MSHA_STRBB
ID MSHA_STRBB Reviewed; 455 AA.
AC D7C367;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=D-inositol 3-phosphate glycosyltransferase;
DE EC=2.4.1.250 {ECO:0000255|HAMAP-Rule:MF_01695};
DE AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01695};
DE Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01695};
GN Name=mshA {ECO:0000255|HAMAP-Rule:MF_01695}; OrderedLocusNames=SBI_05009;
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=749414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1;
RX PubMed=20581206; DOI=10.1128/jb.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20489017; DOI=10.1126/science.1183605;
RA Nelson K.E., Weinstock G.M., Highlander S.K., Worley K.C., Creasy H.H.,
RA Wortman J.R., Rusch D.B., Mitreva M., Sodergren E., Chinwalla A.T.,
RA Feldgarden M., Gevers D., Haas B.J., Madupu R., Ward D.V., Birren B.W.,
RA Gibbs R.A., Methe B., Petrosino J.F., Strausberg R.L., Sutton G.G.,
RA White O.R., Wilson R.K., Durkin S., Giglio M.G., Gujja S., Howarth C.,
RA Kodira C.D., Kyrpides N., Mehta T., Muzny D.M., Pearson M., Pepin K.,
RA Pati A., Qin X., Yandava C., Zeng Q., Zhang L., Berlin A.M., Chen L.,
RA Hepburn T.A., Johnson J., McCorrison J., Miller J., Minx P., Nusbaum C.,
RA Russ C., Sykes S.M., Tomlinson C.M., Young S., Warren W.C., Badger J.,
RA Crabtree J., Markowitz V.M., Orvis J., Cree A., Ferriera S., Fulton L.L.,
RA Fulton R.S., Gillis M., Hemphill L.D., Joshi V., Kovar C., Torralba M.,
RA Wetterstrand K.A., Abouellleil A., Wollam A.M., Buhay C.J., Ding Y.,
RA Dugan S., FitzGerald M.G., Holder M., Hostetler J., Clifton S.W.,
RA Allen-Vercoe E., Earl A.M., Farmer C.N., Liolios K., Surette M.G., Xu Q.,
RA Pohl C., Wilczek-Boney K., Zhu D.;
RT "A catalog of reference genomes from the human microbiome.";
RL Science 328:994-999(2010).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01695};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002047; ADI08129.1; -; Genomic_DNA.
DR RefSeq; WP_014177596.1; NC_016582.1.
DR AlphaFoldDB; D7C367; -.
DR SMR; D7C367; -.
DR STRING; 749414.SBI_05009; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; ADI08129; ADI08129; SBI_05009.
DR KEGG; sbh:SBI_05009; -.
DR PATRIC; fig|749414.3.peg.5180; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_3_11; -.
DR OMA; HTMAKVK; -.
DR OrthoDB; 694191at2; -.
DR Proteomes; UP000000377; Chromosome.
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 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 Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR03449; mycothiol_MshA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..455
FT /note="D-inositol 3-phosphate glycosyltransferase"
FT /id="PRO_0000400161"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 51..52
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 56..61
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 59
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 114
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 147
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 171
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 191
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 266
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 271
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 354
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 362
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
SQ SEQUENCE 455 AA; 48982 MW; 35F7C0A02E619BD9 CRC64;
MSQHVSRLGG LRGRSHGHGA FGGPYHQRLR RVGRRPRRIA MLSVHTSPLH QPGTGDAGGM
NVYIVELAKR LAAIDIEVEI FTRATTGTLP PTVELAPGVL VRHVDAGPYE GLAKEDLPAQ
LCAFTHGVMG AWAGHRPGYY DLVHSHYWLS GHVGWLAAER WRVPLVHAMH TMAKVKNAAL
AEGDTPEPAA RVIGEEQIVG AADRLIANTE EEADELVRHY GADPELVAVV HPGVNLERFR
PADGRAAARA RLGLPPDALI PLFAGRIQPL KAPDILLHAV AHLLDEDPRL RERIVVPVVG
GPSGSGLAKP ERLHKLAARL GVSDVIRFRP PCTQDELADW YRAASVLVMP SYNESFGLVA
IEAQACGTPV IAAEVGGLPV AVRDGHSGIL VPGHNPADYA RELHRLSADP GLLKRLGSGA
AHHAERFGWD KAAAATADVY AEAMRGYRRL RSVHG
