INO1_MYCTU
ID INO1_MYCTU Reviewed; 367 AA.
AC P9WKI1; L0T457; P71703;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=Rv0046c; ORFNames=MTCY21D4.09c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEASOME SUBSTRATE, PUPYLATION AT LYS-73, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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-73 by the prokaryotic ubiquitin-like protein Pup,
CC which leads to its degradation by the proteasome.
CC {ECO:0000269|PubMed:20066036}.
CC -!- MISCELLANEOUS: Was identified as a natural substrate of the
CC M.tuberculosis proteasome.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42768.1; -; Genomic_DNA.
DR PIR; F70912; F70912.
DR RefSeq; NP_214560.1; NC_000962.3.
DR RefSeq; WP_003902822.1; NZ_NVQJ01000005.1.
DR PDB; 1GR0; X-ray; 1.95 A; A=1-367.
DR PDBsum; 1GR0; -.
DR AlphaFoldDB; P9WKI1; -.
DR SMR; P9WKI1; -.
DR STRING; 83332.Rv0046c; -.
DR iPTMnet; P9WKI1; -.
DR PaxDb; P9WKI1; -.
DR DNASU; 887028; -.
DR GeneID; 887028; -.
DR KEGG; mtu:Rv0046c; -.
DR TubercuList; Rv0046c; -.
DR eggNOG; COG1260; Bacteria.
DR OMA; GTKEWAD; -.
DR PhylomeDB; P9WKI1; -.
DR BioCyc; MetaCyc:G185E-4160-MON; -.
DR Reactome; R-MTU-879299; Mycothiol biosynthesis.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IMP:MTBBASE.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR GO; GO:0006021; P:inositol biosynthetic process; IMP:MTBBASE.
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 3D-structure; Acetylation; Inositol biosynthesis; Isomerase;
KW Isopeptide bond; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..367
FT /note="Inositol-3-phosphate synthase"
FT /id="PRO_0000195203"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CROSSLNK 73
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1GR0"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1GR0"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 283..294
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 298..309
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 312..330
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:1GR0"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1GR0"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:1GR0"
SQ SEQUENCE 367 AA; 40094 MW; 3976AA08452183F9 CRC64;
MSEHQSLPAP EASTEVRVAI VGVGNCASSL VQGVEYYYNA DDTSTVPGLM HVRFGPYHVR
DVKFVAAFDV DAKKVGFDLS DAIFASENNT IKIADVAPTN VIVQRGPTLD GIGKYYADTI
ELSDAEPVDV VQALKEAKVD VLVSYLPVGS EEADKFYAQC AIDAGVAFVN ALPVFIASDP
VWAKKFTDAR VPIVGDDIKS QVGATITHRV LAKLFEDRGV QLDRTMQLNV GGNMDFLNML
ERERLESKKI SKTQAVTSNL KREFKTKDVH IGPSDHVGWL DDRKWAYVRL EGRAFGDVPL
NLEYKLEVWD SPNSAGVIID AVRAAKIAKD RGIGGPVIPA SAYLMKSPPE QLPDDIARAQ
LEEFIIG
