.5.1.4;
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 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
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).
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;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; 98.
DR DIP; DIP-5687N; -.
DR IntAct; P11986; 28.
DR MINT; P11986; -.
DR STRING; 4932.YJL153C; -.
DR iPTMnet; P11986; -.
DR MaxQB; P11986; -.
DR PaxDb; P11986; -.
DR PRIDE; P11986; -.
DR EnsemblFungi; YJL153C_mRNA; YJL153C; YJL153C.
DR GeneID; 853288; -.
DR KEGG; sce:YJL153C; -.
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; EHDLFIQ; -.
DR BioCyc; YEAST:YJL153C-MON; -.
DR Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; P11986; -.
DR UniPathway; UPA00823; UER00787.
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 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; PTHR11510; 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; SSF51735; SSF51735; 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 MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
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
