ID A0A0T5Y190_MYCTX Unreviewed; 477 AA.
AC A0A0T5Y190;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ECO:0000313|EMBL:CFH74018.1};
GN ORFNames=ERS053720_00960 {ECO:0000313|EMBL:CFH74018.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:CFH74018.1, ECO:0000313|Proteomes:UP000046674};
RN [1] {ECO:0000313|EMBL:CFH74018.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH74018.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CFH74018.1}.
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DR EMBL; CFSW01000005; CFH74018.1; -; Genomic_DNA.
DR Proteomes; UP000046674; Unassembled WGS sequence.
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 63..238
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 249..404
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 56..57
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 61..66
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 64
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 119
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 152
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 176
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 196
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 270
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 275
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 328
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 350
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 358
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
SQ SEQUENCE 477 AA; 50314 MW; FC6BA0A3D22B728C CRC64;
MRHDDGSGLI AQRRPVRGEG ATRSRGPSGP SNRNVSAADD PRRVALLAVH TSPLAQPGTG
DAGGMNVYML QSALHLARRG IEVEIFTRAT ASADPPVVRV APGVLVRNVV AGPFEGLDKY
DLPTQLCAFA AGVLRAEAVH EPGYYDIVHS HYWLSGQVGW LARDRWAVPL VHTAHTLAAV
KNAALADGDG PEPPLRTVGE QQVVDEADRL IVNTDDEARQ VISLHGADPA RIDVVHPGVD
LDVFRPGDRR AARAALGLPV DERVVAFVGR IQPLKAPDIV LRAAAKLPGV RIIVAGGPSG
SGLASPDGLV RLADELGISA RVTFLPPQSH TDLATLFRAA DLVAVPSYSE SFGLVAVEAQ
ACGTPVVAAA VGGLPVAVRD GITGTLVSGH EVGQWADAID HLLRLCAGPR GRVMSRAAAR
HAATFSWENT TDALLASYRR AIGEYNAERQ RRGGEVISDL VAVGKPRHWT PRRGVGA
//
