ID   INO1_MYCS2              Reviewed;         363 AA.
AC   A0R7G6; I7GGA1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Inositol-3-phosphate synthase;
DE            Short=IPS;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol 1-phosphate synthase;
DE            Short=MI-1-P synthase;
DE            Short=MIP synthase;
GN   Name=ino1; OrderedLocusNames=MSMEG_6904, MSMEI_6720;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PROTEASOME SUBSTRATE, PUPYLATION AT LYS-65, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19028679; DOI=10.1074/jbc.m808032200;
RA   Burns K.E., Liu W.-T., Boshoff H.I.M., Dorrestein P.C., Barry C.E. III;
RT   "Proteasomal protein degradation in mycobacteria is dependent upon a
RT   prokaryotic ubiquitin-like protein.";
RL   J. Biol. Chem. 284:3069-3075(2009).
RN   [5]
RP   PUPYLATION AT LYS-65, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- FUNCTION: Catalyzes the conversion of glucose 6-phosphate to 1D-myo-
CC       inositol 3-phosphate. {ECO:0000250}.
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   -!- PTM: Pupylated at Lys-65 by the prokaryotic ubiquitin-like protein Pup,
CC       which leads to its degradation by the proteasome.
CC       {ECO:0000269|PubMed:19028679, ECO:0000269|PubMed:20094657}.
CC   -!- MISCELLANEOUS: Was identified as a natural substrate of the M.smegmatis
CC       proteasome.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK72827.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP43146.1; -; Genomic_DNA.
DR   RefSeq; WP_011731620.1; NZ_SIJM01000001.1.
DR   RefSeq; YP_891104.1; NC_008596.1.
DR   AlphaFoldDB; A0R7G6; -.
DR   SMR; A0R7G6; -.
DR   STRING; 246196.MSMEI_6720; -.
DR   PRIDE; A0R7G6; -.
DR   EnsemblBacteria; ABK72827; ABK72827; MSMEG_6904.
DR   EnsemblBacteria; AFP43146; AFP43146; MSMEI_6720.
DR   GeneID; 66738158; -.
DR   KEGG; msg:MSMEI_6720; -.
DR   KEGG; msm:MSMEG_6904; -.
DR   PATRIC; fig|246196.19.peg.6725; -.
DR   eggNOG; COG1260; Bacteria.
DR   OMA; GTKEWAD; -.
DR   OrthoDB; 669352at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR   InterPro; IPR017815; Myo-inos-1-P_Synthase_actino.
DR   InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01658; Inos-1-P_synth; 1.
DR   PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03450; mycothiol_INO1; 1.
PE   1: Evidence at protein level;
KW   Inositol biosynthesis; Isomerase; Isopeptide bond; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..363
FT                   /note="Inositol-3-phosphate synthase"
FT                   /id="PRO_0000383479"
FT   CROSSLNK        65
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:19028679,
FT                   ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   363 AA;  39300 MW;  931F94699B6C8BD4 CRC64;
     MSEHAGEIRV AIVGVGNCAS SLVQGVQYYR NADENTTVPG LMHVKFGPYH VRDVNFVAAF
     DVDAKKVGFD LSEAIFASEN NTIKIADVPP TDVIVQRGPT LDGIGKYYAD TIEVSDAEPV
     DVVKVLKEAE VDVLVSYLPV GSEEADKFYA QCAIDAGVAF VNALPVFIAS DPVWAKKFED
     AGVPIVGDDI KSQVGATITH RVMAKLFEDR GVTLDRTYQL NVGGNMDFLN MLERSRLESK
     KVSKTQAVTS NLSGALAGKV EDKNVHIGPS DHVAWLDDRK WAYVRLEGRA FGDVPLNLEY
     KLEVWDSPNS AGVIIDAVRA AKIAKDRGIG GPIEAASAYL MKSPPKQLAD DVARAELETF
     IEG