ID A0A495XFL9_9PSEU Unreviewed; 417 AA.
AC A0A495XFL9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=DFJ66_5237 {ECO:0000313|EMBL:RKT71935.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT71935.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT71935.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT71935.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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:RKT71935.1}.
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DR EMBL; RBXR01000001; RKT71935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495XFL9; -.
DR OrthoDB; 9810929at2; -.
DR Proteomes; UP000272729; 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}; Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01695}.
FT DOMAIN 23..198
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 208..384
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 10
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 16..17
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 21..26
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 24
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 79
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 112
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 136
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 156
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 230
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 235
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 296
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 318
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 326
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
SQ SEQUENCE 417 AA; 44307 MW; 83B04B72A8C5CC76 CRC64;
MKRVAVLSVH TSPLEQPGTG DAGGMNVYIV QTAVRMARRG VEVEIFTRAT SSDLPPVAEL
VPGVTVRHVV AGPFEGLGKE ELPGQLCAFT AGVLRAEARQ EPGHYDVVHS HYWLSGQVGW
LARERWGVPL VHTAHTLAKV KNANLASCDA PEPRLRVIGE EQVAAEADLL VANTDVEAGE
LVKLYDADPA KVAVVPPGVD LDRFTPGDRD AARAALGLRE DAVVLAFVGR IQPLKAPDVL
VNAAAELLRR EPHLRDRLVV LVVGGPSGSG MKTPESLREL AGHLGISDVV RFLPPQGGEA
LARVYRAADV VAVPSHNESF GLVALEAQAC GTPVVAAAVG GLPVAVRDGV SGLLVAGHEP
DAWAKTLAEL VLHPAYREEL ASNAVGHARR FSWDRTTDSL LAGYARARDV FREEVFA
//