ID A0A2I2KWH5_9ACTN Unreviewed; 435 AA.
AC A0A2I2KWH5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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 ECO:0000313|EMBL:SNQ50033.1};
GN ORFNames=FRACA_40062 {ECO:0000313|EMBL:SNQ50033.1};
OS Frankia canadensis.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ50033.1, ECO:0000313|Proteomes:UP000234331};
RN [1] {ECO:0000313|EMBL:SNQ50033.1, ECO:0000313|Proteomes:UP000234331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ50033.1};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01695}.
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DR EMBL; FZMO01000334; SNQ50033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2KWH5; -.
DR OrthoDB; 9810929at2; -.
DR Proteomes; UP000234331; 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:UP000234331};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01695}.
FT DOMAIN 43..218
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 233..401
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 36..37
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 41..46
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 44
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 99
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 132
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 176
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 250
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 255
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"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 338
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 346
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01695"
SQ SEQUENCE 435 AA; 45987 MW; 32CE5675EFF9F266 CRC64;
MRLIGSGAEA GRTGPERGRR PRRVAMLSMH TSPLEQPGTG DAGGLNVYVV ELSRQLAALG
VEVEVFTRAV SSRAPTSAEL VPGVTVRHVD AGPFEEVHRE DLPAWLCAFT ADVLRAEAGQ
EPGWFDLIHS HYWLSGQVAL AVARRWGVPF VHTSHTLAKV KNDALAAGDR PEPPGRVRGE
QEVIAGATRL IASTEDEREH LGGLYGAAAD RVDVVAPGVD LDVFRPGDAA RSRALLGLDP
DGDLLLFVGR IQPLKAPDLL LHAAAELLRR DPGRRDRLTV AVVGGPSGSG LEQPDVLVKL
AADLGISDLV RFQPPAPQRD LAHWYRAATA VVVPSHSESF GLVALEAQAC GTPVVAAAVG
GLRTAVADGV SGLLVPGRDP ARYADALDQL LRQPHWRARL AAGALGRASG FGWSTTARGV
LRSYRHALSP AAVAV
//
