ID A0A1H8XPK8_9PSEU Unreviewed; 418 AA.
AC A0A1H8XPK8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04489732_108112 {ECO:0000313|EMBL:SEP41238.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP41238.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP41238.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP41238.1,
RC ECO:0000313|Proteomes:UP000198582};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOEF01000008; SEP41238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8XPK8; -.
DR STRING; 394193.SAMN04489732_108112; -.
DR OrthoDB; 9810929at2; -.
DR Proteomes; UP000198582; 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 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:UP000198582};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01695}.
FT DOMAIN 18..193
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 206..379
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 11..12
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 16..21
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 19
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 74
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 107
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 131
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 151
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 225
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
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 291
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 300
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 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 313
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 321
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
SQ SEQUENCE 418 AA; 44700 MW; CBF470D625B145AD CRC64;
MLSVHTSPLE QPGTGDAGGM NVYVSQTAQE MARRGVEVEV FTRATSSDQP PLVELAPGVT
VRHVQAGPFE PLGRDELPAQ LCAFTSGVLR AEAFHEPGYY DLIHSHYWLS GQVGWLARDR
WGVPLVHTAH TLAKVKNAAL ADGDKPEPRT RVMGEEQVVA EADCLVANTP VEARQLVEMY
GAEPHAVHAV PPGVDLERFT PGSQALSRQA LGLPQDAVVL AFAGRIQPLK APDVLLHAAA
ELLRKRPELA PRLVVLVVGG PSGTGLEQPQ ALRELAVSLG IRDQVRFLPP QPGPALVDVY
RAADLVAVPS YNESFGLVAL EAQACGTPVV AAEVGGLPVA VVHGVSGLLV PSHGAAEWAD
ALAALALRPD RRRELAANAV EHARRFSWRR TTDSLLDIYA QATRAFRNAL DLRTEVAV
//
