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Database: UniProt
Entry: A0A495XFL9_9PSEU
LinkDB: A0A495XFL9_9PSEU
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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
//
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