(data stored in ACNUC7421 zone)

SWISSPROT: MSHA_SALTO

ID   MSHA_SALTO              Reviewed;         482 AA.
AC   A4X1R6;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   11-DEC-2019, entry version 74.
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=Strop_0331;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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}.
DR   EMBL; CP000667; ABP52816.1; -; Genomic_DNA.
DR   SMR; A4X1R6; -.
DR   STRING; 369723.Strop_0331; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; A4X1R6; -.
DR   EnsemblBacteria; ABP52816; ABP52816; Strop_0331.
DR   KEGG; stp:Strop_0331; -.
DR   eggNOG; ENOG4107R5M; Bacteria.
DR   eggNOG; COG0438; LUCA.
DR   HOGENOM; HOG000077288; -.
DR   KO; K15521; -.
DR   OMA; HTMAKVK; -.
DR   Proteomes; UP000000235; 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;
DR   PRODOM; A4X1R6.
DR   SWISS-2DPAGE; A4X1R6.
KW   Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..482
FT                   /note="D-inositol 3-phosphate glycosyltransferase"
FT                   /id="PRO_0000400156"
FT   REGION          69..70
FT                   /note="UDP-GlcNAc binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   REGION          74..79
FT                   /note="1D-inositol 3-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           364
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           365
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           367
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   METAL           391
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         63
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         77
FT                   /note="UDP-GlcNAc; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         132
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         165
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         189
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         209
FT                   /note="1D-inositol 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         289
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         294
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         355
FT                   /note="UDP-GlcNAc; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         377
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT   BINDING         385
FT                   /note="UDP-GlcNAc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
SQ   SEQUENCE   482 AA;  51686 MW;  A20739447F3D9733 CRC64;
     MRNYRSPIGK MTPGVEVDRE APVVRAATVA EGADVAEQHT GVGHQRGARP WPLPRRIATL
     SVHTSPLHQP GTGDAGGMNV YILEVARRLA EANVEVEIFT RATAADLPPV VEMVPGVHVR
     HIMSGPLGGL TKEELPGQLC AFTAGVLRAE AVRAAGHYDL IHSHYWLSGQ VGWLAKERWG
     VPLVHTAHTL AKVKNAQLAA GDRPEPKARV IGEEQVVAEA DRLVANTKTE AGDLIDRYDA
     DPTRVEVVEP GVDLARFCPA SGDRARAQVL ARRRLDLPER GYVVAFVGRI QPLKAPDVLI
     RAAAALRQRD PALADDMTVV VCGGPSGSGL ERPTHLIELA AALGITDRVR FLPPQTGDDL
     PALYRAADLV AVPSYNESFG LVALEAQACG TPVVAAAVGG LNTAVRDEVS GVLVDGHDPV
     AWARSLGRLL PDAGRRAMLA RGAQRHARNF SWDRTVKDLL DVYGEAVAEH RTRLSDFATC
     SR
//

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