ID A0A0G3IVU0_9MYCO Unreviewed; 431 AA.
AC A0A0G3IVU0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=D-inositol-3-phosphate glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01695};
DE EC=2.4.1.250 {ECO:0000256|HAMAP-Rule:MF_01695};
DE AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_01695};
DE Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_01695};
GN Name=mshA {ECO:0000256|HAMAP-Rule:MF_01695};
GN ORFNames=AB431_03770 {ECO:0000313|EMBL:AKK30217.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK30217.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK30217.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK30217.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
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:0000256|HAMAP-Rule:MF_01695}.
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:0000256|ARBA:ARBA00000935, ECO:0000256|HAMAP-
CC Rule:MF_01695};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01695}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC subfamily. {ECO:0000256|ARBA:ARBA00008449, ECO:0000256|HAMAP-
CC Rule:MF_01695}.
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DR EMBL; CP011773; AKK30217.1; -; Genomic_DNA.
DR RefSeq; WP_047333053.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IVU0; -.
DR STRING; 1545728.AB431_03770; -.
DR KEGG; mye:AB431_03770; -.
DR PATRIC; fig|1545728.4.peg.760; -.
DR OrthoDB; 9810929at2; -.
DR Proteomes; UP000035237; 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 CDD; cd03800; GT4_sucrose_synthase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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 NCBIfam; TIGR03449; mycothiol_MshA; 1.
DR PANTHER; PTHR45947; SULFOQUINOVOSYL TRANSFERASE SQD2; 1.
DR PANTHER; PTHR45947:SF3; SULFOQUINOVOSYL TRANSFERASE SQD2; 1.
DR Pfam; PF13579; Glyco_trans_4_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01695};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01695};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01695}.
FT DOMAIN 24..199
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 211..373
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 11
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 17..18
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 22..27
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 25
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 80
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 113
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 137
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 157
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 231
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 236
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 289
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 311
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 319
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
SQ SEQUENCE 431 AA; 45541 MW; 27234B99D75FD4DD CRC64;
MPRRVAVLSV HTSPLAQPGT GDAGGMNVYV LQTALQMARR GVEVEIFTRA TSSSDQPVVR
VAPGVLVRNV VAGPFEGLDK YDLPTQLCAF TAGVLRAEAN HEPGYYDIVH SHYWLSGQVG
WLARDRWAVP LVHTAHTLAA VKNAALADGD APEPPLRSVG EQQVVDEADR LVVNTEDEAH
QLISLHNADP RRIDVVYPGV DLETFTPGNR HAARAALGLP DGERVVAFVG RIQPLKAPDV
LLRAAARLPG VRVLVAGGPS GSGLAAPDAL VGLVAELGMA DRVTFLPPQS REQLVNVYRA
ADLVAVPSYS ESFGLVAVEA QACGTPVVAA AVGGLPVAVA DGVSGALVAG HEPGQWADAI
DGLLARDPGE LSAAAEAHAQ RFSWAHTVDG LLASYSRAIT DYASVRRRHA AGDALARRNG
RRWTMRRGVR L
//
