MSHA_MYCLE
ID MSHA_MYCLE Reviewed; 428 AA.
AC P54138; Q9CB50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=D-inositol 3-phosphate glycosyltransferase;
DE EC=2.4.1.250;
DE AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase;
DE Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase;
GN Name=mshA; OrderedLocusNames=ML2443; ORFNames=B2168_C2_201, u2168f;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to
CC 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-
CC deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis
CC pathway. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine
CC = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-
CC phosphate + H(+) + UDP; Xref=Rhea:RHEA:26188, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:58892; EC=2.4.1.250;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17228.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00018; AAA17228.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583925; CAC31960.1; -; Genomic_DNA.
DR PIR; H87214; H87214.
DR PIR; S72892; S72892.
DR RefSeq; NP_302584.1; NC_002677.1.
DR RefSeq; WP_010908903.1; NC_002677.1.
DR AlphaFoldDB; P54138; -.
DR SMR; P54138; -.
DR STRING; 272631.ML2443; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; CAC31960; CAC31960; CAC31960.
DR KEGG; mle:ML2443; -.
DR PATRIC; fig|272631.5.peg.4690; -.
DR Leproma; ML2443; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_3_11; -.
DR OMA; HTMAKVK; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102710; F:D-inositol-3-phosphate glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01695; MshA; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR017814; Mycothiol_biosynthesis_MshA.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR03449; mycothiol_MshA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..428
FT /note="D-inositol 3-phosphate glycosyltransferase"
FT /id="PRO_0000080320"
FT BINDING 5
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 11..12
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 16..21
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 428 AA; 45292 MW; A14F9F0187E3587C CRC64;
MLAVHTSPLA QPGIGDAGGM NVYVLQSALH LARRGIEVEI FTRATASADP PIVWVAPGVL
VRNVVAGPFE GLDKYDLPTQ LCAFAAGVLR AEAAHEPGYY DIVHSHYWLS GQVGWLARDR
WAVPLVHTAH TLAAVKNAAL ADGDAAEPPL RSVGEQQVVD EADRMIVNTD DEARQLISIH
RADPAKIDVA HPGVDLDMFR PGDRRAARAA LGLPLDGNVV AFVGRIQPLK APDIVLRAAA
KLPQVRIVVA GGPSGSGLAS PDGLVRLADE LGITARVTFL PPQSRTNLAT VFQAADLVAV
PSYSESFGLV AVEAQACGTP VVAAAVGGLP VAVRDGVTGT LVFGHNVGHW ADAVDQLLRL
SAGPQARAIS RAAVVHAAQF SWDNTTDALL ASYRRAIGDF TATRQHRVRD LVATRKPRRW
ISRRGMGA
