MSHA_MYCS2
ID MSHA_MYCS2 Reviewed; 434 AA.
AC A0QQZ8; I7F752;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=MSMEG_0933, MSMEI_0910;
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 FUNCTION.
RX PubMed=12754249; DOI=10.1128/jb.185.11.3476-3479.2003;
RA Newton G.L., Koledin T., Gorovitz B., Rawat M., Fahey R.C., Av-Gay Y.;
RT "The glycosyltransferase gene encoding the enzyme catalyzing the first step
RT of mycothiol biosynthesis (mshA).";
RL J. Bacteriol. 185:3476-3479(2003).
RN [5]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16940050; DOI=10.1074/jbc.m604724200;
RA Newton G.L., Ta P., Bzymek K.P., Fahey R.C.;
RT "Biochemistry of the initial steps of mycothiol biosynthesis.";
RL J. Biol. Chem. 281:33910-33920(2006).
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:0000269|PubMed:12754249}.
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 Evidence={ECO:0000269|PubMed:16940050};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for UDP-GlcNAc {ECO:0000269|PubMed:16940050};
CC KM=0.15 mM for 1D-inositol 3-phosphate {ECO:0000269|PubMed:16940050};
CC Vmax=0.7 nmol/min/mg enzyme {ECO:0000269|PubMed:16940050};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK76112.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37390.1; -; Genomic_DNA.
DR RefSeq; WP_011727296.1; NZ_SIJM01000010.1.
DR RefSeq; YP_885336.1; NC_008596.1.
DR AlphaFoldDB; A0QQZ8; -.
DR SMR; A0QQZ8; -.
DR STRING; 246196.MSMEI_0910; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; ABK76112; ABK76112; MSMEG_0933.
DR EnsemblBacteria; AFP37390; AFP37390; MSMEI_0910.
DR GeneID; 66739100; -.
DR KEGG; msg:MSMEI_0910; -.
DR KEGG; msm:MSMEG_0933; -.
DR PATRIC; fig|246196.19.peg.923; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; HTMAKVK; -.
DR OrthoDB; 694191at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..434
FT /note="D-inositol 3-phosphate glycosyltransferase"
FT /id="PRO_0000399824"
FT REGION 414..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 25..26
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 30..35
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 45935 MW; 2F321E8580DE4B83 CRC64;
MRLATDLETP RRVAVLSVHT SPLAQPGTGD AGGMNVYVLQ TALQLARRGV EVEVFTRATS
SADAPVVPVA PGVLVRNVVA GPFEGLDKND LPTQLCAFTA GVLRAEATHE PGYYDVVHSH
YWLSGQVGWL ARDRWAVPLV HTAHTLAAVK NAALAAGDAP EPPLRAVGEQ QVVDEADRLI
VNTEVEAQQL VSLHNADRSR IDVVHPGVDL DVFTPGSRDA ARAVFGLPTD QKIVAFVGRI
QPLKAPDILL RAAAKLPGVR VLIAGGPSGS GLAQPDTLVR LADELGISDR VTFLPPQSRE
QLVNVYRAAD LVAVPSYSES FGLVAVEAQA CGTPVVAAAV GGLPVAVADG VSGALVDGHD
IGDWADTISE VLDREPAALS RASAEHAAQF SWAHTVDALL ASYSRAMSDY RARHPRPAAR
RSGRRFSMRR GVRT
